|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-757 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1062.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 19 IGLDLLVNVFGLAWNGKYFTFDNIAHWFDLaNYSFLKNPVDFLAVALIRDSILlggAVSAWASPSGFSQ-VAENVKNVVF 97
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLRDLLQGIFGL-LLPFEKGLYVLWLEGTLRLGVL---WLGALGILLNKAGgLLAAVKPLVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 98 AMMLLIVAFAPSKLLAFYE--DDNIRLAVGDWILMIWCIFASLLLQGIWTSVLAhvtevaagTGDSllfgdaeheerlrq 175
Cdd:TIGR00958 77 ALCLATPSLSSLRALAFWEalDPAVRVALGLWSWFVWSYGAALPAAALWAVLSS--------AGAS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 176 eEAEKAAEQRETFQLLFRLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSL 255
Cdd:TIGR00958 135 -EKEAEQGQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDK-GPPALASAIFFMCLLSI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 256 ASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGS 335
Cdd:TIGR00958 213 ASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 336 LIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNV 415
Cdd:TIGR00958 293 LGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 416 TLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASR 495
Cdd:TIGR00958 373 TLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 496 KVFEFIDRPPRVENTGTYAPDGMTGKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYE 575
Cdd:TIGR00958 453 KVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 576 PTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNDTTdGYNTNV 655
Cdd:TIGR00958 533 PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN-GYDTEV 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 656 GEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEaiSKNLKGKTVILIAHRLSTVENADKIVVINKG 735
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKG 689
|
730 740
....*....|....*....|..
gi 17511077 736 KVEQLGNHKTLMEQEGLYKQLV 757
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
185-763 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 555.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 185 RETFQLLFRLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLR 264
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 265 GGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSW 344
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 345 KLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKV 424
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE-ANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 425 FVVIGLIWS-NELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDR 503
Cdd:COG1132 241 ARLSALFFPlMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 504 PPRV-ENTGTYAPDGMTGKIEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVL 582
Cdd:COG1132 321 PPEIpDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 583 IDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQM 662
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEA-LPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 663 SGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGN 742
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570 580
....*....|....*....|.
gi 17511077 743 HKTLMEQEGLYKQLVQRQMMS 763
Cdd:COG1132 558 HEELLARGGLYARLYRLQFGE 578
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
191-760 |
6.14e-145 |
|
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: 438.75 E-value: 6.14e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 191 LFRLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVFgDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTY 270
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGF-SKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 271 AHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMIT 350
Cdd:TIGR02204 85 LGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 351 LINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGL 430
Cdd:TIGR02204 165 LLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 431 IWSNELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRVE-- 508
Cdd:TIGR02204 245 TAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKap 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 509 NTGTYAPDGMTGKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV 588
Cdd:TIGR02204 325 AHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 589 REYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQ 668
Cdd:TIGR02204 405 RQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFI-SALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLME 748
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
570
....*....|..
gi 17511077 749 QEGLYKQLVQRQ 760
Cdd:TIGR02204 564 KGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
174-761 |
1.01e-143 |
|
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: 440.04 E-value: 1.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 174 RQEEAEKAAEQRETFQllfRLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGML 253
Cdd:COG2274 130 PTPEFDKRGEKPFGLR---WFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQ-DLSTLWVLAIGLLLA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 254 SLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSaDCQTMSNTLS-LYMNVLTrNLTML 332
Cdd:COG2274 206 LLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTALL-DLLFV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 333 FGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTF 412
Cdd:COG2274 284 LIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 413 LNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVG 492
Cdd:COG2274 364 LAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 493 ASRKVFEFIDRPP-RVENTGTYAPDGMTGKIEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLE 571
Cdd:COG2274 444 ALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 572 HFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNDTtDGY 651
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALP-MGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 652 NTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVV 731
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
570 580 590
....*....|....*....|....*....|
gi 17511077 732 INKGKVEQLGNHKTLMEQEGLYKQLVQRQM 761
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
208-497 |
2.58e-133 |
|
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: 398.07 E-value: 2.58e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADG-SREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd18572 80 LRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLW 447
Cdd:cd18572 160 YRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17511077 448 YGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18572 240 YGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
522-760 |
1.10e-121 |
|
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: 366.09 E-value: 1.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNDTtDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPV 681
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLP-DGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQ 760
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
192-756 |
1.15e-119 |
|
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: 372.90 E-value: 1.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 192 FRLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPyytgEVVTAVFGDKASYEKLHKTVFI-MGMLSLAStvfggLRG-GSF- 268
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLA----ALLKPLLDDGFGGRDRSVLWWVpLVVIGLAV-----LRGiCSFv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 269 -TYAHA----TIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLS 343
Cdd:TIGR02203 74 sTYLLSwvsnKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 344 WKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFmTFLNVTLKIATRK 423
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRF-DAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 424 VFVVIGLiwSNELLQMGI---LTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEF 500
Cdd:TIGR02203 233 MTSAGSI--SSPITQLIAslaLAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 501 IDRPPRVEnTGTYAPDGMTGKIEFRHVAFSYPIRpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGE 580
Cdd:TIGR02203 311 LDSPPEKD-TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 581 VLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYG-LDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKG 659
Cdd:TIGR02203 389 ILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFV-DKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 660 SQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQ 739
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
570
....*....|....*..
gi 17511077 740 LGNHKTLMEQEGLYKQL 756
Cdd:TIGR02203 548 RGTHNELLARNGLYAQL 564
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
208-497 |
1.52e-113 |
|
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: 346.99 E-value: 1.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEK-SQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd18784 80 VSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLW 447
Cdd:cd18784 160 YKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17511077 448 YGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18784 240 YGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
511-737 |
3.81e-109 |
|
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: 332.90 E-value: 3.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 511 GTYAPDGMTGKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVRE 590
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 591 YDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRI 670
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFIS-ELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKV 737
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
522-756 |
3.84e-98 |
|
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: 304.54 E-value: 3.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPV 681
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIME-LPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQL 756
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
278-760 |
3.25e-97 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 314.65 E-value: 3.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 278 QIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPII 357
Cdd:PRK11176 99 TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 358 FLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNvtlKIATRKVFVVIGLIWSNELL 437
Cdd:PRK11176 179 SIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN---RMRQQGMKMVSASSISDPII 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 438 QMgI----LTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRvENTGTY 513
Cdd:PRK11176 256 QL-IaslaLAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE-KDEGKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 514 APDGMTGKIEFRHVAFSYPIRpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDH 593
Cdd:PRK11176 334 VIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 KFLHTKVALVGQEPVLYARSVTENIGYGL-DKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAI 672
Cdd:PRK11176 413 ASLRNQVALVSQNVHLFNDTIANNIAYARtEQYSREQIEEAARMAYAMDFI-NKMDNGLDTVIGENGVLLSGGQRQRIAI 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGL 752
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGV 571
|
....*...
gi 17511077 753 YKQLVQRQ 760
Cdd:PRK11176 572 YAQLHKMQ 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
193-751 |
4.17e-94 |
|
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: 305.53 E-value: 4.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 193 RLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAH 272
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 273 ATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLI 352
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 353 NIPII----------------------------FLVN-------KIFGvwydmLSEETQNSVAKAndvAEEVlsSIRTVK 397
Cdd:COG4988 167 TAPLIplfmilvgkgaakasrrqwralarlsghFLDRlrglttlKLFG-----RAKAEAERIAEA---SEDF--RKRTMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 398 --------SFACEnyessrFMTFLNVTLkIAtrkVFVVIGLIWSNELLQMGILTIVLwygghlvienkvesgllvSFLLY 469
Cdd:COG4988 237 vlrvaflsSAVLE------FFASLSIAL-VA---VYIGFRLLGGSLTLFAALFVLLL------------------APEFF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 470 QfqlgeNLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGT-YAPDGMTGKIEFRHVAFSYPirPDLPIMEDLTFTVE 548
Cdd:COG4988 289 L-----PLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTaPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 549 PGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDD 628
Cdd:COG4988 362 PGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 629 MVQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNL 708
Cdd:COG4988 442 ELEAALEAAGLDEFVA-ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA 520
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17511077 709 KGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEG 751
Cdd:COG4988 521 KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
239-760 |
1.04e-91 |
|
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: 303.20 E-value: 1.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 239 SYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLsadcQTMSNTL 318
Cdd:TIGR01846 174 GLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARV----RELEQIR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 319 SLYMN-VLTRNLTMLFgSLIF---MFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIR 394
Cdd:TIGR01846 250 NFLTGsALTVVLDLLF-VVVFlavMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 395 TVKSFACEnyesSRFMTFLNVTLKIATRKVFVVI--GLIWSN--ELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQ 470
Cdd:TIGR01846 329 TIKATATE----PQFQNRWDRQLAAYVAASFRVTnlGNIAGQaiELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLA 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 471 FQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAPDGMTGKIEFRHVAFSYpiRPDLP-IMEDLTFTVEP 549
Cdd:TIGR01846 405 GRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRY--APDSPeVLSNLNLDIKP 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 550 GEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDM 629
Cdd:TIGR01846 483 GEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEH 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 630 VQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK 709
Cdd:TIGR01846 563 VIHAAKLAGAHDFIS-ELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR 641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 17511077 710 GKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQ 760
Cdd:TIGR01846 642 GRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
190-760 |
1.34e-91 |
|
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: 300.20 E-value: 1.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 190 LLFRLLGYMGRQWKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVfGDKASYEKLHKTVFIM-----GMLSLASTVFGGLR 264
Cdd:COG5265 20 LRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAI-DALLSGAAALLVVPVGlllayGLLRLLSVLFGELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 265 GGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEIcSR------LSADcqtmsnTLSLYM--NVLTRNLTMLFGSL 336
Cdd:COG5265 99 DALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGL-SRdiergtKGIE------FLLRFLlfNILPTLLEIALVAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 337 IFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNvT 416
Cdd:COG5265 172 ILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALA-R 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 417 LKIATRKVFVviGLIWSNeLLQMGI----LTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVG 492
Cdd:COG5265 251 YERAAVKSQT--SLALLN-FGQALIialgLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 493 ASRKVFEFIDRPPRVENtgtyAPDGMT-----GKIEFRHVAFSYpiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCI 567
Cdd:COG5265 328 DMERMFDLLDQPPEVAD----APDAPPlvvggGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 568 AMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdT 647
Cdd:COG5265 402 RLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIES-L 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 648 TDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENAD 727
Cdd:COG5265 481 PDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDAD 560
|
570 580 590
....*....|....*....|....*....|....
gi 17511077 728 KIVVINKGK-VEQlGNHKTLMEQEGLYKQLVQRQ 760
Cdd:COG5265 561 EILVLEAGRiVER-GTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
520-751 |
3.01e-91 |
|
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: 286.43 E-value: 3.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYpiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTK 599
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 VALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQ 679
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMK-LPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 680 PVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEG 751
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
522-760 |
4.32e-91 |
|
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: 286.05 E-value: 4.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPV 681
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMR-FPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQ 760
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
436-759 |
6.34e-82 |
|
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: 273.18 E-value: 6.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 436 LLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAP 515
Cdd:COG4987 248 LAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 516 DGMTGKIEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKF 595
Cdd:COG4987 328 APGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRIAIARA 675
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLA-ALPDGLDTWLGEGGRRLSGGERRRLALARA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQ 755
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
....
gi 17511077 756 LVQR 759
Cdd:COG4987 566 LYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
522-760 |
2.23e-81 |
|
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: 260.88 E-value: 2.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYpiRPDLP-IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKV 600
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQP 680
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFIS-ELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 681 VVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQ 760
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
208-497 |
1.75e-78 |
|
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: 254.79 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVfGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTI-IKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLW 447
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17511077 448 YGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18557 240 YGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
522-736 |
4.36e-76 |
|
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: 243.83 E-value: 4.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIgygldkydddmvqnsaklanahtfimndttdgyntnvgekgsqMSGGQKQRIAIARALVRQPV 681
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGK 736
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
439-766 |
2.53e-75 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 256.04 E-value: 2.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 439 MGILTIVLWygghLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRV-ENTGTYAPDG 517
Cdd:PRK13657 255 LAILVLGAA----LVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVrDPPGAIDLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIRPdlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRIAIARALV 677
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIE-RKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLV 757
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
....*....
gi 17511077 758 QRQMMSGED 766
Cdd:PRK13657 568 RAQGMLQED 576
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
223-776 |
1.04e-73 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 251.17 E-value: 1.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 223 PYYTGEVVTAVFGDKASYEKLhkTVFIMGMLSLASTVFGgLR--------GGSFTYAhatidRQIRNDLFRSVVKQEIGF 294
Cdd:PRK10789 15 PKVVGIIVDGVTEQHMTTGQI--LMWIGTMVLIAVVVYL-LRyvwrvllfGASYQLA-----VELREDFYRQLSRQHPEF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 295 FDMNKTGEICSRLSADCQTMsnTLSLYMNVLT--RNLTMLFGSLIFMFT-LSWKLSMITLINIPIIFLVNKIFGvwyDML 371
Cdd:PRK10789 87 YLRHRTGDLMARATNDVDRV--VFAAGEGVLTlvDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRYG---DQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 372 SEE---TQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVT-------LKIATR---KVFVVIGLiwSNeLLQ 438
Cdd:PRK10789 162 HERfklAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkknmrvARIDARfdpTIYIAIGM--AN-LLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 439 MGiltivlwYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAPDGm 518
Cdd:PRK10789 239 IG-------GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 519 TGKIEFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHT 598
Cdd:PRK10789 311 RGELDVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQKQRIAIARALVR 678
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILR-LPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQ 758
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
570
....*....|....*...
gi 17511077 759 RQMMsgEDGLDDEIEEPE 776
Cdd:PRK10789 549 YQQL--EAALDDAPEIRE 564
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
191-783 |
2.86e-73 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 250.79 E-value: 2.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 191 LFRLLGYmGRQW-KYYGMAFFFLFCYSLSRV----FIPYYTGEVVTA-------VFGDKASYEKLHktvFIMGMLSLAST 258
Cdd:PRK10790 11 LKRLLAY-GSPWrKPLGLAVLMLWVAAAAEVsgplLISYFIDNMVAKgnlplglVAGLAAAYVGLQ---LLAAGLHYAQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 259 VFgglrggsFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNtlsLYMNVLT---RNLTMLFGS 335
Cdd:PRK10790 87 LL-------FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD---LYVTVVAtvlRSAALIGAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 336 LIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFAcenyESSRF---MTF 412
Cdd:PRK10790 157 LVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFR----QQARFgerMGE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 413 LNVTLKIATRKVFVVIGLIWsNELLQM-------GILtivLWYGghLVIENKVESGLLVSFLLYQFQLGENLRELGEVWN 485
Cdd:PRK10790 233 ASRSHYMARMQTLRLDGFLL-RPLLSLfsalilcGLL---MLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 486 GLMQAVGASRKVFEFIDRPPRventgTYAPDG---MTGKIEFRHVAFSYpiRPDLPIMEDLTFTVEPGEVVALVGPSGGG 562
Cdd:PRK10790 307 MLQQAVVAGERVFELMDGPRQ-----QYGNDDrplQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 563 KSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQ--NSAKLANah 640
Cdd:PRK10790 380 KSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQalETVQLAE-- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 641 tfIMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRL 720
Cdd:PRK10790 458 --LARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 721 STVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQMMSgedgldDEIEEPEPAREGGS 783
Cdd:PRK10790 536 STIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAG------EELAASVREEESLS 592
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
208-497 |
1.63e-72 |
|
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: 239.07 E-value: 1.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAV-----FGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRND 282
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVtnhsgSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 283 LFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNK 362
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 363 IFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGIL 442
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 443 TIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
227-732 |
7.63e-72 |
|
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: 7.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 227 GEVVTAVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSR 306
Cdd:TIGR02857 27 ARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 307 LSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVA 386
Cdd:TIGR02857 107 ALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 387 EEVLSSIRTVKSFACENYES-----------SRFMTflnvTLKIATRKVFVVigliwsnELL-QMGILTIVLWYGGHLVI 454
Cdd:TIGR02857 187 LDRLRGLPTLKLFGRAKAQAaairrsseeyrERTMR----VLRIAFLSSAVL-------ELFaTLSVALVAVYIGFRLLA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 455 EN-KVESGLLVSFLLYQFQLgeNLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAPDGMTGKIEFRHVAFSYPI 533
Cdd:TIGR02857 256 GDlDLATGLFVLLLAPEFYL--PLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPdlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARS 613
Cdd:TIGR02857 334 RR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 614 VTENIGYGLDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:TIGR02857 412 IAENIRLARPDASDAEIREALERAGLDEFV-AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 17511077 694 AESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVI 732
Cdd:TIGR02857 491 AETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
208-497 |
9.87e-71 |
|
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: 234.15 E-value: 9.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTaVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVID-ILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd18590 80 VQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLW 447
Cdd:cd18590 160 HQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17511077 448 YGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
520-737 |
1.95e-63 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 212.06 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYPIRPdLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTK 599
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 VALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFiMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQ 679
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDF-VNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 680 PVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKV 737
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
294-757 |
2.95e-63 |
|
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: 225.77 E-value: 2.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 294 FFDMNKTGEICSRLSaDCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSE 373
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNH 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 374 ETQNSVAKANDVAEEVLSSIRTVKSFACENYE----SSRFMTFLNVTLKIAtrKVFVVIGLIWSneLLQMGILTIVLWYG 449
Cdd:TIGR01193 325 DAMQANAVLNSSIIEDLNGIETIKSLTSEAERyskiDSEFGDYLNKSFKYQ--KADQGQQAIKA--VTKLILNVVILWTG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 450 GHLVIENKVESGLLVSF-LLYQFQLG--ENLRELGEvwnGLMQAVGASRKVFEFIDRPPRVENTGTY-APDGMTGKIEFR 525
Cdd:TIGR01193 401 AYLVMRGKLTLGQLITFnALLSYFLTplENIINLQP---KLQAARVANNRLNEVYLVDSEFINKKKRtELNNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 526 HVAFSYPIRPdlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQ 605
Cdd:TIGR01193 478 DVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 606 EPVLYARSVTENIGYGL-DKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLL 684
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIEN-MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 685 LDEATSALDAESEHTVQEAISkNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLV 757
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
221-761 |
1.18e-59 |
|
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: 215.21 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 221 FIPYYTGEVVTAVFGDkASYEKLHKTVFIMGMLSLASTVFGGLRG---------GSFTYAHATIDRqirndLFRSVVkqe 291
Cdd:TIGR03797 154 LVPIATGILIGTAIPD-ADRSLLVQIALALLAAAVGAAAFQLAQSlavlrletrMDASLQAAVWDR-----LLRLPV--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 292 iGFFDMNKTGEICSRLSADCQtMSNTLSlyMNVLTRNLTMLFG--SLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYD 369
Cdd:TIGR03797 225 -SFFRQYSTGDLASRAMGISQ-IRRILS--GSTLTTLLSGIFAllNLGLMFYYSWKLALVAVALALVAIAVTLVLGLLQV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 370 MLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYG 449
Cdd:TIGR03797 301 RKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 450 GHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTyAPDGMTGKIEFRHVAF 529
Cdd:TIGR03797 381 ISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKT-DPGKLSGAIEVDRVTF 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 530 SYpiRPDLP-IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPV 608
Cdd:TIGR03797 460 RY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGR 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 LYARSVTENIGyGLDKYDDDMVQNSAKLANahtfIMNDTTD---GYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:TIGR03797 538 LMSGSIFENIA-GGAPLTLDEAWEAARMAG----LAEDIRAmpmGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLF 612
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 686 DEATSALDAESEHTVQEAISKnLKGkTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQM 761
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLER-LKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
442-778 |
1.89e-59 |
|
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: 212.44 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 442 LTIVLWYGGHLVIENKVESGLLVSFLLY-QFQLGEnlreLGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAP----D 516
Cdd:TIGR01192 254 MMCILVIGTVLVIKGELSVGEVIAFIGFaNLLIGR----LDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADapelP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 517 GMTGKIEFRHVAFSYPIRPDLpiMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFL 596
Cdd:TIGR01192 330 NVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMnDTTDGYNTNVGEKGSQMSGGQKQRIAIARAL 676
Cdd:TIGR01192 408 RKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFIL-KRSNGYDTLVGERGNRLSGGERQRLAIARAI 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 677 VRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQL 756
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
330 340
....*....|....*....|..
gi 17511077 757 VQRQMMSgedgLDDEIEEPEPA 778
Cdd:TIGR01192 567 LRRSGLL----TNQPATKPLRK 584
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
520-742 |
1.82e-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: 198.49 E-value: 1.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYpiRPDL-PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHT 598
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEPVLYARSVTENIGyGLDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVR 678
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFV-ESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGN 742
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
175-733 |
1.99e-56 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 211.04 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 175 QEEAEKAAEQRETFQLLfrllgymgRQWKYYGMAFFFLF----------------CYSLSRVFIPYYTgEVVTAVFGDKA 238
Cdd:PTZ00265 21 KDEVEKELNKKGTFELY--------KKIKTQKIPFFLPFkclpashrkllgvsfvCATISGGTLPFFV-SVFGVIMKNMN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 239 SYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTL 318
Cdd:PTZ00265 92 LGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 319 -SLYMNVLTRNLTMLfGSLIFMFTLSWKLSMITLINIPIIFL----------VNKIFGVWYDmlseetQNSVAkandVAE 387
Cdd:PTZ00265 172 gTKFITIFTYASAFL-GLYIWSLFKNARLTLCITCVFPLIYIcgvicnkkvkINKKTSLLYN------NNTMS----IIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 388 EVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVV---IGLIwsNELLqMGILTIVLWYGGHLVIE--------N 456
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMEslhIGMI--NGFI-LASYAFGFWYGTRIIISdlsnqqpnN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 457 KVESGLLVSFLL----YQFQLGENLRELGEvwngLMQAVGASRKVFEFIDRPPRVENT--GTYAPDgmTGKIEFRHVAFS 530
Cdd:PTZ00265 318 DFHGGSVISILLgvliSMFMLTIILPNITE----YMKSLEATNSLYEIINRKPLVENNddGKKLKD--IKKIQFKNVRFH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 531 YPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLI-DGVPVREYDHKFLHTKVALVGQEPVL 609
Cdd:PTZ00265 392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 YARSVTENIGYGL------------------DKYDDDMVQNS--AKLANAHTFIMNDTT--------------------- 648
Cdd:PTZ00265 472 FSNSIKNNIKYSLyslkdlealsnyynedgnDSQENKNKRNScrAKCAGDLNDMSNTTDsneliemrknyqtikdsevvd 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 649 ---------------DGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISkNLKG--- 710
Cdd:PTZ00265 552 vskkvlihdfvsalpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN-NLKGnen 630
|
650 660
....*....|....*....|...
gi 17511077 711 KTVILIAHRLSTVENADKIVVIN 733
Cdd:PTZ00265 631 RITIIIAHRLSTIRYANTIFVLS 653
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
216-497 |
7.82e-56 |
|
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: 193.84 E-value: 7.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 216 SLSRVFIPYYTGEVVTAVFGDKASyEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFF 295
Cdd:cd18589 9 SLGEMAIPYYTGRMTDWIMNKDAP-EAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 296 DMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEET 375
Cdd:cd18589 88 DSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 376 QNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIE 455
Cdd:cd18589 168 QKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17511077 456 NKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18589 248 GTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
436-741 |
7.89e-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: 201.52 E-value: 7.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 436 LLQMGILTIvlwyGGHLVIENKVESGLLV--SFLLyqfqlGenlRELG------EVWNGLMQAVGASRKVFEFI-DRPPR 506
Cdd:COG4618 251 LLQSAVLGL----GAYLVIQGEITPGAMIaaSILM-----G---RALApieqaiGGWKQFVSARQAYRRLNELLaAVPAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 507 VENTGTYAPdgmTGKIEFRHVAFSYPIRpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGV 586
Cdd:COG4618 319 PERMPLPRP---KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 587 PVREYDHKFLHTKVALVGQEPVLYARSVTENIGyGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQ 666
Cdd:COG4618 395 DLSQWDREELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILR-LPDGYDTRIGEGGARLSGGQ 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 667 KQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
208-497 |
1.48e-54 |
|
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: 190.42 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASYEKLHKT--VFIMGMLSL----ASTVFGglRGGSFTYAHATIDRQIRN 281
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSlkTFALALLGVfvvgAAANFG--RVYLLRIAGERIVARLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 282 DLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVN 361
Cdd:cd18573 79 RLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 362 KIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGI 441
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 442 LTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18573 239 LLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
275-758 |
3.41e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 204.11 E-value: 3.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 275 IDRQIRNDLFRSVVKQEIGFFDMNKT--GEICSRLSADCQTMSNTLSlymnvltrNLTMLFGSLIFMFTLSWKLS----- 347
Cdd:PTZ00265 897 VEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLV--------NNIVIFTHFIVLFLVSMVMSfyfcp 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 348 MITLINIPIIFLVNKIFGVWYDMLS-------EETQNSVAKA--ND---------VAEEVLSSIRTVKSFACENYESSRF 409
Cdd:PTZ00265 969 IVAAVLTGTYFIFMRVFAIRARLTAnkdvekkEINQPGTVFAynSDdeifkdpsfLIQEAFYNMNTVIIYGLEDYFCNLI 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 410 MTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIENKVE-SGLLVSFLLYQFQlgenlrelGEVWNGLM 488
Cdd:PTZ00265 1049 EKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILvDDFMKSLFTFLFT--------GSYAGKLM 1120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 489 QAVGASR-------KVFEFIDRPPRVE---NTGTYAPDG--MTGKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALV 556
Cdd:PTZ00265 1121 SLKGDSEnaklsfeKYYPLIIRKSNIDvrdNGGIRIKNKndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 557 GPSGGGKSSCIAMLEHFYE------------------------------------------------------PTSGEVL 582
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 583 IDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQM 662
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFI-ESLPNKYDTNVGPYGKSL 1359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 663 SGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTVENADKIVVINKGK---- 736
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgs 1439
|
570 580
....*....|....*....|....
gi 17511077 737 -VEQLGNHKTLME-QEGLYKQLVQ 758
Cdd:PTZ00265 1440 fVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
460-760 |
8.35e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.60 E-value: 8.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 460 SGLLVSFL---LYQfqlgeNLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAPDGMTG-KIEFRH-VAFSYPir 534
Cdd:PRK11174 289 AGFFVLILapeFYQ-----PLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPvTIEAEDlEILSPD-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 535 pDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYePTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSV 614
Cdd:PRK11174 362 -GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGLDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDA 694
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFL-PLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 695 ESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVQRQ 760
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
442-760 |
1.56e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 195.43 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 442 LTIVLWYGGHLViENKVESG----LLVSFLLYQFqlgENLRELGEVWNGLMQAVGASRKVFEFIDRPPRVENTGTYAPDG 517
Cdd:PRK11160 259 VVLMLWLAAGGV-GGNAQPGaliaLFVFAALAAF---EALMPVAGAFQHLGQVIASARRINEITEQKPEVTFPTTSTAAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNS------AKLAnahtfimnDTTDGYNTNVGEKGSQMSGGQKQRIA 671
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVlqqvglEKLL--------EDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 672 IARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEG 751
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
....*....
gi 17511077 752 LYKQLVQRQ 760
Cdd:PRK11160 566 RYYQLKQRL 574
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
206-473 |
1.26e-52 |
|
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: 184.38 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 206 GMAFFFLFCYSLSRVFIPYYTGeVVTAVFGDKASYEKLHKTVFIMGMLSL--ASTVFGGLRGGSFTYAHATIDRQIRNDL 283
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLG-RILDVLLPDGDPETQALNVYSLALLLLglAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 284 FRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKI 363
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 364 FGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILT 443
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|
gi 17511077 444 IVLWYGGHLVIENKVESGLLVSFLLYQFQL 473
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
208-497 |
6.68e-52 |
|
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: 182.68 E-value: 6.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGG-DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIAtRKVFVVIGLIWS-NELLQMGILTIVL 446
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLA-LKRARIRALFSSfIIFLLFGAIVAVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17511077 447 WYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18576 239 WYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
208-494 |
1.67e-51 |
|
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: 181.91 E-value: 1.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGdKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFA-AGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd18575 80 LRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKV-------FVVIGLIwsnellqMG 440
Cdd:cd18575 160 VRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIraralltALVIFLV-------FG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 441 ILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGAS 494
Cdd:cd18575 233 AIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
436-741 |
1.54e-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: 186.40 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 436 LLQMGILTIvlwyGGHLVIENKVESGLLV--SFLLYqfqlgenlRELG------EVWNGLMQAVGASRKVFEFIDR-PPR 506
Cdd:TIGR01842 237 VLQSLVLGL----GAYLAIDGEITPGMMIagSILVG--------RALApidgaiGGWKQFSGARQAYKRLNELLANyPSR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 507 VENTGTYAPDGmtgKIEFRHVAFSYPIrPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGV 586
Cdd:TIGR01842 305 DPAMPLPEPEG---HLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 587 PVREYDHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQ 666
Cdd:TIGR01842 381 DLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILR-LPDGYDTVIGPGGATLSGGQ 459
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 667 KQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAI-SKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
208-497 |
8.73e-50 |
|
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: 176.97 E-value: 8.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAG-DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 VKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVW 367
Cdd:cd07346 83 QRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 368 YDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFL--NVTLKIATRKVFVVIGLIWsnELLQMGILTIV 445
Cdd:cd07346 163 IRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANrdLRDANLRAARLSALFSPLI--GLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17511077 446 LWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
519-741 |
1.13e-46 |
|
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: 165.28 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 519 TGKIEFRHVAFSYpiRPDLP-IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:cd03369 4 HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVLYARSVTENIGYgLDKYDDDMVQNSAKlanahtfimndttdgyntnVGEKGSQMSGGQKQRIAIARALV 677
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALR-------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
522-737 |
1.74e-46 |
|
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: 163.54 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIgygldkydddmvqnsaklanahtfimndttdgyntnvgekgsqMSGGQKQRIAIARALVRQPV 681
Cdd:cd03246 80 YLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 682 VLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVENADKIVVINKGKV 737
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAI-AALKaaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
436-720 |
2.28e-45 |
|
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: 171.00 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 436 LLQMGILTI-VLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEFIDRPPRV-----EN 509
Cdd:TIGR02868 245 LLAAGLAVLgALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVaegsaPA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 510 TGTYAPDGMTgkIEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVR 589
Cdd:TIGR02868 325 AGAVGLGKPT--LELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 590 EYDHKFLHTKVALVGQEPVLYARSVTENIGYGL-DKYDDDM--VQNSAKLANahtfIMNDTTDGYNTNVGEKGSQMSGGQ 666
Cdd:TIGR02868 401 SLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELwaALERVGLAD----WLRALPDGLDTVLGEGGARLSGGE 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 667 KQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRL 720
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
522-748 |
3.82e-45 |
|
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: 161.73 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPV--LYARSVTENIGYG-----LDKYD-DDMVQNSAK------LANAHTFimndttdgyntnvgekgsQMSGGQK 667
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlgLPREEiRERVEEALElvglehLADRPPH------------------ELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 668 QRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTV-ENADKIVVINKGKV-------E 738
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIvadgtprE 220
|
250
....*....|
gi 17511077 739 QLGNHKTLME 748
Cdd:COG1122 221 VFSDYELLEE 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
522-737 |
1.09e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.98 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDLpimEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:COG4619 1 LELEGLSFRVGGKPIL---SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENI----GYGLDKYDDDMVQNSAKLANAHTFIMNDTTDgyntnvgekgsQMSGGQKQRIAIARALV 677
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVE-----------RLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAISKNL--KGKTVILIAH------RLstvenADKIVVINKGKV 737
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
277-753 |
1.57e-44 |
|
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: 174.36 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 277 RQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFtLSWKLSMITLINIPI 356
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVIL-LATPIAAVIIPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 357 I-FLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFAcenyESSRFMTFLNVTLKIATRKVFVVIgliWSNE 435
Cdd:TIGR00957 1117 LyFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE----EQERFIHQSDLKVDENQKAYYPSI---VANR 1189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 436 LLQMGIL----TIVLWYGGHLVI-ENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKVFEF----IDRPPR 506
Cdd:TIGR00957 1190 WLAVRLEcvgnCIVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYseteKEAPWQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 507 VEntGTYAPDGM--TGKIEFRHVAFSYpiRPDLP-IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLI 583
Cdd:TIGR00957 1270 IQ--ETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 584 DGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGyGLDKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMS 663
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFV-SALPDKLDHECAEGGENLS 1423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNH 743
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAP 1503
|
490
....*....|
gi 17511077 744 KTLMEQEGLY 753
Cdd:TIGR00957 1504 SNLLQQRGIF 1513
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
206-461 |
2.78e-44 |
|
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: 161.87 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 206 GMAFFFLFCYSLSRVFIPYYTGEVVTAVFgdkasYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFR 285
Cdd:cd18577 14 ALPLMTIVFGDLFDAFTDFGSGESSPDEF-----LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 286 SVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFG 365
Cdd:cd18577 89 ALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 366 VWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVV---IGLIWsneLLQMGIL 442
Cdd:cd18577 169 KLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSglgLGLLF---FIIFAMY 245
|
250
....*....|....*....
gi 17511077 443 TIVLWYGGHLVIENKVESG 461
Cdd:cd18577 246 ALAFWYGSRLVRDGEISPG 264
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
522-760 |
3.35e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 3.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREyDHKFLHTKVA 601
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIG-----YGLDKYDDDmvQNSAKLANAhtFIMNDTTDgyntnvgEKGSQMSGGQKQRIAIARA 675
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEAR--ERIDELLEL--FGLTDAAD-------RKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQ--E 750
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELL-RELAaeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARllE 224
|
250
....*....|
gi 17511077 751 GLYKQLVQRQ 760
Cdd:COG1131 225 DVFLELTGEE 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
522-741 |
4.92e-44 |
|
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: 158.07 E-value: 4.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDG-----VPVREydhkfl 596
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgVPPER------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 hTKVALVGQEPVLYA-RSVTENIGYGLD--KYDDDMVQNSAKLANAHTFIMNDttdgyntnVGEKGSQMSGGQKQRIAIA 673
Cdd:cd03259 72 -RNIGMVFQDYALFPhLTVAENIAFGLKlrGVPKAEIRARVRELLELVGLEGL--------LNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLS-TVENADKIVVINKGKVEQLG 741
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
205-497 |
5.32e-44 |
|
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: 160.67 E-value: 5.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 205 YGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKAsYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLF 284
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGL-RELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 285 RSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIF 364
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 365 GVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKVFVVIGLIWS-NELLQMGILT 443
Cdd:cd18542 160 FKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDK-ENEEYRDLNIKLAKLLAKYWPlMDFLSGLQIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 444 IVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18542 239 LVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
205-497 |
1.06e-43 |
|
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: 159.90 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 205 YGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASyeklhKTVFIMGMLSLASTVFGGLrggsFTYAHA--------TID 276
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDL-----EALLLVPLAIIGLFLLRGL----ASYLQTylmayvgqRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 277 RQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPI 356
Cdd:cd18552 72 RDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 357 IFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNEL 436
Cdd:cd18552 152 AALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 437 LQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18552 232 LGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
522-734 |
1.23e-43 |
|
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: 157.25 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYP-IRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREydhkfLHTKV 600
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEPVLYA-RSVTENIGYGLdkyddDMVQNSAKLANAHtfimndtTDGYNTNVGEKG------SQMSGGQKQRIAIA 673
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----ELQGVPKAEARER-------AEELLELVGLSGfenaypHQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLS-TVENADKIVVINK 734
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
518-731 |
1.97e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.94 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTG---KIEFRHVAFSYPIRP-DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVRE 590
Cdd:COG1116 1 MSAaapALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrLIAGLE---KPTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 591 ydhkfLHTKVALVGQEPVLYA-RSVTENIGYGLdkyddDMVQNSAKLANAHtfimndtTDGYNTNVGEKG------SQMS 663
Cdd:COG1116 78 -----PGPDRGVVFQEPALLPwLTVLDNVALGL-----ELRGVPKAERRER-------ARELLELVGLAGfedaypHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAH------RLstvenADKIVV 731
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVV 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
485-739 |
2.22e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 165.08 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 485 NGLMQAVGASRKVFEFIDR----PPRVENTGTYAPDGMTGK--IEFRHVAFSYPIRP--DLPIMEDLTFTVEPGEVVALV 556
Cdd:COG1123 218 DGRIVEDGPPEEILAAPQAlaavPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 557 GPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDH---KFLHTKVALVGQEPvlYA-----RSVTENIGYGLDKYDD- 627
Cdd:COG1123 298 GESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDP--YSslnprMTVGDIIAEPLRLHGLl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 628 -------------DMVQNSAKLANAHTFimndttdgyntnvgekgsQMSGGQKQRIAIARALVRQPVVLLLDEATSALDA 694
Cdd:COG1123 376 sraerrervaellERVGLPPDLADRYPH------------------ELSGGQRQRVAIARALALEPKLLILDEPTSALDV 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17511077 695 esehTVQEAISKNLK------GKTVILIAHRLSTVEN-ADKIVVINKGK-VEQ 739
Cdd:COG1123 438 ----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRiVED 486
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
522-751 |
2.84e-43 |
|
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: 156.94 E-value: 2.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLhTKVA 601
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIGYGLDKYDDDMVQNSAKLAN-AHTFIMNDTTDgynTNVGEkgsqMSGGQKQRIAIARALVRQ 679
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEElIELLGLEEFLD---RRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 680 PVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQEG 751
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREIL-RALKkeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
195-507 |
9.54e-43 |
|
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: 158.00 E-value: 9.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 195 LGYMGRQWKYYGMAFFF---------LFCYSLSRVFipyytgevvtAVFGDKASYEKLHKTVFIMGM---LSLASTVFGG 262
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGaiiagavfpVFAILFSKLI----------SVFSLPDDDELRSEANFWALMflvLAIVAGIAYF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 263 LRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDM--NKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMF 340
Cdd:cd18578 71 LQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDpeNSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 341 TLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIA 420
Cdd:cd18578 151 VYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 421 TRKVFVViGLIWS-NELLQMGILTIVLWYGGHLVIENKVESG--LLVSFLLYQ--FQLGENLRELGEVwnglMQAVGASR 495
Cdd:cd18578 231 LRRALIS-GLGFGlSQSLTFFAYALAFWYGGRLVANGEYTFEqfFIVFMALIFgaQSAGQAFSFAPDI----AKAKAAAA 305
|
330
....*....|..
gi 17511077 496 KVFEFIDRPPRV 507
Cdd:cd18578 306 RIFRLLDRKPEI 317
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
522-741 |
1.62e-42 |
|
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: 152.47 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDhKFLHTKVA 601
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIGygldkydddmvqnsaklanahtfimndttdgyntnvgekgSQMSGGQKQRIAIARALVRQPV 681
Cdd:cd03247 79 VLNQRPYLFDTTLRNNLG----------------------------------------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
183-751 |
2.27e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 167.46 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 183 EQRET----FQLLFRLLGYMGRQWkyygMAFFFLFCYSLSRVFipYYTGEVVTAVFGDKASYEKLHKTVFIM--GMLSLA 256
Cdd:PLN03232 889 EERETgiisWNVLMRYNKAVGGLW----VVMILLVCYLTTEVL--RVSSSTWLSIWTDQSTPKSYSPGFYIVvyALLGFG 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 257 STVFgglrggSFTYAHATID------RQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADC----QTMSNTLSLYMNVLT 326
Cdd:PLN03232 963 QVAV------TFTNSFWLISsslhaaKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgdidRNVANLMNMFMNQLW 1036
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 327 RnltmlfgsLIFMFTLSWKLSMITLINI-PIIFLVNKIFgVWYDMLSEETQ--NSVAKANDVAE-----EVLSSIRTVKS 398
Cdd:PLN03232 1037 Q--------LLSTFALIGTVSTISLWAImPLLILFYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgealNGLSSIRAYKA 1107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 399 -----------------FACENYESSRFMTFLNVTLKiatrkvFVVIGLIWSNELLQMGiltivlwygghlVIENKV--- 458
Cdd:PLN03232 1108 ydrmakingksmdnnirFTLANTSSNRWLTIRLETLG------GVMIWLTATFAVLRNG------------NAENQAgfa 1169
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 459 -ESGLLVSFLLYQFQLGEN-LRELGEVWNGLmqavGASRKVFEFIDRPPR----VENTGTYAPDGMTGKIEFRHVAFSYp 532
Cdd:PLN03232 1170 sTMGLLLSYTLNITTLLSGvLRQASKAENSL----NSVERVGNYIDLPSEataiIENNRPVSGWPSRGSIKFEDVHLRY- 1244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 533 iRPDLP-IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYA 611
Cdd:PLN03232 1245 -RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RSVTENIGYGLDKYDDDMVQnsaKLANAHTF-IMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDADLWE---ALERAHIKdVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 691 ALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEG 751
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
523-736 |
4.29e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 152.62 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 523 EFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVAL 602
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VGQEP--VLYARSVTENIGYGL-----DKYDDDMVQNSA-------KLANAHTFimndttdgyntnvgekgsQMSGGQKQ 668
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLenlglPEEEIEERVEEAlelvgleGLRDRSPF------------------TLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGK 736
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
205-473 |
1.45e-41 |
|
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: 153.72 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 205 YGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLF 284
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 285 RSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIF 364
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 365 GVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKVFVVIGLIWSNELLQMGILT- 443
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDK-LNEEYVEKNLRLARVDALFFPLIGLLIGLSFl 239
|
250 260 270
....*....|....*....|....*....|
gi 17511077 444 IVLWYGGHLVIENKVESGLLVSFLLYQFQL 473
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAFNSYLGML 269
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
522-741 |
9.21e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 153.33 E-value: 9.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV-------REydhk 594
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 595 flhtkVALVGQEpvlYA----RSVTENIGYGL--DKYDD-----------DMVQnsakLAN-AHTFImndttdgyntnvg 656
Cdd:COG3842 79 -----VGMVFQD---YAlfphLTVAENVAFGLrmRGVPKaeirarvaellELVG----LEGlADRYP------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 657 ekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLS---TVenADKIVV 731
Cdd:COG3842 134 ---HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAV 208
|
250
....*....|
gi 17511077 732 INKGKVEQLG 741
Cdd:COG3842 209 MNDGRIEQVG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
522-736 |
1.48e-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: 146.95 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYD--HKFL 596
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTllrCIAGLE---EPDSGSILIDGEDLTDLEdeLPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYAR-SVTENIGYGLdkydddmvqnsaklanahtfimndttdgyntnvgekgsqmSGGQKQRIAIARA 675
Cdd:cd03229 75 RRRIGMVFQDFALFPHlTVLENIALGL----------------------------------------SGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGK 736
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
522-737 |
1.51e-40 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 146.77 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHtKVA 601
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIgygldkydddmvqnsaklanahtfimndttdgyntnvgekgsQMSGGQKQRIAIARALVRQP 680
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 681 VVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
522-736 |
2.07e-40 |
|
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: 147.62 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDL--PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAML--EhfYEPTSGEVlidgvpvreydhkFLH 597
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVLYARSVTENIGYGLdKYDDDMVQNSAK-------LAnahtfIMndtTDGYNTNVGEKGSQMSGGQKQRI 670
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGK-PFDEERYEKVIKacalepdLE-----IL---PDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAE-SEHTVQEAISKNLK-GKTVILIAHRLSTVENADKIVVINKGK 736
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
523-736 |
2.92e-40 |
|
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: 145.47 E-value: 2.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 523 EFRHVAFSYPIRPDLpimEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVAL 602
Cdd:cd00267 1 EIENLSFRYGGRTAL---DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VgqepvlyarsvtenigygldkydddmvqnsaklanahtfimndttdgyntnvgekgSQMSGGQKQRIAIARALVRQPVV 682
Cdd:cd00267 78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 683 LLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVENA-DKIVVINKGK 736
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
541-690 |
6.19e-40 |
|
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: 144.33 E-value: 6.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 541 EDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYAR-SVTENIG 619
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 620 YGLDKYDDDMVQNSAKLANAHTFImnDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
520-741 |
8.39e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.61 E-value: 8.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDG-----VPVREY 591
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIGGrdvtdLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 592 DhkflhtkVALVGQEPVLY-ARSVTENIGYGL-----DKYD-DDMVQNSAKLanahtfimndttdgynTNVGE----KGS 660
Cdd:COG3839 76 N-------IAMVFQSYALYpHMTVYENIAFPLklrkvPKAEiDRRVREAAEL----------------LGLEDlldrKPK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAES-EHTVQE--AISKNLkGKTVILIAH------RLstvenADKIVV 731
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAEikRLHRRL-GTTTIYVTHdqveamTL-----ADRIAV 206
|
250
....*....|
gi 17511077 732 INKGKVEQLG 741
Cdd:COG3839 207 MNDGRIQQVG 216
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
222-468 |
3.04e-39 |
|
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: 147.31 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 222 IPYYTGEVVTAVfgdkASYEKLHKTVFIMGMLSLASTVFG--GLRGGsFTYAHAT--------IDRQIRNDLFRSVVKQE 291
Cdd:cd18574 15 IPLLLGDLVNVI----SRSLKETNGDFIEDLKKPALKLLGlyLLQSL-LTFAYISllsvvgerVAARLRNDLFSSLLRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 292 IGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDML 371
Cdd:cd18574 90 IAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 372 SEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATrKVFVVIGLI--WSNELLQmGILTIVLWYG 449
Cdd:cd18574 170 SRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNE-KLGLGIGIFqgLSNLALN-GIVLGVLYYG 247
|
250
....*....|....*....
gi 17511077 450 GHLVIENKVESGLLVSFLL 468
Cdd:cd18574 248 GSLVSRGELTAGDLMSFLV 266
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
522-737 |
4.87e-39 |
|
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: 144.17 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPD-LPIMEDLTFTVEPGEVVALVGPSGGGKS---SCIAMLEHfyePTSGEVLIDGVPVREYDHK--- 594
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVRVDGTDISKLSEKela 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 595 -FLHTKVALVGQE----PVLyarSVTENIGYGLdkydddMVQNSAK---LANAHTFImndttdgynTNVG------EKGS 660
Cdd:cd03255 78 aFRRRHIGFVFQSfnllPDL---TALENVELPL------LLAGVPKkerRERAEELL---------ERVGlgdrlnHYPS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVENADKIVVINKGKV 737
Cdd:cd03255 140 ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
522-747 |
6.41e-39 |
|
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: 144.75 E-value: 6.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPdlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYA-RSVTENIGY--GLDKYDDDMVQNSAK--LAnahtfIMNDTTDGYntnVGEKGSQMSGGQKQRIAIARAL 676
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIALvpKLLKWPKEKIRERADelLA-----LVGLDPAEF---ADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 677 VRQPVVLLLDEATSALDAESEHTVQEAIsKNLK---GKTVILIAH------RLstvenADKIVVINKGKVEQLGNHKTLM 747
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEF-KRLQqelGKTIVFVTHdideafRL-----ADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
522-741 |
6.70e-39 |
|
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: 144.25 E-value: 6.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHFY--EPTSGEVLIDGVPVREYDHKFL 596
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIpgAPDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 H--TKVALVGQEPVLYARSVTENIGYGL-------DKYDDDMVQNSAKLANAHTFIMNDTtdgyntnvgeKGSQMSGGQK 667
Cdd:cd03260 78 ElrRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklKEELDERVEEALRKAALWDEVKDRL----------HALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 668 QRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLKGK-TVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELI-AELKKEyTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
522-741 |
9.62e-39 |
|
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: 143.88 E-value: 9.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRP-DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLE---RPTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 T---KVALVGQE-PVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFI-MNDTTDGYNtnvgekgSQMSGGQKQRIAI 672
Cdd:cd03258 79 KarrRIGMIFQHfNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVgLEDKADAYP-------AQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLK-GKTVILIAHRLSTV-ENADKIVVINKGKVEQLG 741
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDiNRElGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEG 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
183-758 |
1.11e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 152.58 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 183 EQRET----FQLLFRLLGYMGRQWkyygMAFFFLFCYSLSRVF-------IPYYTgevvtavfgdKASYEKLHKTVFIMG 251
Cdd:PLN03130 892 EERETgvvsWKVLERYKNALGGAW----VVMILFLCYVLTEVFrvssstwLSEWT----------DQGTPKTHGPLFYNL 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 252 MLSLAStvFGGLR---GGSFTYAHATID--RQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLt 326
Cdd:PLN03130 958 IYALLS--FGQVLvtlLNSYWLIMSSLYaaKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMF- 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 327 rnLTMLFgSLIFMFTLSWKLSMITLINI-PIIFLVNKIFgVWYDMLSEE-------TQNSVAKANDVAEEVLSSIRTVKS 398
Cdd:PLN03130 1035 --LGQIF-QLLSTFVLIGIVSTISLWAImPLLVLFYGAY-LYYQSTAREvkrldsiTRSPVYAQFGEALNGLSTIRAYKA 1110
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 399 F---ACENYES----SRFmTFLNVTLK--IATRKVFVVIGLIWsnellqmgiLTIVLWYGGHLVIENKV----ESGLLVS 465
Cdd:PLN03130 1111 YdrmAEINGRSmdnnIRF-TLVNMSSNrwLAIRLETLGGLMIW---------LTASFAVMQNGRAENQAafasTMGLLLS 1180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 466 FLLYQFQLGENLRELGEVWNGLMQAVgasRKVFEFID----RPPRVENTgtYAPDG--MTGKIEFRHVAFSYpiRPDLP- 538
Cdd:PLN03130 1181 YALNITSLLTAVLRLASLAENSLNAV---ERVGTYIDlpseAPLVIENN--RPPPGwpSSGSIKFEDVVLRY--RPELPp 1253
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENi 618
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN- 1332
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 619 gygLDKYDDdmvQNSA----KLANAHtfiMNDT----TDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:PLN03130 1333 ---LDPFNE---HNDAdlweSLERAH---LKDVirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 691 ALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEG-LYKQLVQ 758
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGsAFSKMVQ 1472
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
522-737 |
1.54e-37 |
|
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: 140.95 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:COG1120 2 LEAENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEP-----------VLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNDTTdgyntnvgekgsQMSGGQKQRI 670
Cdd:COG1120 79 YVPQEPpapfgltvrelVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVD------------ELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLstveN-----ADKIVVINKGKV 737
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDL----NlaaryADRLVLLKDGRI 216
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
221-497 |
3.73e-37 |
|
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: 141.03 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 221 FIPYYTGEVVTAVFGDKASYeklhKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKT 300
Cdd:cd18551 17 AQPLLVKNLIDALSAGGSSG----GLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 301 GEICSRLSADCQTMSNTLS-LYMNVLTrNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLV-----NKIFGVwydmlSEE 374
Cdd:cd18551 93 GDLVSRVTNDTTLLRELITsGLPQLVT-GVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIilplgRRIRKA-----SKR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 375 TQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATR--KVFVVIGLIwsNELLQMGILTIVLWYGGHL 452
Cdd:cd18551 167 AQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKaaKIEALIGPL--MGLAVQLALLVVLGVGGAR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17511077 453 VIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18551 245 VASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
522-741 |
4.50e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.59 E-value: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfyePTSGEVLIDG------VPVREyd 592
Cdd:COG1118 3 IEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGrdlftnLPPRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 593 hkflhTKVALVGQEpvlYA--R--SVTENIGYGL-----------DKYDD--DMVQnSAKLANAhtfimndttdgyntnv 655
Cdd:COG1118 75 -----RRVGFVFQH---YAlfPhmTVAENIAFGLrvrppskaeirARVEEllELVQ-LEGLADR---------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 656 geKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAEsehtVQEAISKNLK------GKTVILIAH-RLSTVENADK 728
Cdd:COG1118 130 --YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK----VRKELRRWLRrlhdelGGTTVFVTHdQEEALELADR 203
|
250
....*....|...
gi 17511077 729 IVVINKGKVEQLG 741
Cdd:COG1118 204 VVVMNQGRIEQVG 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
522-739 |
5.28e-37 |
|
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: 138.79 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPD-LPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD---HKFLH 597
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVLY---ARSVTENIGYGLDKYDDDMVQNSAKLANAHTFI-MNDTTDGYNtnvgEKGSQMSGGQKQRIAIA 673
Cdd:cd03257 82 KEIQMVFQDPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEVLN----RYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 674 RALVRQPVVLLLDEATSALDAesehTVQEAI------SKNLKGKTVILIAHRLSTVEN-ADKIVVINKGK-VEQ 739
Cdd:cd03257 158 RALALNPKLLIADEPTSALDV----SVQAQIldllkkLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKiVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
522-740 |
7.33e-37 |
|
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: 138.78 E-value: 7.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRP-DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfyePTSGEVLIDGVPVREYDHKFLH 597
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPvlYA---------RSVTE--NIgYGLDKYDDDMvqnsAKLANAhtfimndttdgyntnVGEKGS------ 660
Cdd:COG1124 79 RRVQMVFQDP--YAslhprhtvdRILAEplRI-HGLPDREERI----AELLEQ---------------VGLPPSfldryp 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 661 -QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAesehTVQEAI------SKNLKGKTVILIAHRLSTVEN-ADKIVVI 732
Cdd:COG1124 137 hQLSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQAEIlnllkdLREERGLTYLFVSHDLAVVAHlCDRVAVM 212
|
....*....
gi 17511077 733 NKGK-VEQL 740
Cdd:COG1124 213 QNGRiVEEL 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
518-738 |
1.26e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.48 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPI-RPDLPIMEDLTFTVEPGEVVALVGPSGGGKS---SCIAMLEHfyePTSGEVLIDGVPVREYDH 593
Cdd:COG1136 1 MSPLLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 KFL----HTKVALVGQE----PVLyarSVTENIGYGLdkydddmvqnsaKLANAHTFIMNDTTDGYNTNVG------EKG 659
Cdd:COG1136 78 RELarlrRRHIGFVFQFfnllPEL---TALENVALPL------------LLAGVSRKERRERARELLERVGlgdrldHRP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 660 SQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNL---KGKTVILIAHRLSTVENADKIVVINKGK 736
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELL-RELnreLGTTIVMVTHDPELAARADRVIRLRDGR 221
|
..
gi 17511077 737 VE 738
Cdd:COG1136 222 IV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
522-749 |
2.19e-36 |
|
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: 136.98 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKflhTKV 600
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEPVLYAR-SVTENIGYGLD--KYDDDMVQnsAKLANAHTFImndTTDGYNtnvGEKGSQMSGGQKQRIAIARALV 677
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGLRlkKLPKAEIK--ERVAEALDLV---QLEGYA---NRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAIsKNLK---GKTVILIAHRLS---TVenADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLEL-KRLQkelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
208-495 |
2.24e-36 |
|
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: 139.08 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVF-----GDKASYEKLHKTVFIMGMLSLASTVFGGLrgGSFTYAHATID--RQIR 280
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIeglggGGGVDFSGLLRILLLLLGLYLLSALFSYL--QNRLMARVSQRtvYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 281 NDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLV 360
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 361 NKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKVFVVIGLI--WSNELLQ 438
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDE-INEELYKASFKAQFYSGLLmpIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 439 MGILTIVLwYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAV-GASR 495
Cdd:cd18547 241 LGYVLVAV-VGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALaGAER 297
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
522-737 |
2.50e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCI-AMLeHFYEPTSGEVLIDGVPVREYDHKflhtkV 600
Cdd:COG1121 7 IELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkAIL-GLLPPTSGTVRLFGKPPRRARRR-----I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQE-------PVlyarSVTENIGYGLDKY----------DDDMVQNSAKLANAHTFImndttdgyNTNVGEkgsqMS 663
Cdd:COG1121 78 GYVPQRaevdwdfPI----TVRDVVLMGRYGRrglfrrpsraDREAVDEALERVGLEDLA--------DRPIGE----LS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
522-752 |
2.59e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 137.95 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDH-KFLHTKV 600
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEP----VlyARSVTENIGYGLDKYD---DDM---VQNSAKLANAHTFIMNDTtdgyntnvgekgSQMSGGQKQRI 670
Cdd:TIGR04520 80 GMVFQNPdnqfV--GATVEDDVAFGLENLGvprEEMrkrVDEALKLVGMEDFRDREP------------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK---GKTVILIAHRLSTVENADKIVVINKGKVEQLG------ 741
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETI-RKLNkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreif 224
|
250
....*....|.
gi 17511077 742 NHKTLMEQEGL 752
Cdd:TIGR04520 225 SQVELLKEIGL 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
522-742 |
8.23e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 138.67 E-value: 8.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRP-DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLE---RPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 T---KVALVGQEP-VLYARSVTENIGY-----GLDKYDD--------DMVQNSAKlANAHTfimndttdgyntnvgekgS 660
Cdd:COG1135 79 AarrKIGMIFQHFnLLSSRTVAENVALpleiaGVPKAEIrkrvaellELVGLSDK-ADAYP------------------S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTV----QEaISKNLkGKTVILIAHRLSTVEN-ADKIVVINKG 735
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIldllKD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENG 217
|
....*..
gi 17511077 736 KVEQLGN 742
Cdd:COG1135 218 RIVEQGP 224
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
208-497 |
9.81e-36 |
|
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: 137.13 E-value: 9.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVV-TAVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRS 286
Cdd:cd18544 4 ALLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 287 VVKQEIGFFDMNKTGEICSRLSADCQTMSNtlsLYMNVLT---RNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKI 363
Cdd:cd18544 84 IQRLPLSFFDRTPVGRLVTRVTNDTEALNE---LFTSGLVtliGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 364 FGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFmTFLNVTLKIATRKVFVVIGLIWS-NELLQMGIL 442
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSIKLFALFRPlVELLSSLAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 443 TIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18544 240 ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
522-737 |
3.68e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:PRK13632 8 IKVENVSFSYP-NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEP--VLYARSVTENIGYGLdkyDDDMVQNSAklanahtfiMNDTTDGYNTNVG-----EKGSQ-MSGGQKQRIAIA 673
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGL---ENKKVPPKK---------MKDIIDDLAKKVGmedylDKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTVENADKIVVINKGKV 737
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
522-739 |
4.19e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.58 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPV--REYDHKFL 596
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYA-RSVTENIGYGLDKydddmVQNSAKlANAHTFIMNdttdgYNTNVG--EKG----SQMSGGQKQR 669
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLAPIK-----VKKMSK-AEAEERAME-----LLERVGlaDKAdaypAQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 670 IAIARALVRQPVVLLLDEATSALDAEsehTVQE--AISKNLK--GKTVILIAHRLS---TVenADKIVVINKGK-VEQ 739
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPE---LVGEvlDVMRDLAkeGMTMVVVTHEMGfarEV--ADRVVFMDGGRiVEE 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
522-741 |
5.00e-35 |
|
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: 132.38 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKflHTKVA 601
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIGYGLD--KYD----DDMVQNSAKLAnahtfimndttdGYNTNVGEKGSQMSGGQKQRIAIAR 674
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKlrKVPkdeiDERVREVAELL------------QIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 675 ALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHrlSTVEN---ADKIVVINKGKVEQLG 741
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH--DQVEAmtmADRIAVMNDGQIQQIG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
522-737 |
9.45e-35 |
|
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: 132.69 E-value: 9.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHT--- 598
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEPVLYAR-SVTENIgygldkydddmvqNSAKLANAHT----FIMNDTTDGYN-----TNVG------EKGSQM 662
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENV-------------LSGRLGRRSTwrslFGLFPKEEKQRalaalERVGlldkayQRADQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 663 SGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
522-737 |
9.56e-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: 131.88 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPV--REYDHKFL 596
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYA-RSVTENIGYGLDKydddmVQNSAK---LANAHTFI----MNDTTDGYNtnvgekgSQMSGGQKQ 668
Cdd:cd03262 75 RQKVGMVFQQFNLFPhLTVLENITLAPIK-----VKGMSKaeaEERALELLekvgLADKADAYP-------AQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNL--KGKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVM-KDLaeEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
207-497 |
5.77e-34 |
|
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: 132.25 E-value: 5.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 207 MAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASYEKLHKTVFIMGML---SLASTVFGGLRGGSFTYAHATIDRQIRNDL 283
Cdd:cd18563 3 LGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLagaYVLSALLGILRGRLLARLGERITADLRRDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 284 FRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKI 363
Cdd:cd18563 83 YEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 364 FG--VW--YDMLSEetqnSVAKANDVAEEVLSSIRTVKSFACENYESSRFmTFLNVTLKIATRKVFVVIGLIWS--NELL 437
Cdd:cd18563 163 FWkkIRrlFHRQWR----RWSRLNSVLNDTLPGIRVVKAFGQEKREIKRF-DEANQELLDANIRAEKLWATFFPllTFLT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 438 QMGILtIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18563 238 SLGTL-IVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
523-737 |
1.37e-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: 128.42 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 523 EFRHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKflhtkVAL 602
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VGQE-------PVlyarSVTENIGYGLDKYDDDMVQNS----AKLANAHTFImnDTTDGYNTNVGEkgsqMSGGQKQRIA 671
Cdd:cd03235 73 VPQRrsidrdfPI----SVRDVVLMGLYGHKGLFRRLSkadkAKVDEALERV--GLSELADRQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 672 IARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
522-737 |
2.25e-33 |
|
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: 127.91 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHK---FLHT 598
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQE-PVLYARSVTENIGYGLdkyddDMVQNSAKLANAHTFIMNDTTdGYNTNVGEKGSQMSGGQKQRIAIARALV 677
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFAL-----EVTGVPPREIRKRVPAALELV-GLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVENADK-IVVINKGKV 737
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
518-737 |
2.56e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.03 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKS---SCIAMLEHFYEPTSGEVLIDGVPVREYDHK 594
Cdd:COG1123 1 MTPLLEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKStlaLALMGLLPHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 595 FLHTKVALVGQEP--VLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFImndttdGYNTNVGEKGSQMSGGQKQRIAI 672
Cdd:COG1123 80 LRGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRI 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
523-737 |
2.67e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.40 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 523 EFRHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVAL 602
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VGQepvlyARSVTenigyGLDKYDDDMVqnsaklanahtfimndttdgyntnvgekgSQMSGGQKQRIAIARALVRQPVV 682
Cdd:cd03214 78 VPQ-----ALELL-----GLAHLADRPF-----------------------------NELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 683 LLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLS-TVENADKIVVINKGKV 737
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
522-737 |
4.72e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.87 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDHKFLH- 597
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLV---EPTSGEILVDGQDVTALRGRALRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 --TKVALVGQEPVLYAR-SVTENI-----GY------GLDKYDDDMVQNsaklanAHTFImnDTtdgyntnVG------E 657
Cdd:COG3638 78 lrRRIGMIFQQFNLVPRlSVLTNVlagrlGRtstwrsLLGLFPPEDRER------ALEAL--ER-------VGladkayQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 658 KGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTV-ENADKIVVINK 734
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLArRYADRIIGLRD 222
|
...
gi 17511077 735 GKV 737
Cdd:COG3638 223 GRV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
518-748 |
5.11e-33 |
|
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: 127.79 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLehfYEPTSGEVLIDGVPV---REY 591
Cdd:COG1127 2 SEPMIEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVllkLIIGL---LRPDSGEILVDGQDItglSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 592 DHKFLHTKVALVGQEPVLY-ARSVTENIGYGLD---KYDDDMVQNSA--KLANahtfimndttdgyntnVGEKG------ 659
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFdSLTVFENVAFPLRehtDLSEAEIRELVleKLEL----------------VGLPGaadkmp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 660 SQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK---GKTVILIAHRLSTVEN-ADKIVVINKG 735
Cdd:COG1127 140 SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELI-RELRdelGLTSVVVTHDLDSAFAiADRVAVLADG 218
|
250
....*....|...
gi 17511077 736 KVEQLGNHKTLME 748
Cdd:COG1127 219 KIIAEGTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
522-741 |
2.68e-32 |
|
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: 125.31 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKS---SCIAMLehfYEPTSGEVLIDGVPVR---EYDHKF 595
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKStllRLIVGL---LRPDSGEVLIDGEDISglsEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LHTKVALVGQEPVLY-ARSVTENIGYGL---DKYDDDMVQNSA--KLANahtfimndttdgyntnVGEKG------SQMS 663
Cdd:cd03261 75 LRRRMGMLFQSGALFdSLTVFENVAFPLrehTRLSEEEIREIVleKLEA----------------VGLRGaedlypAELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTV-ENADKIVVINKGKVEQL 740
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAE 218
|
.
gi 17511077 741 G 741
Cdd:cd03261 219 G 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
522-737 |
1.64e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.85 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHK---FLHT 598
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQE-PVLYARSVTENIGY-----GLDKYDD--------DMVQNSAKlanAHTFIMndttdgyntnvgekgsQMSG 664
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIrrrvrevlDLVGLSDK---AKALPH----------------ELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 665 GQKQRIAIARALVRQPVVLLLDEATSALDAE-SEHTVQ--EAIskNLKGKTVILIAHRLSTVENADK-IVVINKGKV 737
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIMEllEEI--NRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
522-750 |
6.33e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.40 E-value: 6.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPImeDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKflhTKV 600
Cdd:COG3840 2 LRLDDLTYRYG---DFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAE---RPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEPVLYAR-SVTENIGYGLD---KYDDDmvqNSAKLANAHTfimndttdgyNTNVGEKG----SQMSGGQKQRIAI 672
Cdd:COG3840 74 SMLFQENNLFPHlTVAQNIGLGLRpglKLTAE---QRAQVEQALE----------RVGLAGLLdrlpGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 673 ARALVRQPVVLLLDEATSALD----AESEHTVQEaISKNLkGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLM 747
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDE-LCRER-GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
...
gi 17511077 748 EQE 750
Cdd:COG3840 219 DGE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
521-752 |
6.94e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 6.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKV 600
Cdd:PRK13635 5 IIRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEP--VLYARSVTENIGYGLDKYD---DDM---VQNSAKLANahtfiMNDTTDgyntnvgEKGSQMSGGQKQRIAI 672
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFGLENIGvprEEMverVDQALRQVG-----MEDFLN-------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTVENADKIVVINKGKV------EQLGNHK 744
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEIleegtpEEIFKSG 231
|
....*...
gi 17511077 745 TLMEQEGL 752
Cdd:PRK13635 232 HMLQEIGL 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
301-788 |
2.43e-30 |
|
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: 129.30 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 301 GEICSRLSADCQTMSNtLSLYMNVLTRNLTMLFGSLIFMFTlswKLSMITLINIPIIFLVNKIFGVwYDMLSEETQNSVA 380
Cdd:TIGR00957 415 GEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYFLWL---NLGPSVLAGVAVMVLMVPLNAV-MAMKTKTYQVAHM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 381 KAND----VAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFV--VIGLIWSNELLQMGILTIVLWYgghLVI 454
Cdd:TIGR00957 490 KSKDnrikLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLhaVGTFTWVCTPFLVALITFAVYV---TVD 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 455 ENKV--ESGLLVSFLLYQFqLGENLRELGEVWNGLMQAVGASRKVFEFIDR----PPRVENTGTyaPDGMTGKIEFRHVA 528
Cdd:TIGR00957 567 ENNIldAEKAFVSLALFNI-LRFPLNILPMVISSIVQASVSLKRLRIFLSHeelePDSIERRTI--KPGEGNSITVHNAT 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 529 FSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhkflhtKVALVGQEPV 608
Cdd:TIGR00957 644 FTWA-RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 LYARSVTENIGYGL---DKYDDDMVQNSAKLANAHTFIMNDTTDgyntnVGEKGSQMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:TIGR00957 710 IQNDSLRENILFGKalnEKYYQQVLEACALLPDLEILPSGDRTE-----IGEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 686 DEATSALDAE-SEHTVQEAISKN--LKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLVqRQMM 762
Cdd:TIGR00957 785 DDPLSAVDAHvGKHIFEHVIGPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL-RTYA 863
|
490 500
....*....|....*....|....*.
gi 17511077 763 SGEDGLDdeIEEPEPAREGGSGRSTR 788
Cdd:TIGR00957 864 PDEQQGH--LEDSWTALVSGEGKEAK 887
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
149-758 |
3.28e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 128.74 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 149 AHVTEVAAGTGDSLLFGDAEHEERLRQEEAEKAAEQRETFQLLFRLLGYMGR-QWKYYGMafFFLFCYSLSR---VFIPY 224
Cdd:PTZ00243 894 AEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSvPWSTYVA--YLRFCGGLHAagfVLATF 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 225 YTGEVVTAVFG-------------DKASYEKLHKTVFIMGMLSLA---STVFGGLRGGSftyahatidRQIRNDLFRSVV 288
Cdd:PTZ00243 972 AVTELVTVSSGvwlsmwstrsfklSAATYLYVYLGIVLLGTFSVPlrfFLSYEAMRRGS---------RNMHRDLLRSVS 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 289 KQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLtrnLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVwY 368
Cdd:PTZ00243 1043 RGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYL---LQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQF-Y 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 369 DMLSEET--QNSVAKAN--DVAEEVLSSIRTVKS------------------FACENYE--SSRFmtfLNVTLKIATRKV 424
Cdd:PTZ00243 1119 NSANREIrrIKSVAKSPvfTLLEEALQGSATITAygkahlvmqealrrldvvYSCSYLEnvANRW---LGVRVEFLSNIV 1195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 425 FVVIGLIwsnellqmGILTIVLWygghlviENKVESGLLVSFLLYQFQLGENL----RELGEVwNGLMQAVgasRKVFEF 500
Cdd:PTZ00243 1196 VTVIALI--------GVIGTMLR-------ATSQEIGLVSLSLTMAMQTTATLnwlvRQVATV-EADMNSV---ERLLYY 1256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 501 IDRPPR-------------VENTGTYAPDGMT------------------GKIEFRHVAFSYpiRPDLP-IMEDLTFTVE 548
Cdd:PTZ00243 1257 TDEVPHedmpeldeevdalERRTGMAADVTGTvviepasptsaaphpvqaGSLVFEGVQMRY--REGLPlVLRGVSFRIA 1334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 549 PGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIgygldkyDDD 628
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV-------DPF 1407
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 629 MVQNSAKLANAHTFI-----MNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALV-RQPVVLLLDEATS----ALDAESEH 698
Cdd:PTZ00243 1408 LEASSAEVWAALELVglrerVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATAnidpALDRQIQA 1487
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 699 TVQEAISknlkGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTL-MEQEGLYKQLVQ 758
Cdd:PTZ00243 1488 TVMSAFS----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVE 1544
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
540-737 |
3.97e-30 |
|
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: 118.62 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREyDHKFLHTKVALVGQEPVLYAR-SVTENI 618
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 619 GY-----GLDKydDDMVQNSAKLANahTFIMNDTTDgyntnvgEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:cd03266 100 EYfaglyGLKG--DELTARLEELAD--RLGMEELLD-------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17511077 694 AESEHTVQEAIsKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03266 169 VMATRALREFI-RQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
542-749 |
8.25e-30 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 119.29 E-value: 8.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFL----HTKVALVGQEPVLYA-RSVTE 616
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 617 NIGYGLDkydddmVQNSAK---LANAHTFImndttdgynTNVGEKG------SQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:cd03294 122 NVAFGLE------VQGVPRaerEERAAEAL---------ELVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 688 ATSALDAESEHTVQE---AISKNLKgKTVILIAHRLS-TVENADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:cd03294 187 AFSALDPLIRREMQDellRLQAELQ-KTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
207-494 |
1.16e-29 |
|
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: 119.49 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 207 MAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRS 286
Cdd:cd18545 4 LALLLMLLSTAASLAGPYLIKIAIDEYIPNG-DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 287 VVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSL-YMNVLTrNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFG 365
Cdd:cd18545 83 LQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNgLINLIP-DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 366 VWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFmTFLNVTLKIATRKVFVVIGLIW-SNELLQMGILTI 444
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIF-DELNRENRKANMRAVRLNALFWpLVELISALGTAL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17511077 445 VLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGAS 494
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASA 290
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
522-731 |
1.28e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.81 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSypiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFlHTKVA 601
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIGY--GLDKYDDDMVQNSAKLAnahTFIMNDTTDgyntnvgEKGSQMSGGQKQRIAIARALVR 678
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaALYGLRADREAIDEALE---AVGLAGLAD-------LPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVENADKIVV 731
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLaRGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-737 |
1.42e-29 |
|
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: 115.22 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReydhkflhtkva 601
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 lvgqepvlyarsvtenigygldkydddmvQNSAKLANAH--TFIMndttdgyntnvgekgsQMSGGQKQRIAIARALVRQ 679
Cdd:cd03216 66 -----------------------------FASPRDARRAgiAMVY----------------QLSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 680 PVVLLLDEATSAL-DAESEHtVQEAIsKNLK--GKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:cd03216 101 ARLLILDEPTAALtPAEVER-LFKVI-RRLRaqGVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
522-748 |
1.78e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.50 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVR--EYDHKFL 596
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDGLKVNdpKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYAR-SVTENIGYGLDKydddmVQNSAKlANAHTFIMNDTTD-GYNTNVGEKGSQMSGGQKQRIAIAR 674
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPLR-----VRGASK-EEAEKQARELLAKvGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 675 ALVRQPVVLLLDEATSALDAESEHTVQEaISKNL--KGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLME 748
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLK-VMQDLaeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
522-739 |
1.82e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPI-RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLE---RPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 T---KVALVGQE-PVLYARSVTENIGY-----GLDKYDD--------DMVQNSAKlANAHTfimndttdgyntnvgekgS 660
Cdd:PRK11153 79 KarrQIGMIFQHfNLLSSRTVFDNVALplelaGTPKAEIkarvtellELVGLSDK-ADRYP------------------A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLK-GKTVILIAHRLSTVEN-ADKIVVINKGK- 736
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDiNRElGLTIVLITHEMDVVKRiCDRVAVIDAGRl 219
|
...
gi 17511077 737 VEQ 739
Cdd:PRK11153 220 VEQ 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
522-741 |
3.35e-29 |
|
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: 116.67 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfyePTSGEVLIDG-----VPVREydh 593
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTllrLIAGLER---PDSGTILFGGedatdVPVQE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 kflhTKVALVGQEPVLYAR-SVTENIGYGLDKYDDDMVQNSAKL-ANAHTFIMNDTTDGYNTNVGekgSQMSGGQKQRIA 671
Cdd:cd03296 74 ----RNVGFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIrAKVHELLKLVQLDWLADRYP---AQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 672 IARALVRQPVVLLLDEATSALDAEsehtvqeaISKNLK----------GKTVILIAHRLS-TVENADKIVVINKGKVEQL 740
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAK--------VRKELRrwlrrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQV 218
|
.
gi 17511077 741 G 741
Cdd:cd03296 219 G 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
542-741 |
7.57e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 114.70 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVePGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREyDHKFLHT-----KVALVGQEPVLYAR- 612
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTllrCIAGLE---KPDGGTIVLNGTVLFD-SRKKINLppqqrKIGLVFQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGLDKYDDDMVQNSA----------KLANAHTfimndttdgyntnvgekgSQMSGGQKQRIAIARALVRQPVV 682
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVdelldllgldHLLNRYP------------------AQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 683 LLLDEATSALDAESEHTVQ---EAISKNLKGkTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLpelKQIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
522-737 |
8.26e-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: 114.19 E-value: 8.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRP---DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMlEHFYEPTSGEVLIDGVPVREYDHKF 595
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTllnALAG-RRTGLGVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LhtkVALVGQEPVLYAR-SVTENIGYgldkydddmvqnSAKLanahtfimndttdgyntnvgekgSQMSGGQKQRIAIAR 674
Cdd:cd03213 83 I---IGYVPQDDILHPTlTVRETLMF------------AAKL-----------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 675 ALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLST--VENADKIVVINKGKV 737
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
540-742 |
8.33e-29 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 115.51 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGV------PVREydhkflhtKVALVGQEPVLYAR- 612
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlpPEKR--------DISYVPQNYALFPHm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGLDKYDDDMVQNSAKLANAHTFImndttdGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSAL 692
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEML------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17511077 693 DAESEHTVQEAISKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGN 742
Cdd:cd03299 161 DVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
522-741 |
1.38e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREY--DHKFLHTk 599
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaENRHVNT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 valVGQEPVLYAR-SVTENIGYGL--DKYDDD-----------MVQNSaKLANahtfimndttdgyntnvgEKGSQMSGG 665
Cdd:PRK09452 91 ---VFQSYALFPHmTVFENVAFGLrmQKTPAAeitprvmealrMVQLE-EFAQ------------------RKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 666 QKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK---GKTVILIAHrlsTVENA----DKIVVINKGKVE 738
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQrklGITFVFVTH---DQEEAltmsDRIVVMRDGRIE 224
|
...
gi 17511077 739 QLG 741
Cdd:PRK09452 225 QDG 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
518-738 |
1.51e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.98 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEP--VLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFI-MNDTTDgyntnvgEKGSQMSGGQKQRIAIAR 674
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVgMQDFKE-------REPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 675 ALVRQPVVLLLDEATSALDAESE----HTVQEAISKNlkGKTVILIAHRLSTVENADKIVVINKGKVE 738
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
512-738 |
4.60e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 512 TYAPDGMTGKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CI-AMLEHfyEP---TSGEVLID 584
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTllrCLnRMNDL--IPgarVEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 585 GVPVreYDHKF----LHTKVALVGQEPVLYARSVTENIGYGL------DKYD-DDMVQNSAKLANahtfIMNDTTDGYNT 653
Cdd:COG1117 77 GEDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgikSKSElDEIVEESLRKAA----LWDEVKDRLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 654 NvgekGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLKGK-TVILIAH------RLStvena 726
Cdd:COG1117 151 S----ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELI-LELKKDyTIVIVTHnmqqaaRVS----- 220
|
250
....*....|...
gi 17511077 727 DKIVVINKGK-VE 738
Cdd:COG1117 221 DYTAFFYLGElVE 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
540-742 |
1.00e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV--REYDHKFLHTKVALVGQEP--VLYARSVT 615
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGYGLDKY--DDDMVQNSAKLAnahtfiMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:PRK13637 103 KDIAFGPINLglSEEEIENRVKRA------MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17511077 694 AESEHTVQEAIsKNLKGK---TVILIAHRLSTVEN-ADKIVVINKGKVEQLGN 742
Cdd:PRK13637 177 PKGRDEILNKI-KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
522-737 |
1.20e-27 |
|
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: 111.44 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReYDHKFLHTKVA 601
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIGY-----GLDKYDDDMVQNsaklanaHTFIMNDTTDGYNTNVGekgsQMSGGQKQRIAIARA 675
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVE-------LLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
522-741 |
1.23e-27 |
|
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: 111.13 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGeVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKfLHTKVA 601
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENIGY-----GL-DKYDDDMVQNSAKLANahtfiMNDTTDgyntnvgEKGSQMSGGQKQRIAIAR 674
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIpSKEVKARVDEVLELVN-----LGDRAK-------KKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 675 ALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
522-737 |
1.27e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReYDHKFL---HT 598
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEP--VLYARSVTENIGYG-LD-KYDDDMVQNSAKLANAhtfimndttdgyntNVGEKGSQ------MSGGQKQ 668
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGpLNlGLSKEEVEKRVKEALK--------------AVGMEGFEnkpphhLSGGQKK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVE-NADKIVVINKGKV 737
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
524-741 |
1.46e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.13 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 524 FRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDHKflHTKV 600
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLE---DITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEPVLYAR-SVTENIGYGL-----DKYD-DDMVQNSAK-LANAHTfimndttdgyntnVGEKGSQMSGGQKQRIAI 672
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGLklagaKKEEiNQRVNQVAEvLQLAHL-------------LDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHrlSTVEN---ADKIVVINKGKVEQLG 741
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
522-737 |
2.70e-27 |
|
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: 110.28 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPdlpimEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVpvreyDHKFLHTK-- 599
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAPPAdr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 -VALVGQEPVLYAR-SVTENIGYG------LDKYDddmvQNSAKLANAHTfimndttdGYNTNVGEKGSQMSGGQKQRIA 671
Cdd:cd03298 71 pVSMLFQENNLFAHlTVEQNVGLGlspglkLTAED----RQAIEVALARV--------GLAGLEKRLPGELSGGERQRVA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 672 IARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
208-473 |
5.13e-27 |
|
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: 111.72 E-value: 5.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAVFGdKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSV 287
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIDEGIA-NGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 288 vkQEIGFFDMNK--TGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVnkIFG 365
Cdd:cd18548 83 --QSFSFAEIDKfgTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALV--VFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 366 VWYDM--LSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKVFVVIGLIWSNELLQMGILT 443
Cdd:cd18548 159 IMKKAipLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDK-ANDDLTDTSLKAGRLMALLNPLMMLIMNLAI 237
|
250 260 270
....*....|....*....|....*....|.
gi 17511077 444 I-VLWYGGHLVIENKVESGLLVSFLLYQFQL 473
Cdd:cd18548 238 VaILWFGGHLINAGSLQVGDLVAFINYLMQI 268
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
275-469 |
6.95e-27 |
|
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: 111.39 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 275 IDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLS-----LYMNVLTrnltmLFGSLIFMFTLSWKLSMI 349
Cdd:cd18549 73 IETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHhgpedLFISIIT-----IIGSFIILLTINVPLTLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 350 TLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKVFVVIG 429
Cdd:cd18549 148 VFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDE-GNDRFLESKKKAYKAMA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17511077 430 LIWSNELLQMGILT-IVLWYGGHLVIENKVESGLLVSFLLY 469
Cdd:cd18549 227 YFFSGMNFFTNLLNlVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
207-473 |
7.38e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 111.42 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 207 MAFFFLFCYSLSRVFIPYYTGEVV-TAVFGDKASYeklhktVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQI----RN 281
Cdd:cd18550 3 LVLLLILLSALLGLLPPLLLREIIdDALPQGDLGL------LVLLALGMVAVAVASALLGVVQTYLSARIGQGVmydlRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 282 DLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVN 361
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 362 KIFGVWYDMLSEETQNSVAKANDVAEEVLS--SIRTVKSFACENYESSRF------MTFLNVTLKIATRKVFVVIGLIws 433
Cdd:cd18550 157 RRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFarrsreLRDLGVRQALAGRWFFAALGLF-- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17511077 434 nellqMGILT-IVLWYGGHLVIENKVESGLLVSFLLYQFQL 473
Cdd:cd18550 235 -----TAIGPaLVYWVGGLLVIGGGLTIGTLVAFTALLGRL 270
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
296-758 |
9.64e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 117.77 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 296 DMNKTGEICSRL----SAD-CQTMSNTLsLYMNVltrNLTMLFGSLIFmftlswklsmitLINIPI-IFLVNKIfgvwyD 369
Cdd:PLN03232 407 DANALQQIAEQLhglwSAPfRIIVSMVL-LYQQL---GVASLFGSLIL------------FLLIPLqTLIVRKM-----R 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 370 MLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLK-------IATRKVFVVIGLIWSNELLQMGIL 442
Cdd:PLN03232 466 KLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSwfrkaqlLSAFNSFILNSIPVVVTLVSFGVF 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 443 TIVlwyGGHLVIENKVESGLLVSFLLYQFQLGENLrelgevwngLMQAVGAS---RKVFEFIDRPPRVENTGTYAPDGmT 519
Cdd:PLN03232 546 VLL---GGDLTPARAFTSLSLFAVLRSPLNMLPNL---------LSQVVNANvslQRIEELLLSEERILAQNPPLQPG-A 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCI-AMLEHFYEPTSGEVLIDGvpvreydhkflht 598
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRG------------- 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEPVLYARSVTENIGYGLD----KY----DDDMVQNSAKLANAHTFimndttdgynTNVGEKGSQMSGGQKQRI 670
Cdd:PLN03232 680 SVAYVPQVSWIFNATVRENILFGSDfeseRYwraiDVTALQHDLDLLPGRDL----------TEIGERGVNISGGQKQRV 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTV-QEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
....*....
gi 17511077 750 EGLYKQLVQ 758
Cdd:PLN03232 830 GSLFKKLME 838
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
222-497 |
1.01e-26 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 111.09 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 222 IPYYTGEVVTAVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTG 301
Cdd:cd18778 18 PPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 302 EICSRLSADCQTMSNTL-----SLYMNVLTrnltmLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQ 376
Cdd:cd18778 98 DLMSRVINDVANVERLIadgipQGITNVLT-----LVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 377 NSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTfLNVTLKIATRKVFVVIGLIW-SNELLQ-MGILtIVLWYGGHLVI 454
Cdd:cd18778 173 EALGELNALLQDNLSGIREIQAFGREEEEAKRFEA-LSRRYRKAQLRAMKLWAIFHpLMEFLTsLGTV-LVLGFGGRLVL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17511077 455 ENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18778 251 AGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
538-737 |
1.79e-26 |
|
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: 107.69 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVpvrEYDHkfLHTKVALVG---QEPVLY-ARS 613
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQK--NIEALRRIGaliEAPGFYpNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 614 VTENI-----GYGLDKYDDDMVQNSAKLANAHtfimndttdgyntnvGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:cd03268 89 ARENLrllarLLGIRKKRIDEVLDVVGLKDSA---------------KKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17511077 689 TSALDAESEHTVQEAI-SKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03268 154 TNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
522-730 |
2.39e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:PRK10247 8 LQLQNVGYLAG---DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENI--GYGLDKYDDDMVQNSAKLANahtFIMNDTTDGYNTNvgekgsQMSGGQKQRIAIARALVRQ 679
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLifPWQIRNQQPDPAIFLDDLER---FALPDTILTKNIA------ELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17511077 680 PVVLLLDEATSALDAESEHTVQEAISKNL--KGKTVILIAHRLSTVENADKIV 730
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
517-761 |
3.61e-26 |
|
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: 108.46 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 517 GMTGKIEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFL 596
Cdd:cd03288 15 GLGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYARSvtenIGYGLD---KYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAIA 673
Cdd:cd03288 94 RSRLSIILQDPILFSGS----IRFNLDpecKCTDDRLWEALEIAQLKNMV-KSLPGGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQE-GL 752
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGV 248
|
....*....
gi 17511077 753 YKQLVQRQM 761
Cdd:cd03288 249 FASLVRTDK 257
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
521-742 |
5.67e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 110.32 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSC---IAMLEhfyEPTSGEVLIDGVPV-----REYD 592
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLE---RITSGEIWIGGRVVnelepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 593 hkflhtkVALVGQEPVLYAR-SVTENIGYGL-----DKYD-DDMVQNSAKLANAHTFImndttdgyntnvGEKGSQMSGG 665
Cdd:PRK11650 78 -------IAMVFQNYALYPHmSVRENMAYGLkirgmPKAEiEERVAEAARILELEPLL------------DRKPRELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 666 QKQRIAIARALVRQPVVLLLDEATSALDAESEhtVQEAIS-KNLK---GKTVILIAHrlSTVEN---ADKIVVINKGKVE 738
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRLEiQRLHrrlKTTSLYVTH--DQVEAmtlADRVVVMNGGVAE 214
|
....
gi 17511077 739 QLGN 742
Cdd:PRK11650 215 QIGT 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
522-759 |
9.27e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.96 E-value: 9.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDlPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGE---VLIDGVPVREYDHKFLHT 598
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEP--VLYARSVTENIGYGLdkydddmvQNSAKLANAHTFIMNDTTD--GYNTNVGEKGSQMSGGQKQRIAIAR 674
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGL--------ENRAVPRPEMIKIVRDVLAdvGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 675 ALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVENADKIVVINKGKV------EQLGNHKTL 746
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLlaqgspVEIFSKVEM 236
|
250
....*....|...
gi 17511077 747 MEQEGLYKQLVQR 759
Cdd:PRK13640 237 LKEIGLDIPFVYK 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
542-785 |
9.49e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReydhkFLHTK------VALVGQEPVLYA-RSV 614
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-----FRSPRdaqaagIAIIHQELNLVPnLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYG--------LDKydDDMVQNSAKLANAHtfimndttdGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:COG1129 97 AENIFLGreprrgglIDW--RAMRRRARELLARL---------GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 687 EATSAL-DAESEHtVQEAIsKNLK--GKTVILIAHRLSTV-ENADKIVVINKGKVEQLGNHKTLMEQEglykqLVqrQMM 762
Cdd:COG1129 166 EPTASLtEREVER-LFRII-RRLKaqGVAIIYISHRLDEVfEIADRVTVLRDGRLVGTGPVAELTEDE-----LV--RLM 236
|
250 260
....*....|....*....|...
gi 17511077 763 SGEdglddEIEEPEPAREGGSGR 785
Cdd:COG1129 237 VGR-----ELEDLFPKRAAAPGE 254
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
522-726 |
9.92e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.26 E-value: 9.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYP-IRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV------Reydhk 594
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 595 flhtkvALVGQEPVLYA-RSVTENIGYGL-----DKydddmvqnSAKLANAHTFImndttdgynTNVGEKG------SQM 662
Cdd:COG4525 79 ------GVVFQKDALLPwLNVLDNVAFGLrlrgvPK--------AERRARAEELL---------ALVGLADfarrriWQL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 663 SGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHrlsTVENA 726
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEA 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
526-737 |
1.16e-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: 105.42 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 526 HVAFSYPIRPDlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREydhKFLHTKVALVGQ 605
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 606 EP--VLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNDttdgyntnvgEKGSQMSGGQKQRIAIARALVRQPVVL 683
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKE----------RHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 684 LLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHR---LSTVenADKIVVINKGKV 737
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDyefLAKV--CDRVLLLANGAI 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
524-774 |
1.21e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 524 FRHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhkflHTKVALV 603
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 604 GQEPVLYA-RSVTENIGYG-------LDKYD------DDMVQNSAKLANAHTFImnDTTDGYN--TNVGE--KG------ 659
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGdaelralEAELEeleaklAEPDEDLERLAELQEEF--EALGGWEaeARAEEilSGlgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 660 ------SQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESehtVQ--EAISKNLKGkTVILIAH-R--LSTVenADK 728
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--ATR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17511077 729 IVVINKGKVEQ-LGNHKTLMEQeglyKQLVQRQMMSGEDGLDDEIEE 774
Cdd:COG0488 219 ILELDRGKLTLyPGNYSAYLEQ----RAERLEQEAAAYAKQQKKIAK 261
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
522-739 |
1.21e-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: 108.60 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRP-DLPIMEDLTFTVEPGEVVALVGPSGGGKS---SCIAMLEHFYEPTSGEVLIDGVPVREYDHK--- 594
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKStlaRAILGLLPPPGITSGEILFDGEDLLKLSEKelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 595 -FLHTKVALVGQEPvlYA-----RSVTENIGYGLDKYDD--------------DMVQ--NSAKLANA--Htfimndttdg 650
Cdd:COG0444 82 kIRGREIQMIFQDP--MTslnpvMTVGDQIAEPLRIHGGlskaeareraiellERVGlpDPERRLDRypH---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 651 yntnvgekgsQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAesehTVQEAIS---KNLK---GKTVILIAHRLSTV- 723
Cdd:COG0444 150 ----------ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILnllKDLQrelGLAILFITHDLGVVa 215
|
250
....*....|....*..
gi 17511077 724 ENADKIVVINKGK-VEQ 739
Cdd:COG0444 216 EIADRVAVMYAGRiVEE 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
542-737 |
1.45e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.50 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReydhkflHTKVALVG---QEPVLYAR-SVTEN 617
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRIGylpEERGLYPKmKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGY-----GLDKydDDMVQNSAKLANAHtfimnDTTDGYNTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLDEATSAL 692
Cdd:COG4152 92 LVYlarlkGLSK--AEAKRRADEWLERL-----GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17511077 693 DAESEHTVQEAI-SKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:COG4152 161 DPVNVELLKDVIrELAAKGTTVIFSSHQMELVEElCDRIVIINKGRK 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
542-737 |
1.45e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReydhkFLHTKVAL------VGQEPVLYAR-SV 614
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-----IRSPRDAIalgigmVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGLDKYDD---DMVQNSAKLAnahtfimnDTTDGYNTNV--GEKGSQMSGGQKQRIAIARALVRQPVVLLLDEAT 689
Cdd:COG3845 98 AENIVLGLEPTKGgrlDRKAARARIR--------ELSERYGLDVdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 690 SALdaesehTVQEA-----ISKNLK--GKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:COG3845 170 AVL------TPQEAdelfeILRRLAaeGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
522-752 |
1.76e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYpiRPDLPI-MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKV 600
Cdd:PRK13648 8 IVFKNVSFQY--QSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEP--VLYARSVTENIGYGLDKYD---DDMVQNSAKlanahtfIMNDTtDGYNTNVGEKGSqMSGGQKQRIAIARA 675
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLENHAvpyDEMHRRVSE-------ALKQV-DMLERADYEPNA-LSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLME-QEGL 752
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDhAEEL 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
522-737 |
4.70e-25 |
|
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: 104.72 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRP------------------DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLI 583
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 584 DG-VPVREYDhKFLHTKVALVGQE-------PVLYARSVTENIgYGLDkyDDDMVQNSAKLANahtfiMNDTTDGYNTNV 655
Cdd:cd03267 81 AGlVPWKRRK-KFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-YDLP--PARFKKRLDELSE-----LLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 656 gekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVI 732
Cdd:cd03267 152 ----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVI 227
|
....*
gi 17511077 733 NKGKV 737
Cdd:cd03267 228 DKGRL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
542-737 |
8.13e-25 |
|
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: 103.67 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV-REYDHKFLHTKVALVGQEPVLYAR-SVTENI- 618
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIARLGIGRTFQIPRLFPElTVLENVm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 619 ---------GYGLDKYDDDMVQNSAKLANAHTFImnDTTDGYNTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLDEAT 689
Cdd:cd03219 98 vaaqartgsGLLLARARREEREARERAEELLERV--GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17511077 690 SAL-DAESEHTVqEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03219 172 AGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
542-749 |
1.78e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.20 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDH---KFLHTKVALVGQEPvlYA---- 611
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTlgrLLLRLE---EPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDP--YAslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 -RSVTENIGYGLDKYDD--------------DMVQNSAKLAN--AHTFimndttdgyntnvgekgsqmSGGQKQRIAIAR 674
Cdd:COG4608 111 rMTVGDIIAEPLRIHGLaskaerrervaellELVGLRPEHADryPHEF--------------------SGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 675 ALVRQPVVLLLDEATSALDAesehTVQEAISkNL-------KGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDV----SIQAQVL-NLledlqdeLGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
...
gi 17511077 747 MEQ 749
Cdd:COG4608 246 YAR 248
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
205-497 |
2.36e-24 |
|
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: 104.57 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 205 YGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASY--------------EKLHKTVFIMGMLSLASTVFGGLRG-GSFT 269
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFlplvpaslgpadprGQLWLLGGLTVAAFLLESLFQYLSGvLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 270 YAHaTIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMI 349
Cdd:cd18565 81 FAQ-RVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 350 TLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIG 429
Cdd:cd18565 160 ALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 430 LIWSNELLQMGILTIVLWYGGHLVIENKVES------GLLVSFLLYQFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18565 240 FFPVIRLVAGAGFVATFVVGGYWVLDGPPLFtgtltvGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
539-737 |
3.92e-24 |
|
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: 101.20 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHkflhTKVALVGQEPVLY-ARSVTEN 617
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR----NRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGY-----GLDKYD-----DDMVQnsaKLanahtfimnDTTDGYNTNVgekgSQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:cd03269 91 LVYlaqlkGLKKEEarrriDEWLE---RL---------ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17511077 688 ATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
253-475 |
7.78e-24 |
|
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: 103.13 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 253 LSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTML 332
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 333 FGSLIFMFTLSWKLSMITLINIPIIFLVNkifGVWYDMLSEET---QNSVAKANDVAEEVLSSIRTVKSFACENYESSRF 409
Cdd:cd18558 148 GTGFIIGFIRGWKLTLVILAISPVLGLSA---VVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRY 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 410 MTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIENKVESG----LLVSFLLYQFQLGE 475
Cdd:cd18558 225 AQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGevltVFFSVLIGAFSAGQ 294
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
501-748 |
8.46e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.15 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 501 IDRPPrventgTYAPDGMTGKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGE 580
Cdd:PRK11607 5 IPRPQ------AKTRKALTPLLEIRNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 581 VLIDGVP---VREYDHkflhtKVALVGQEPVLYAR-SVTENIGYGLdKYD-------DDMVQNSAKLANAHTFimndttd 649
Cdd:PRK11607 76 IMLDGVDlshVPPYQR-----PINMMFQSYALFPHmTVEQNIAFGL-KQDklpkaeiASRVNEMLGLVHMQEF------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 650 gyntnVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAH-RLSTVENA 726
Cdd:PRK11607 143 -----AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMA 217
|
250 260
....*....|....*....|..
gi 17511077 727 DKIVVINKGKVEQLGNHKTLME 748
Cdd:PRK11607 218 GRIAIMNRGKFVQIGEPEEIYE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
539-749 |
9.02e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.65 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReyDHKFLHTKVALVGQEPVLYAR-SVTEN 617
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGYGLDKYD------DDMVQNSAKLANAHTFimndtTDGYNtnvgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSA 691
Cdd:PRK11432 99 VGYGLKMLGvpkeerKQRVKEALELVDLAGF-----EDRYV-------DQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 692 LDAESEHTVQEAIsKNLK---GKTVILIAHRLS-TVENADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:PRK11432 167 LDANLRRSMREKI-RELQqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
536-748 |
1.19e-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: 100.20 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFLHTKVALVGQEPVLYAR-S 613
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 614 VTENI---GYGLDKYD-----DDMVQNSAKLAnahtfimndttdgynTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:cd03224 92 VEENLllgAYARRRAKrkarlERVYELFPRLK---------------ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 686 DEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTV-ENADKIVVINKGKVEQLGNHKTLME 748
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
522-743 |
1.28e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIrpdLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDG------VPVREYDHKF 595
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LHTKVALVGQEPVLYA-RSVTENIG------YGLDKydDDMVQNSAKLANahTFIMNDTTDGYNTnvgekgsQMSGGQKQ 668
Cdd:COG4161 80 LRQKVGMVFQQYNLWPhLTVMENLIeapckvLGLSK--EQAREKAMKLLA--RLRLTDKADRFPL-------HLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRlstVENADKI----VVINKGKVEQLGN 742
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSqtGITQVIVTHE---VEFARKVasqvVYMEKGRIIEQGD 224
|
.
gi 17511077 743 H 743
Cdd:COG4161 225 A 225
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
239-466 |
1.60e-23 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 101.75 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 239 SYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSaDCQTMSNTL 318
Cdd:cd18570 37 DINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 319 SLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKS 398
Cdd:cd18570 116 SSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 399 FACENYES----SRFMTFLNVTLKiatrkvFVVIGLIWSN--ELLQMGILTIVLWYGGHLVIENKVESGLLVSF 466
Cdd:cd18570 196 LNAEEQFLkkieKKFSKLLKKSFK------LGKLSNLQSSikGLISLIGSLLILWIGSYLVIKGQLSLGQLIAF 263
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
539-741 |
1.67e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.85 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHFyepTSGEVLIDGVPVREydhkfLHTK---VALVGQEPVLYAR 612
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTllrIIAGLEHQ---TSGHIRFHGTDVSR-----LHARdrkVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 -SVTENIGYGLDKYDD-----------------DMVQnSAKLANAHTfimndttdgyntnvgekgSQMSGGQKQRIAIAR 674
Cdd:PRK10851 89 mTVFDNIAFGLTVLPRrerpnaaaikakvtqllEMVQ-LAHLADRYP------------------AQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 675 ALVRQPVVLLLDEATSALDAESEHTVQEAISK---NLKGKTVILIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
538-741 |
1.75e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVL-YARSVTE 616
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 617 NIGYGLDKYDDDMVQNSAKLANAhtfiMNDT-TDGYntnVGEKGSQMSGGQKQRIAIARALVR------QPVVLLLDEAT 689
Cdd:PRK13548 96 VVAMGRAPHGLSRAEDDALVAAA----LAQVdLAHL---AGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 690 SALDAESEHTVQEaISKNL---KGKTVILIAHRLstveN-----ADKIVVINKGKVEQLG 741
Cdd:PRK13548 169 SALDLAHQHHVLR-LARQLaheRGLAVIVVLHDL----NlaaryADRIVLLHQGRLVADG 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
544-750 |
1.96e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 544 TFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPvreydhkflHTK-------VALVGQEPVLYAR-SVT 615
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---------HTTtppsrrpVSMLFQENNLFSHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGYGLD---KYDDDMVQNSAKLANahtfimndttdgyntNVGEKG------SQMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:PRK10771 90 QNIGLGLNpglKLNAAQREKLHAIAR---------------QMGIEDllarlpGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 687 EATSALD----AESEHTVQE-AISKNLkgkTVILIAHRLstvENADKI----VVINKGKVEQLGNHKTLMEQE 750
Cdd:PRK10771 155 EPFSALDpalrQEMLTLVSQvCQERQL---TLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDELLSGK 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
529-775 |
2.90e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 106.36 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 529 FSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCI-AMLEHFYEPTSGEVLIDGvpvreydhkflhtKVALVGQEP 607
Cdd:PLN03130 622 FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRG-------------TVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 608 VLYARSVTENIGYGLDkYDDDMVqNSAKLANAHTFIMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:PLN03130 689 WIFNATVRDNILFGSP-FDPERY-ERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 688 ATSALDAESEHTV-QEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLvqrqmMSGED 766
Cdd:PLN03130 767 PLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL-----MENAG 841
|
....*....
gi 17511077 767 GLDDEIEEP 775
Cdd:PLN03130 842 KMEEYVEEN 850
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
215-481 |
3.14e-23 |
|
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: 100.63 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 215 YSLSRVFIPYYTGEVVTAV--FGDKASyekLHKTVFIMGMLSLASTVFGGLRggSFTYAHATIDRQ--IRNDLFRSVVKQ 290
Cdd:cd18543 11 ATLAGLAIPLLTRRAIDGPiaHGDRSA---LWPLVLLLLALGVAEAVLSFLR--RYLAGRLSLGVEhdLRTDLFAHLQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 291 EIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTrNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDM 370
Cdd:cd18543 86 DGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLG-NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 371 LSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGG 450
Cdd:cd18543 165 ASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGG 244
|
250 260 270
....*....|....*....|....*....|.
gi 17511077 451 HLVIENKVESGLLVSFLLYQFQLGENLRELG 481
Cdd:cd18543 245 WLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
535-735 |
3.83e-23 |
|
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: 98.56 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 535 PDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTK----VALVGQEPVLY 610
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 ARSVTENIGYG--LDKYDDDMVQNSAKLANAhtfiMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:cd03290 92 NATVEENITFGspFNKQRYKAVTDACSLQPD----IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17511077 689 TSALDAE-SEHTVQEAISKNLKG--KTVILIAHRLSTVENADKIVVINKG 735
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
522-737 |
4.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDH-KFLHTKV 600
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEP--VLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFImndttdGYNTNVGEKGSQMSGGQKQRIAIARALVR 678
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI------GLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVENADKIVVINKGKV 737
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
540-741 |
6.32e-23 |
|
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: 98.31 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREY--DHKFLHTKVALvgqepvLYARSVTEN 617
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNYSL------LPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGYGLDKYDDDMVQNSAKLanahtfIMNDTTD--GYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAE 695
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERRA------IVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17511077 696 SEHTVQEAISK--NLKGKTVILIAHRL-STVENADKIVVINKGKVEQLG 741
Cdd:TIGR01184 149 TRGNLQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
537-735 |
6.75e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 97.89 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 537 LPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLidgvpvreYDHKFlhTKVALVGQEP--VLYARSV 614
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG--GWVDLAQASPreILALRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TenIGY------------GLD---------KYDDDMVQNSAKLANAH-------------TFimndttdgyntnvgekgs 660
Cdd:COG4778 94 T--IGYvsqflrviprvsALDvvaepllerGVDREEARARARELLARlnlperlwdlppaTF------------------ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 661 qmSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVEN-ADKIVVINKG 735
Cdd:COG4778 154 --SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKarGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
526-718 |
7.05e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.62 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 526 HVAFSYPIRPDLpimEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVR----EYDHKFLHtkva 601
Cdd:PRK11248 6 HLYADYGGKPAL---EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaERGVVFQN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 lvgqEPVLYARSVTENIGYGLDKYDddmVQNSAKLANAHTFImndttdgynTNVGEKGS------QMSGGQKQRIAIARA 675
Cdd:PRK11248 79 ----EGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQML---------KKVGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAH 718
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
521-749 |
9.15e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 9.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFRHVAFSYpiRPDLPI----MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV-REYDHKF 595
Cdd:PRK13646 2 TIRFDNVSYTY--QKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LHT---KVALVGQ--EPVLYARSVTENIGYGLDKYDDDMVQNSAKlanAHTFIMNDttdGYNTNVGEKGS-QMSGGQKQR 669
Cdd:PRK13646 80 IRPvrkRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNY---AHRLLMDL---GFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 670 IAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
...
gi 17511077 747 MEQ 749
Cdd:PRK13646 234 FKD 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
539-781 |
9.21e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.60 E-value: 9.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREydhkfLHTKVALVGQEPVLYA-RSVTEN 617
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGYGLD-KYDDDMVQ--NSAKLANahtfimndttdgyntNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDA 694
Cdd:PRK11247 102 VGLGLKgQWRDAALQalAAVGLAD---------------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 695 ESEHTVQEAIsKNL---KGKTVILIAHRLS-TVENADKIVVINKGKVeqlgnhktlmeqeglykqlvqrqmmsgedGLDD 770
Cdd:PRK11247 167 LTRIEMQDLI-ESLwqqHGFTVLLVTHDVSeAVAMADRVLLIEEGKI-----------------------------GLDL 216
|
250
....*....|.
gi 17511077 771 EIEEPEPAREG 781
Cdd:PRK11247 217 TVDLPRPRRRG 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
486-740 |
2.38e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.19 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 486 GLMQAVGAsrkvfefIDRPPRVENTGTYAPDGMtgkIEFRHVAFSypiRPDL-PIMEDLTFTVEPGEVVALVGPSGGGKS 564
Cdd:COG4178 337 GFEEALEA-------ADALPEAASRIETSEDGA---LALEDLTLR---TPDGrPLLEDLSLSLKPGERLLITGPSGSGKS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 565 S---CIAMLEHFYeptSGEVLidgVPVREydhkflhtKVALVGQEP----------VLYARSVtenigyglDKYDDDMVQ 631
Cdd:COG4178 404 TllrAIAGLWPYG---SGRIA---RPAGA--------RVLFLPQRPylplgtlreaLLYPATA--------EAFSDAELR 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 632 NSAKLANAHTFI--MNDTTDgyntnvgeKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK 709
Cdd:COG4178 462 EALEAVGLGHLAerLDEEAD--------WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP 533
|
250 260 270
....*....|....*....|....*....|.
gi 17511077 710 GKTVILIAHRLSTVENADKIVVINKGKVEQL 740
Cdd:COG4178 534 GTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
522-737 |
2.95e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.69 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKS---SCIAMLEhfyEPTSGEVLIDGVPVREYDHKFLHT 598
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKStllSMISRLL---PPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEPVLYAR-SVTENIGYG--------LDKYDDDMVQNSAKLAN----AHTFImndttdgyntnvgekgSQMSGG 665
Cdd:COG4604 76 RLAILRQENHINSRlTVRELVAFGrfpyskgrLTAEDREIIDEAIAYLDledlADRYL----------------DELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 666 QKQRIAIARALVRQPVVLLLDEATSALDAesEHTVQeaISKNLK------GKTVILIAHRLstveN-----ADKIVVINK 734
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQ--MMKLLRrladelGKTVVIVLHDI----NfascyADHIVAMKD 211
|
...
gi 17511077 735 GKV 737
Cdd:COG4604 212 GRV 214
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
251-495 |
3.37e-22 |
|
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: 97.97 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 251 GMLSLASTVFGGLRGGSFTYAhatidrqIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLT 330
Cdd:cd18564 68 GLASYAGTYLTALVGQRVVLD-------LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 331 MLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFM 410
Cdd:cd18564 141 TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 411 TFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQA 490
Cdd:cd18564 221 RENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKA 300
|
....*.
gi 17511077 491 -VGASR 495
Cdd:cd18564 301 sASAER 306
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
542-737 |
3.45e-22 |
|
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: 96.65 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV---REYdhkflhtKVALVG-----QEPVLYAR- 612
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPH-------RIARLGiartfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENI--------GYGLDKYDDDMVQNSAKLANAHTFIMN-----DTTDGYNTNVGEkgsqMSGGQKQRIAIARALVRQ 679
Cdd:COG0411 95 TVLENVlvaaharlGRGLLAALLRLPRARREEREARERAEEllervGLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 680 PVVLLLDEATSAL-DAESEHTVQ--EAISKNLkGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELAEliRRLRDER-GITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
522-743 |
3.48e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDLpimEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydHKF------ 595
Cdd:PRK11124 3 IQLNGINCFYGAHQAL---FDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG-------NHFdfsktp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 -------LHTKVALVGQEPVLYAR-SVTENI------GYGLDKydDDMVQNSAKLANahTFIMNDTTDGYNTnvgekgsQ 661
Cdd:PRK11124 73 sdkaireLRRNVGMVFQQYNLWPHlTVQQNLieapcrVLGLSK--DQALARAEKLLE--RLRLKPYADRFPL-------H 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 662 MSGGQKQRIAIARALVRQPVVLLLDEATSALDAESehTVQ-EAISKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI--TAQiVSIIRELAetGITQVIVTHEVEVARKtASRVVYMENGHI 219
|
....*.
gi 17511077 738 EQLGNH 743
Cdd:PRK11124 220 VEQGDA 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
261-755 |
3.72e-22 |
|
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: 103.07 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 261 GGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSlIFMF 340
Cdd:TIGR01271 942 GFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGA-IFVV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 341 TLSWKLSMITLINIPIIFLVNKIFgvwYDMLSEETQNSVAKAND-VAEEVLSSIR---TVKSFACENYessrFMTFLNVT 416
Cdd:TIGR01271 1021 SVLQPYIFIAAIPVAVIFIMLRAY---FLRTSQQLKQLESEARSpIFSHLITSLKglwTIRAFGRQSY----FETLFHKA 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 417 LKIATRKVFVVIG-LIWsnelLQMGI-LTIVLWYGGHLVI------ENKVESGLLVSF---LLYQFQLGENLrelGEVWN 485
Cdd:TIGR01271 1094 LNLHTANWFLYLStLRW----FQMRIdIIFVFFFIAVTFIaigtnqDGEGEVGIILTLamnILSTLQWAVNS---SIDVD 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 486 GLMQAVGasrKVFEFIDRP---PRVENTGTYAPDGMTGKIEFRHVAFSYPIRPDL--------------PIMEDLTFTVE 548
Cdd:TIGR01271 1167 GLMRSVS---RVFKFIDLPqeePRPSGGGGKYQLSTVLVIENPHAQKCWPSGGQMdvqgltakyteagrAVLQDLSFSVE 1243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 549 PGEVVALVGPSGGGKSSCIAMLEHFYEpTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLYARSVTENIGyGLDKYDDD 628
Cdd:TIGR01271 1244 GGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDE 1321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 629 MVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNL 708
Cdd:TIGR01271 1322 EIWKVAEEVGLKSVI-EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF 1400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17511077 709 KGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQ 755
Cdd:TIGR01271 1401 SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
547-746 |
7.47e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.59 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 547 VEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSG-----EVLIDG-VPVREYDH--KFLHTKVALVGQEPVLYA-RSV 614
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTllrCINLLE---QPEAGtirvgDITIDTaRSLSQQKGliRQLRQHVGFVFQNFNLFPhRTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGLDKYDDDMVQNSAKLANAHTfimndttdgynTNVGEKGSQ------MSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:PRK11264 103 LENIIEGPVIVKGEPKEEATARARELL-----------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 689 TSALDAESEHTVQEAISKNLKGK-TVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
536-741 |
7.69e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.76 E-value: 7.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVLY----A 611
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSfefdV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RSVTEnIGY--------GLDKYDDDMVQNSAKLANAHTFIMNDTTdgyntnvgekgsQMSGGQKQRIAIARALVRQPVVL 683
Cdd:PRK09536 95 RQVVE-MGRtphrsrfdTWTETDRAAVERAMERTGVAQFADRPVT------------SLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 684 LLDEATSALDAesEHTVQE-AISKNL--KGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:PRK09536 162 LLDEPTASLDI--NHQVRTlELVRRLvdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
522-739 |
8.05e-22 |
|
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: 100.14 E-value: 8.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIR--------PDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyePTSGEVLIDGVPVRE 590
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglALLRLI----PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 591 YDHK---FLHTKVALVGQEPvlYA-----RSVTENIGYGLDKYDDDM--VQNSAKLANA---------------HTFimn 645
Cdd:COG4172 352 LSRRalrPLRRRMQVVFQDP--FGslsprMTVGQIIAEGLRVHGPGLsaAERRARVAEAleevgldpaarhrypHEF--- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 646 dttdgyntnvgekgsqmSGGQKQRIAIARALVRQPVVLLLDEATSALDAesehTVQEAISKNLK------GKTVILIAHR 719
Cdd:COG4172 427 -----------------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQAQILDLLRdlqrehGLAYLFISHD 485
|
250 260
....*....|....*....|..
gi 17511077 720 LSTVEN-ADKIVVINKGK-VEQ 739
Cdd:COG4172 486 LAVVRAlAHRVMVMKDGKvVEQ 507
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-490 |
1.00e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 96.39 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 202 WKYYGMAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMG--MLSLASTVFGGLRGGSftYAHATIDRQI 279
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPG-TLDGLTGFILLYLglILIQALSVFLFIRLAG--KIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 280 RNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFL 359
Cdd:cd18540 78 RKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 360 VNKIFgvwydmlseetQNSVAKAN-DVAE----------EVLSSIRTVKSFACENYESSRFMtflNVTLKIATRKV---- 424
Cdd:cd18540 158 VSIYF-----------QKKILKAYrKVRKinsritgafnEGITGAKTTKTLVREEKNLREFK---ELTEEMRRASVraar 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 425 -----FVVIGLIWSnellqMGiLTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQA 490
Cdd:cd18540 224 lsalfLPIVLFLGS-----IA-TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSA 288
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
538-750 |
1.06e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.53 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVreyDHKFLHTKVAL-VG---QEPVLYAR- 612
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMHKRARLgIGylpQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGLDKYDDDMVQNSAKLanahtfimNDTTDGYN--TNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:cd03218 91 TVEENILAVLEIRGLSKKEREEKL--------EELLEEFHitHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 691 ALDAESEHTVQEAIsKNLKGKTV-ILIA-HRLS-TVENADKIVVINKGKVEQLGNHKTLMEQE 750
Cdd:cd03218 163 GVDPIAVQDIQKII-KILKDRGIgVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
518-752 |
1.24e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYpiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK13647 1 MDNIIEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEP--VLYARSVTENIGYG-----LDKYD-DDMVQNSAKLANahtfiMNDTTDgyntnvgEKGSQMSGGQKQR 669
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEvERRVEEALKAVR-----MWDFRD-------KPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 670 IAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLS-TVENADKIVVINKGKV-----EQLGN 742
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVlaegdKSLLT 226
|
250
....*....|
gi 17511077 743 HKTLMEQEGL 752
Cdd:PRK13647 227 DEDIVEQAGL 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
533-732 |
1.35e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 533 IRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEP---TSGEVLIDGVPVREYdhKFLHTKVALVGQEPVL 609
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL--PAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 YAR-SVTENIGYGLDkydddmvqNSAKLANAHTFIMNDTTDgyntnVGEKG------SQMSGGQKQRIAIARALVRQPVV 682
Cdd:COG4136 88 FPHlSVGENLAFALP--------PTIGRAQRRARVEQALEE-----AGLAGfadrdpATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 683 LLLDEATSALDAE-----SEHTVQEAISKNLkgkTVILIAHRLSTVENADKIVVI 732
Cdd:COG4136 155 LLLDEPFSKLDAAlraqfREFVFEQIRQRGI---PALLVTHDEEDAPAAGRVLDL 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
517-798 |
1.36e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 517 GMTGKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHkFL 596
Cdd:PRK13537 3 MSVAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQ----EPVLyarSVTENIG-----YGLDKYD-DDMVQ---NSAKLANAHtfimndttdgyNTNVGEkgsqMS 663
Cdd:PRK13537 79 RQRVGVVPQfdnlDPDF---TVRENLLvfgryFGLSAAAaRALVPpllEFAKLENKA-----------DAKVGE----LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 742 NHKTLMEQE-----------------GLYKQLVQRQMMSGEDgLDDEIEEPEP--AREGGsgrstRAGARRIRSPS 798
Cdd:PRK13537 221 APHALIESEigcdvieiygpdpvalrDELAPLAERTEISGET-LFCYVRDPEPlhARLKG-----RAGLRYLHRPA 290
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
536-777 |
1.75e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVL-YARSV 614
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGLDKY---------DDDMVQNSAklanahtfiMNDTtdGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:PRK11231 94 RELVAYGRSPWlslwgrlsaEDNARVNQA---------MEQT--RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 686 DEATSALD----AESEHTVQEAiskNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMeQEGLYKQLVQrq 760
Cdd:PRK11231 163 DEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM-TPGLLRTVFD-- 236
|
250
....*....|....*..
gi 17511077 761 mmsgedgLDDEIeEPEP 777
Cdd:PRK11231 237 -------VEAEI-HPEP 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
518-737 |
2.16e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.41 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPI-RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD---- 592
Cdd:PRK10535 1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 593 ---------------HKFLHTKVALVGQEPVLYArsvtenigyGLDKydddmvqnSAKLANAHTFImndTTDGYNTNVGE 657
Cdd:PRK10535 81 aqlrrehfgfifqryHLLSHLTAAQNVEVPAVYA---------GLER--------KQRLLRAQELL---QRLGLEDRVEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 658 KGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQeAISKNL--KGKTVILIAHRLSTVENADKIVVINKG 735
Cdd:PRK10535 141 QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM-AILHQLrdRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
..
gi 17511077 736 KV 737
Cdd:PRK10535 220 EI 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
541-746 |
2.31e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 541 EDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDG-VPVREyDHKFLHtKVALV-GQE-------PVL-- 609
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKR-RKEFAR-RIGVVfGQRsqlwwdlPAIds 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 --YARSVtenigYGLDkyDDDMVQNSAKLANahtfiMNDTTDGYNTNVgekgSQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:COG4586 117 frLLKAI-----YRIP--DAEYKKRLDELVE-----LLDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 688 ATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVINKGKV----------EQLGNHKTL 746
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIiydgsleelkERFGPYKTI 252
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
509-783 |
2.70e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 100.24 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 509 NTGTYAPDGMTGKIEFRHVAFsYPIRPDLpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDgvpv 588
Cdd:PTZ00243 647 HEATPTSERSAKTPKMKTDDF-FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 589 reydhkflhTKVALVGQEPVLYARSVTENIGYgldkYDDdmvQNSAKLANAHTFI-----MNDTTDGYNTNVGEKGSQMS 663
Cdd:PTZ00243 721 ---------RSIAYVPQQAWIMNATVRGNILF----FDE---EDAARLADAVRVSqleadLAQLGGGLETEIGEKGVNLS 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAE-SEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGN 742
Cdd:PTZ00243 785 GGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17511077 743 HKTLMeQEGLYKQLVQRQMMS---GEDGLDDEIEEPEPAREGGS 783
Cdd:PTZ00243 865 SADFM-RTSLYATLAAELKENkdsKEGDADAEVAEVDAAPGGAV 907
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
542-741 |
2.95e-21 |
|
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: 93.20 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREyDHKFLHTKVALVGQEPVL-YARSVTENI-- 618
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTGWENLyi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 619 -----GYGLDKYDDdmvqnsaKLANAHTFImnDTTDGYNTNVgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:cd03265 97 harlyGVPGAERRE-------RIDELLDFV--GLLEAADRLV----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17511077 694 AESEHTVQEAISKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:cd03265 164 PQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEG 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
545-746 |
3.77e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 545 FTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDH---KFLHTKVALVGQEPvlYArSVT--ENIG 619
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNP--YG-SLNprKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 620 YGLDK-----YDDDMVQNSAKLANahtfIMndttdgynTNVGEKGSQ------M-SGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:PRK11308 113 QILEEpllinTSLSAAERREKALA----MM--------AKVGLRPEHydryphMfSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 688 ATSALDAesehTVQeAISKNLK-------GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:PRK11308 181 PVSALDV----SVQ-AQVLNLMmdlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
518-760 |
4.76e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 93.75 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIR------PDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREY 591
Cdd:COG4167 1 MSALLEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 592 DHKFLHTKVALVGQEPV--LYARSvteNIGYGLD---KYDDDMVQNSAKLANAHTF----IMNDTTDGYntnvgekgSQM 662
Cdd:COG4167 81 DYKYRCKHIRMIFQDPNtsLNPRL---NIGQILEeplRLNTDLTAEEREERIFATLrlvgLLPEHANFY--------PHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 663 -SGGQKQRIAIARALVRQPVVLLLDEATSALDAesehTVQEAISkNL-------KGKTVILIAHRLSTVEN-ADKIVVIN 733
Cdd:COG4167 150 lSSGQKQRVALARALILQPKIIIADEALAALDM----SVRSQII-NLmlelqekLGISYIYVSQHLGIVKHiSDKVLVMH 224
|
250 260
....*....|....*....|....*....
gi 17511077 734 KGKVEQLGNHKTLME--QEGLYKQLVQRQ 760
Cdd:COG4167 225 QGEVVEYGKTAEVFAnpQHEVTKRLIESH 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
535-736 |
4.94e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 535 PDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYePT---SGEVLIDGVP-----VREYDHK---FLHTKVALV 603
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEElqasnIRDTERAgiaIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 604 GQepvlyaRSVTENIGYG--------LDkyDDDMVQNSAK-LANAHTFImndttdgyntNVGEKGSQMSGGQKQRIAIAR 674
Cdd:PRK13549 95 KE------LSVLENIFLGneitpggiMD--YDAMYLRAQKlLAQLKLDI----------NPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 675 ALVRQPVVLLLDEATSALdAESEHTVQEAISKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGK 736
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAVLLDIIRDLKahGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
522-742 |
6.22e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVrEYDHKF---LHT 598
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmkLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEP--VLYARSVTENIGYGLD--KYDDDMVQNSAKLANAHTFImndttdgynTNVGEKGSQ-MSGGQKQRIAIA 673
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVnlKLPEDEVRKRVDNALKRTGI---------EHLKDKPTHcLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTVE-NADKIVVINKGKVEQLGN 742
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
540-741 |
7.11e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFL----HTKVALVGQEPVLYAR-SV 614
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGLDKYDDDMVQNSAKLANAHTFI-MNDTTDGYNtnvgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVgLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17511077 694 AESEHTVQEAISKnLKGK---TVILIAHRL-STVENADKIVVINKGKVEQLG 741
Cdd:PRK10070 197 PLIRTEMQDELVK-LQAKhqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
522-719 |
8.63e-21 |
|
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: 89.91 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVlidGVPVREydhkflhtKVA 601
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE--------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYARSVTENIGYGLDKydddmvqnsaklanahtfimndttdgyntnvgekgsQMSGGQKQRIAIARALVRQPV 681
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDD------------------------------------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKnlKGKTVILIAHR 719
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
522-737 |
9.78e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.36 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirPDLPI----MEDLTFTVEPGEVVALVGPSGGGKSSciaMLEHF---YEPTSGEVLIDGVPVR----E 590
Cdd:PRK13641 3 IKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKST---LMQHFnalLKPSSGTITIAGYHITpetgN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 591 YDHKFLHTKVALVGQ--EPVLYARSVTENIGYGLDKY--DDDMVQNSAKLANAHTfimndttdGYNTNVGEKGS-QMSGG 665
Cdd:PRK13641 78 KNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFgfSEDEAKEKALKWLKKV--------GLSEDLISKSPfELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 666 QKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEaISKNLK--GKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQkaGHTVILVTHNMDDVaEYADDVLVLEHGKL 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
522-741 |
1.14e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.41 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEpTSGEVLIDG--------VPVREYDH 593
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 KFLHTKVALVGQEPVLYARSVTENIGYGLD------KYD-DDMVQNSAKLAnahtfimnDTTDGYNTNVGEKGSQMSGGQ 666
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEiDDIVESALKDA--------DLWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 667 KQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAI-SKNLKGK-TVILIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGNENRIG 232
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
220-491 |
1.29e-20 |
|
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: 93.01 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 220 VFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNK 299
Cdd:cd18568 19 LALPLFTQIILDRVLVHK-NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 300 TGEICSRLSAD---CQTMSN-TLSLYMNVLtrnltMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEET 375
Cdd:cd18568 98 VGDIITRFQENqkiRRFLTRsALTTILDLL-----MVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 376 QNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKVFVVIGLIWSNELLQMGILTIVLWYGGHLVIE 455
Cdd:cd18568 173 FQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVIS 252
|
250 260 270
....*....|....*....|....*....|....*.
gi 17511077 456 NKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAV 491
Cdd:cd18568 253 GQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETR 288
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
522-751 |
1.66e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREyDHKFLHTKVA 601
Cdd:PRK13536 42 IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEPVLYAR-SVTENI-----GYGLDKYDDDMVQNS----AKLANAhtfimndttdgYNTNVgekgSQMSGGQKQRIA 671
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENLlvfgrYFGMSTREIEAVIPSllefARLESK-----------ADARV----SDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 672 IARALVRQPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVEN-ADKIVVINKG-KVEQLGNHKTLME 748
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHALIDE 262
|
...
gi 17511077 749 QEG 751
Cdd:PRK13536 263 HIG 265
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
522-749 |
2.09e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDL--PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREY----DHKF 595
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LHTKVALVGQ--EPVLYARSVTENIGYGLDKYDDDMvQNSAKLANAHTFIMNDTTDGYNTNVGEkgsqMSGGQKQRIAIA 673
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAREKLALVGISESLFEKNPFE----LSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEaISKNL--KGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
542-741 |
2.51e-20 |
|
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: 93.25 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVPVREYDHK-FLHT---KVALVGQEPVLYAR-S 613
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTlirLIAGLT---RPDEGEIVLNGRTLFDSRKGiFLPPekrRIGYVFQEARLFPHlS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 614 VTENIGYGLDKYDDDMVQNS-----AKLANAHTfimndttdgyntnVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISferviELLGIGHL-------------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 689 TSALDAESEHTVQ---EAISKNLkGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:TIGR02142 159 LAALDDPRKYEILpylERLHAEF-GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAG 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
522-736 |
2.52e-20 |
|
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: 87.89 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVlidgvpvreydhkflhtkva 601
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 lvgqepvlyARSVTENIGYgldkydddmvqnsaklanahtFimndttdgyntnvgekgSQMSGGQKQRIAIARALVRQPV 681
Cdd:cd03221 58 ---------TWGSTVKIGY---------------------F-----------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 682 VLLLDEATSALDAESEHTVQEAIsKNLKGkTVILIAH-R--LSTVenADKIVVINKGK 736
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
518-741 |
3.33e-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: 93.24 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVafsypiRPDLPImeDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfyePTSGEVLIDGVPVreYDHK 594
Cdd:COG4148 1 MMLEVDFRLR------RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTllrAIAGLER---PDSGRIRLGGEVL--QDSA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 595 ---FLHT---KVALVGQEPVLYA-RSVTENIGYGL-------DKYD-DDMVQ--NSAKLANAHTfimndttdgyntnvge 657
Cdd:COG4148 68 rgiFLPPhrrRIGYVFQEARLFPhLSVRGNLLYGRkrapraeRRISfDEVVEllGIGHLLDRRP---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 658 kgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQ---EAISKNLKGKtVILIAHRLSTVEN-ADKIVVIN 733
Cdd:COG4148 132 --ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDELDIP-ILYVSHSLDEVARlADHVVLLE 208
|
....*...
gi 17511077 734 KGKVEQLG 741
Cdd:COG4148 209 QGRVVASG 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
537-739 |
3.41e-20 |
|
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: 91.02 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 537 LPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD---HKFLHTKVALVGQE---PVLY 610
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 ARSVTENIGYGLDKYDDdmVQNSAKLANAHTFImnDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTS--LDESEQKARIAELL--DMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 691 ALDAESEHTVQEAISKnLK---GKTVILIAHRLSTVEN-ADKIVVINKGK-VEQ 739
Cdd:TIGR02769 180 NLDMVLQAVILELLRK-LQqafGTAYLFITHDLRLVQSfCQRVAVMDKGQiVEE 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-741 |
3.68e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAML----EHFYEP-TSGEVLIDGVPVREYDHKF 595
Cdd:PRK14247 3 KIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrliELYPEArVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 LHTKVALVGQEP-VLYARSVTENIGYGLDKydDDMVQNSAKLANAHTFIMNDTT--DGYNTNVGEKGSQMSGGQKQRIAI 672
Cdd:PRK14247 80 LRRRVQMVFQIPnPIPNLSIFENVALGLKL--NRLVKSKKELQERVRWALEKAQlwDEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAH------RLStvenaDKIVVINKGKVEQLG 741
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
538-756 |
4.75e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKF-LHTKVALVGQEP--VLYARSV 614
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYG---LDKYDDDM---VQNSAKLANahtfiMNDTTDgYNTNVgekgsqMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:PRK13633 104 EEDVAFGpenLGIPPEEIrerVDESLKKVG-----MYEYRR-HAPHL------LSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 689 TSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQL 756
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMMKKI 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
522-739 |
6.85e-20 |
|
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: 89.42 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPiRPD--LPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfyePTSGEVLIDGVPVREYDH--- 593
Cdd:COG4181 9 IELRGLTKTVG-TGAgeLTILKGISLEVEAGESVAIVGASGSGKSTllgLLAGLDR---PTSGTVRLAGQDLFALDEdar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 -KFLHTKVALVGQ-EPVLYARSVTENIGYGLD-KYDDDMVQNSAKLANAhtfimndttdgyntnVGEKG------SQMSG 664
Cdd:COG4181 85 aRLRARHVGFVFQsFQLLPTLTALENVMLPLElAGRRDARARARALLER---------------VGLGHrldhypAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 665 GQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAI-SKNLK-GKTVILIAHRLSTVENADKIVVINKGKVEQ 739
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
522-755 |
8.35e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.25 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYpiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVA 601
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQEP--VLYARSVTENIGYGLDKY--DDDMVQNSAKLAnAHTFIMNDTTDgyntnvgEKGSQMSGGQKQRIAIARALV 677
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLglDEETVAHRVSSA-LHMLGLEELRD-------RVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTV-ENADKIVVINKGKVEQLGNHKTLMEQEGLYK 754
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
.
gi 17511077 755 Q 755
Cdd:PRK13652 234 R 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
526-763 |
1.89e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 526 HVAFsyPIRPDL--------PIMEDLTFTVEPGEVVALVGPSGGGKSSC-IAMLEHFyePTSGEVLIDGVPVREYDHKFL 596
Cdd:PRK15134 282 QVAF--PIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 ---HTKVALVGQEP--VLYAR-SVTENIGYGLDKYDDDMvqNSAKLANAHTFIMN------DTTDGYNtnvgekgSQMSG 664
Cdd:PRK15134 358 lpvRHRIQVVFQDPnsSLNPRlNVLQIIEEGLRVHQPTL--SAAQREQQVIAVMEevgldpETRHRYP-------AEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 665 GQKQRIAIARALVRQPVVLLLDEATSALDaeseHTVQEAISKNLKG------KTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEV 504
|
250 260
....*....|....*....|....*.
gi 17511077 738 EQLGNHKTLMEQEglyKQLVQRQMMS 763
Cdd:PRK15134 505 VEQGDCERVFAAP---QQEYTRQLLA 527
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
536-742 |
2.08e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYE------PTSGEVLIDGVPVREYDHKFLHTKVALVGQEPVL 609
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 YAR-SVTENIGYGLDKY---DDDMVQNSAKLANAHTFIMNDTTDGYNTnvgeKGSQMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:PRK14246 102 FPHlSIYDNIAYPLKSHgikEKREIKKIVEECLRKVGLWKEVYDRLNS----PASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 686 DEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGN 742
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
539-741 |
2.21e-19 |
|
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: 87.71 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHFYEPTSGEVLIDGVPVREydHKFLHtKVALVGQEPVLYAR-SV 614
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGL---------DKYDDDMVQNSAKLANAHTFIMNDttdgyntnvgeKGSQMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:cd03234 99 RETLTYTAilrlprkssDAIRKKRVEDVLLRDLALTRIGGN-----------LVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 686 DEATSALDAESEHTVQEAISKNLK-GKTVILIAH--RLSTVENADKIVVINKGKVEQLG 741
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
522-760 |
2.50e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYpiRPDLPI----MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIdGVPV-----REYD 592
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 593 HKFLHTKVALVGQ--EPVLYARSVTENIGYGLDKY---DDDMVQNSAKLANahtfimndtTDGYNTNVGEKGS-QMSGGQ 666
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFgvsEEDAKQKAREMIE---------LVGLPEELLARSPfELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 667 KQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGN- 742
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTp 230
|
250 260 270
....*....|....*....|....*....|
gi 17511077 743 -----HKTLMEQEGL-------YKQLVQRQ 760
Cdd:PRK13634 231 reifaDPDELEAIGLdlpetvkFKRALEEK 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
535-732 |
3.63e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 535 PDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhkflHTKVALVGQE-------P 607
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevpdslP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 608 VLYARSVTenIGY--------GLDKYDDDMVQNS------AKLANAhtfimndttdgyntNVGEkgsqMSGGQKQRIAIA 673
Cdd:NF040873 72 LTVRDLVA--MGRwarrglwrRLTRDDRAAVDDAlervglADLAGR--------------QLGE----LSGGQRQRALLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 674 RALVRQPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVENADKIVVI 732
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
540-729 |
4.13e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.52 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYE-----PTSGEVLIDGVPV--REYDHKFLHTKVALVGQEPVLYAR 612
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGL------DKYD-DDMVQNSAKLANahtfIMNDTTDG-YNTNVGekgsqMSGGQKQRIAIARALVRQPVVLL 684
Cdd:PRK14239 101 SIYENVVYGLrlkgikDKQVlDEAVEKSLKGAS----IWDEVKDRlHDSALG-----LSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17511077 685 LDEATSALDAESEHTVQEAISkNLKGKTVILIAHRlsTVENADKI 729
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLL-GLKDDYTMLLVTR--SMQQASRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
518-737 |
5.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEP--VLYARSVTENIGYGLDKYD---DDMVQNSAKLANAHTFIMNDTtdgyntnvgEKGSQMSGGQKQRIAI 672
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMENQGiprEEMIKRVDEALLAVNMLDFKT---------REPARLSGGQKQRVAV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 673 ARALVRQPVVLLLDEATSALDAESEHTVQEAISKnLKGK---TVILIAHRLSTVENADKIVVINKGKV 737
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
545-736 |
5.63e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 545 FTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVP--------------VREYDHKFLHTKVALVgqEPVLY 610
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiarmgvVRTFQHVRLFREMTVI--ENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 A--RSVTENIGYGLDKYDDDMVQNSAKLANAHTFI--MNdTTDGYNTNVGekgsQMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:PRK11300 104 AqhQQLKTGLFSGLLKTPAFRRAESEALDRAATWLerVG-LLEHANRQAG----NLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17511077 687 EATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTVEN-ADKIVVINKGK 736
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
538-735 |
1.05e-18 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.90 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhkflhtKVALVGQEPVLYARSVTEN 617
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGYGL--DKYDDDMVQNSAKLANAHTFIMNDTtdgyNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAE 695
Cdd:TIGR01271 507 IIFGLsyDEYRYTSVIKACQLEEDIALFPEKD----KTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17511077 696 SEHTVQEA-ISKNLKGKTVILIAHRLSTVENADKIVVINKG 735
Cdd:TIGR01271 583 TEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
522-754 |
1.55e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYpiRPDLPIME----DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV----REYDH 593
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 KFLHTKVALVGQEP--VLYARSVTENIGYGLDKYDddMVQNSAKLANAHTFIMNdttdGYNTNVGEKGS-QMSGGQKQRI 670
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFG--IPKEKAEKIAAEKLEMV----GLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAI-SKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLME 748
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFeSIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
....*.
gi 17511077 749 QEGLYK 754
Cdd:PRK13643 234 EVDFLK 239
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
246-497 |
2.37e-18 |
|
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: 86.39 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 246 TVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDL----FRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLY 321
Cdd:cd18546 37 VLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLrlrvFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 322 MNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFAC 401
Cdd:cd18546 117 LVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 402 ENYESSRFmTFLNVTLKIATRKVFVVIGLIWSN-ELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLREL 480
Cdd:cd18546 197 ERRNAERF-AELSDDYRDARLRAQRLVAIYFPGvELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQL 275
|
250
....*....|....*..
gi 17511077 481 GEVWNGLMQAVGASRKV 497
Cdd:cd18546 276 SQVFDSYQQARAALEKI 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
522-738 |
2.75e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIdGVPVRE-Y---DHKFLH 597
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgYfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKvalvgqepvlyaRSVTENIGYGLDkyDDDMVQNSAKLAN-------AHTFImndttdgyntnvgekgSQMSGGQKQRI 670
Cdd:COG0488 392 PD------------KTVLDELRDGAP--GGTEQEVRGYLGRflfsgddAFKPV----------------GVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLKGkTVILIAH-R--LSTVenADKIVVINKGKVE 738
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
536-737 |
3.04e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.73 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfYEPTSGEVLID---------------------------- 584
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDgedilelspderaragiflafqypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 585 GVPVREydhkFLHTKVALVGQEPvLYARSVTENIGYGLD--KYDDDMVQNSAklanahtfimndttdgyntNVGekgsqM 662
Cdd:COG0396 91 GVSVSN----FLRTALNARRGEE-LSAREFLKLLKEKMKelGLDEDFLDRYV-------------------NEG-----F 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 663 SGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAH--RLSTVENADKIVVINKGKV 737
Cdd:COG0396 142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRI 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
534-718 |
3.14e-18 |
|
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: 83.56 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV---REYDHKFLHTKVALVGQEPVLy 610
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYLGHLPGLKPEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 arSVTENIGY--GLDKYDDDMVQNSAKLANahtfiMNDTTDgynTNVGekgsQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:TIGR01189 89 --SALENLHFwaAIHGGAQRTIEDALAAVG-----LTGFED---LPAA----QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 17511077 689 TSALDAESEHTVQEAISKNL-KGKTVILIAH 718
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLaRGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
534-718 |
4.12e-18 |
|
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: 83.31 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREyDHKFLHTKVALVGQEPVLYAR- 612
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGLDKYDDDMVQNSakLANAHTFIMNDTTDGyntnvgekgsQMSGGQKQRIAIARALVRQPVVLLLDEATSAL 692
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEA--LARVGLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 17511077 693 DAESEHTVQEAISKNL-KGKTVILIAH 718
Cdd:cd03231 157 DKAGVARFAEAMAGHCaRGGMVVLTTH 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
538-735 |
5.92e-18 |
|
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: 84.91 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhkflhtKVALVGQEPVLYARSVTEN 617
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGYGL--DKYDDDMVQNSAKLA-NAHTFIMNDttdgyNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDA 694
Cdd:cd03291 118 IIFGVsyDEYRYKSVVKACQLEeDITKFPEKD-----NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17511077 695 ESEHTVQEA-ISKNLKGKTVILIAHRLSTVENADKIVVINKG 735
Cdd:cd03291 193 FTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
540-720 |
1.05e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHFYEP--TSGEVL----------IDGVPVREydhkflhtKVALVG 604
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTfhgknlyapdVDPVEVRR--------RIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 605 QEPVLYARSVTENIGYG--LDKYDDDM---VQNSAKLAnahtFIMNDTTDGYNTNvgekGSQMSGGQKQRIAIARALVRQ 679
Cdd:PRK14243 98 QKPNPFPKSIYDNIAYGarINGYKGDMdelVERSLRQA----ALWDEVKDKLKQS----GLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17511077 680 PVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRL 720
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
540-749 |
1.09e-17 |
|
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: 87.17 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLI----DGVPVRE--YDHKFLHTK-VALVGQEPVLYA- 611
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgPDGRGRAKRyIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RSVTENI--GYGLDKYDDdmvqnSAKLANAHTFIMNDTTDGYNTNVGEK-GSQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:TIGR03269 380 RTVLDNLteAIGLELPDE-----LARMKAVITLKMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 689 TSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
518-737 |
1.13e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD----H 593
Cdd:PRK15439 8 APPLLCARSISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakaH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 KFlhtKVALVGQEPVLYAR-SVTENIGYGLDKYDDDMVQNSAKLANAhtfimndttdGYNTNVGEKGSQMSGGQKQRIAI 672
Cdd:PRK15439 85 QL---GIYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAAL----------GCQLDLDSSAGSLEVADRQIVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 673 ARALVRQPVVLLLDEATSALD-AESEHTVQEAISKNLKGKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
522-720 |
1.55e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 82.83 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSypiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAML--EHFyePTSGEVLI------DGVPVREydh 593
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgDLP--PTYGNDVRlfgerrGGEDVWE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 kfLHTKVALVGQEPVL-YARSVT-ENI---GY----GL-DKYDDDMVQNS---------AKLANaHTFimndttdgyntn 654
Cdd:COG1119 76 --LRKRIGLVSPALQLrFPRDETvLDVvlsGFfdsiGLyREPTDEQRERArellellglAHLAD-RPF------------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 655 vgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRL 720
Cdd:COG1119 141 -----GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHV 203
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
209-466 |
1.64e-17 |
|
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: 83.71 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 209 FFFLFCYSLSRVFIPYYTGEVVTAVFGDKaSYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVV 288
Cdd:cd18555 8 LLLSLLLQLLTLLIPILTQYVIDNVIVPG-NLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 289 KQEIGFFDMNKTGEICSRLSADC---QTMSNTL-SLYMNVLtrnltMLFGSLIFMFTLSWKLSMITL----INIPIIFLV 360
Cdd:cd18555 87 KLPYSFFENRSSGDLLFRANSNVyirQILSNQViSLIIDLL-----LLVIYLIYMLYYSPLLTLIVLllglLIVLLLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 361 NKIfgvwYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYE----SSRFMTFLNVTLKIAtrKVFVVIGLIwsNEL 436
Cdd:cd18555 162 RKK----IKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIykkwENLFKKQLKAFKKKE--RLSNILNSI--SSS 233
|
250 260 270
....*....|....*....|....*....|
gi 17511077 437 LQMGILTIVLWYGGHLVIENKVESGLLVSF 466
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLGELIAF 263
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
539-737 |
1.82e-17 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 82.19 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV-REYDHKFLHTKVALV--GQE--PVLyarS 613
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGIAYVpqGREifPRL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 614 VTENIGYGLdkydddmvqnsAKLANAHTFIMNDTTDGY---NTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:TIGR03410 92 VEENLLTGL-----------AALPRRSRKIPDEIYELFpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17511077 691 ALDAESEHTVQEAISK--NLKGKTVILIAHRLS-TVENADKIVVINKGKV 737
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRV 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
536-748 |
2.02e-17 |
|
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: 86.39 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHF--YEPTSGEVLI----------------DGVPVREYDHKFLH 597
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGEPCPVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVLYARsVTENIGYGLDK----YDDDMVqnsakLANahtfIMNDTTD-GYN--------------TNVGEK 658
Cdd:TIGR03269 92 EEVDFWNLSDKLRRR-IRKRIAIMLQRtfalYGDDTV-----LDN----VLEALEEiGYEgkeavgravdliemVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 659 ----GSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTVEN-ADKIVV 731
Cdd:TIGR03269 162 ithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIW 241
|
250
....*....|....*..
gi 17511077 732 INKGKVEQLGNHKTLME 748
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVA 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
518-739 |
2.27e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAfsypIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKS-SCIAMLEHF---YEPTSGEVLIDGVPVREYDH 593
Cdd:PRK10418 1 MPQQIELRNIA----LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 594 KflHTKVALVGQEP----------------VLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFimndttdgyntnvge 657
Cdd:PRK10418 77 R--GRKIATIMQNPrsafnplhtmhthareTCLALGKPADDATLTAALEAVGLENAARVLKLYPF--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 658 kgsQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVINK 734
Cdd:PRK10418 140 ---EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSH 216
|
....*.
gi 17511077 735 GK-VEQ 739
Cdd:PRK10418 217 GRiVEQ 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
540-763 |
2.96e-17 |
|
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: 85.65 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYE--PTSGEVLIDGVP-----VREYDHK---FLHTKVALVgqePVL 609
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPlkasnIRDTERAgivIIHQELTLV---PEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 yarSVTENIGYGLD-------KYDDDMVQNSAKL-ANAHTFIMNDTTDgyntnVGEKGsqmsGGQKQRIAIARALVRQPV 681
Cdd:TIGR02633 94 ---SVAENIFLGNEitlpggrMAYNAMYLRAKNLlRELQLDADNVTRP-----VGDYG----GGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 682 VLLLDEATSALdAESEHTVQEAISKNLKGKTV--ILIAHRLSTVEN-ADKIVVINKGkvEQLGNHK-TLMEQEGLYKQLV 757
Cdd:TIGR02633 162 LLILDEPSSSL-TEKETEILLDIIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDG--QHVATKDmSTMSEDDIITMMV 238
|
....*.
gi 17511077 758 QRQMMS 763
Cdd:TIGR02633 239 GREITS 244
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
538-737 |
3.24e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAML--EHFYEPTSGEVLIDGVPvreydhkflhtkvalVGQEpvlyaRSVT 615
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQ---------------FGRE-----ASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGYGLDKYDDDMVQNSAKLANAHTFImndttdgyntnvgEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAE 695
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAVGLSDAVLWL-------------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17511077 696 SEHTVQEAISKNLK--GKTVILIAHRlSTVENA---DKIVVINKGKV 737
Cdd:COG2401 171 TAKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGV 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
209-466 |
3.49e-17 |
|
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: 83.03 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 209 FFFLFCYSLSRVFIPYYTGEVVTAVFGdKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVV 288
Cdd:cd18782 8 LALSFVVQLLGLANPLLFQVIIDKVLV-QQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 289 KQEIGFFDMNKTGEICSRLSaDCQTMSN-----TLSLYMNVLtrnltMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKI 363
Cdd:cd18782 87 RLPLGFFDKRPVGELSTRIS-ELDTIRGfltgtALTTLLDVL-----FSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 364 FGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIATRKvfVVIGLIWSN--ELLQMGI 441
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKL--TVLGTTSGSlsQFLNKLS 238
|
250 260
....*....|....*....|....*
gi 17511077 442 LTIVLWYGGHLVIENKVESGLLVSF 466
Cdd:cd18782 239 SLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
538-739 |
4.27e-17 |
|
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: 85.12 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKS----SCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHT----KVALVGQEPV- 608
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 ----LY--ARSVTENIG--YGLDKYDD--------DMVQ--NSAKLANA--HtfimndttdgyntnvgekgsQMSGGQKQ 668
Cdd:COG4172 104 slnpLHtiGKQIAEVLRlhRGLSGAAAraralellERVGipDPERRLDAypH--------------------QLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAesehTVQEAISKNLK------GKTVILIAHRLSTVEN-ADKIVVINKGK-VEQ 739
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDV----TVQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRVAVMRQGEiVEQ 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
539-741 |
5.10e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.55 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEhfyEPTSGEVLIDGVP---VREYDH----------KFLHTKVAL 602
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLE---KPSEGSIVVNGQTinlVRDKDGqlkvadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VGQEPVLYAR-SVTENIG------YGLDKYDddmVQNSAKLANAHTFIMNDTTDGYNtnvgekgSQMSGGQKQRIAIARA 675
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMeapiqvLGLSKQE---ARERAVKYLAKVGIDERAQGKYP-------VHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLG 741
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
518-736 |
5.78e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYP-IRPdlpiMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVReydhkFL 596
Cdd:PRK11288 1 SSPYLSFDGIGKTFPgVKA----LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-----FA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTK------VALVGQE----PVLyarSVTENIGYGldkydddmvqnsaKLANAHTFI----MNDTTDGYNTNVGE----- 657
Cdd:PRK11288 72 STTaalaagVAIIYQElhlvPEM---TVAENLYLG-------------QLPHKGGIVnrrlLNYEAREQLEHLGVdidpd 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 658 -KGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDA-ESEHTVqeAISKNLK--GKTVILIAHRLSTV-ENADKIVVI 732
Cdd:PRK11288 136 tPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF--RVIRELRaeGRVILYVSHRMEEIfALCDAITVF 213
|
....
gi 17511077 733 NKGK 736
Cdd:PRK11288 214 KDGR 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
524-737 |
5.88e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 524 FRHVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD---HKFLHTKV 600
Cdd:PRK10419 13 YAHGGLSGK-HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALVGQEP---VLYARSVTENIG------YGLDKydddmvqnSAKLANAHTfiMNDTTDGYNTNVGEKGSQMSGGQKQRIA 671
Cdd:PRK10419 92 QMVFQDSisaVNPRKTVREIIReplrhlLSLDK--------AERLARASE--MLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 672 IARALVRQPVVLLLDEATSALDAesehTVQEAISKNLK------GKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDL----VLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
534-741 |
5.93e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEhFYEPT----SGEVLIDGVPVreyDHKFLHTKVALVGQEPVL 609
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 yarsvtenIGYgLDKYDDDMVQNSAKLANAHTF---------IMNDT--TDGYNTNVGEKGSQ--MSGGQKQRIAIARAL 676
Cdd:TIGR00955 111 --------IPT-LTVREHLMFQAHLRMPRRVTKkekrervdeVLQALglRKCANTRIGVPGRVkgLSGGERKRLAFASEL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 677 VRQPVVLLLDEATSALDAESEHTVQEAIsKNL--KGKTVILIAHRLST--VENADKIVVINKGKVEQLG 741
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVL-KGLaqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLG 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
525-752 |
6.17e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 525 RHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVG 604
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 605 QE-PVLYARSVTENIGYG-------LDKY---DDDMVQNSAKLAN----AHTFImndttdgyntnvgekgSQMSGGQKQR 669
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGrypwhgaLGRFgaaDREKVEEAISLVGlkplAHRLV----------------DSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 670 IAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
....*.
gi 17511077 747 MEQEGL 752
Cdd:PRK10575 236 MRGETL 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
539-757 |
9.05e-17 |
|
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: 81.44 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCI-AMLEHFYepTSGEVLIDGV-----PVREYDHKFlhtkvALVGQEPVLYAR 612
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLsAFLRLLN--TEGDIQIDGVswnsvPLQKWRKAF-----GVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIG-YGldKYDDDMVQNSAKLANAHTFImNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSA 691
Cdd:cd03289 92 TFRKNLDpYG--KWSDEEIWKVAEEVGLKSVI-EQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 692 LDAESEHTVQEAISKNLKGKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQLV 757
Cdd:cd03289 169 LDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
539-747 |
1.32e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKflhTKVALVGQE--------PVLY 610
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA---AKAELRNQKlgfiyqfhHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 ARSVTENIGYGL--DKYDDDMVQNSAKLANAHTfimndttdGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:PRK11629 101 DFTALENVAMPLliGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 689 TSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVENADKIVVINKGkveQLGNHKTLM 747
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDG---RLTAELSLM 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
539-750 |
1.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEV----------------LIDGVPVREYDHKFLHTKVAL 602
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhelITNPYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VGQEP--VLYARSVTENIGYG-----LDKYDddmvqnSAKLANAHTFIMNDTTDGYNTNVGEkgsqMSGGQKQRIAIARA 675
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpvalgVKKSE------AKKLAKFYLNKMGLDDSYLERSPFG----LSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 676 LVRQPVVLLLDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLSTV-ENADKIVVINKGKVEQLGN-HKTLMEQE 750
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTpYEIFTDQH 268
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
541-737 |
3.23e-16 |
|
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: 77.47 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 541 EDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFLHTKVALV----GQEPVLYARSVT 615
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVpedrKREGLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGYGldkydddmvqnsaklanahtfimndttdgyntnvgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAE 695
Cdd:cd03215 97 ENIALS--------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17511077 696 SEHTVQEAISK-NLKGKTVILIAHRLSTV-ENADKIVVINKGKV 737
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
534-742 |
3.80e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVGQEPV--LYA 611
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStsLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RsvtENIGYGLD---KYDDDMVQNSAKLANAHTF----IMNDTTDGYNtnvgekgSQMSGGQKQRIAIARALVRQPVVLL 684
Cdd:PRK15112 103 R---QRISQILDfplRLNTDLEPEQREKQIIETLrqvgLLPDHASYYP-------HMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 685 LDEATSALDAESEHTV-------QEAisknlKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGN 742
Cdd:PRK15112 173 ADEALASLDMSMRSQLinlmlelQEK-----QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
246-490 |
6.57e-16 |
|
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: 79.08 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 246 TVFIMGML--SLASTVFGGLRggSFTYAHAT--IDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLsadcQTMSN----- 316
Cdd:cd18588 42 DVLAIGLLvvALFEAVLSGLR--TYLFSHTTnrIDAELGARLFRHLLRLPLSYFESRQVGDTVARV----RELESirqfl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 317 TLSLYMNVLTRNLTMLFgsLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTV 396
Cdd:cd18588 116 TGSALTLVLDLVFSVVF--LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 397 KSFACENYESSRFMTFLNVTLKiATRKVfVVIGLIWSN--ELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLYQFQLG 474
Cdd:cd18588 194 KSLAVEPQFQRRWEELLARYVK-ASFKT-ANLSNLASQivQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVS 271
|
250
....*....|....*.
gi 17511077 475 ENLRELGEVWNGLMQA 490
Cdd:cd18588 272 QPVLRLVQLWQDFQQA 287
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
539-750 |
7.11e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 7.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTKVALVG-----------QEP 607
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAqnattpgditvQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 608 VLYARSVTENIGYGLDKYDDDMVqNSAKLANAHTFIMNDTTDgyntnvgekgsQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAV-TKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 688 ATSALDAESEHTVQEAISK--NLKGKTVILIAHRLS-TVENADKIVVINKGKVEQLGNHKTLMEQE 750
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
536-752 |
7.87e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVrEYDHK---FLHTKVALVGQEPvlyar 612
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 svTENIGYglDKYDDDMVQNSAKLANAHTFIMNDTTDGYNTNVGEKGSQ-----MSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:PRK13638 87 --EQQIFY--TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 688 ATSALDAESEhTVQEAISKNL--KGKTVILIAHRLSTV-ENADKIVVINKGKVEQLGN------HKTLMEQEGL 752
Cdd:PRK13638 163 PTAGLDPAGR-TQMIAIIRRIvaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGApgevfaCTEAMEQAGL 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
522-737 |
2.05e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYpiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV---REYDHKFLHT 598
Cdd:PRK10908 2 IRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEP-VLYARSVTENIGYGL----DKYDDDMVQNSAKLANAHTFimnDTTDGYNTnvgekgsQMSGGQKQRIAIA 673
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVAIPLiiagASGDDIRRRVSAALDKVGLL---DKAKNFPI-------QLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 674 RALVRQPVVLLLDEATSALD-AESEHTVQEAISKNLKGKTVILIAHRLSTVENAD-KIVVINKGKV 737
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
533-717 |
3.01e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 533 IRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKflhTKVALVGQ----EPV 608
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA---EACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 LyarSVTENIGYGLDKYDDDMVQNSAKLAnahTFIMNDTTD---GYntnvgekgsqMSGGQKQRIAIARALVRQPVVLLL 685
Cdd:PRK13539 88 L---TVAENLEFWAAFLGGEELDIAAALE---AVGLAPLAHlpfGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 17511077 686 DEATSALDAESEHTVQEAISKNLKGKTVILIA 717
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
518-735 |
3.68e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIrpdLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKfLH 597
Cdd:PRK09700 2 ATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TK--VALVGQE-PVLYARSVTEN--IG-------YGLDKYDDDMVQNSAKlanahtfIMNDTTdGYNTNVGEKGSQMSGG 665
Cdd:PRK09700 78 AQlgIGIIYQElSVIDELTVLENlyIGrhltkkvCGVNIIDWREMRVRAA-------MMLLRV-GLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 666 QKQRIAIARALVRQPVVLLLDEATSAL-DAESEHTVqeAISKNLK--GKTVILIAHRLSTV-ENADKIVVINKG 735
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRkeGTAIVYISHKLAEIrRICDRYTVMKDG 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
536-737 |
5.49e-15 |
|
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: 75.02 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHfyePTSGEVLIDGVPVREYD-HKFLHTKVALVGQEPVLYA 611
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkAISGLLP---PRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 R-SVTENI---GYGLDKYDD-----DMVqnsaklanahtfimndttdgYNT--NVGE----KGSQMSGGQKQRIAIARAL 676
Cdd:COG0410 92 SlTVEENLllgAYARRDRAEvradlERV--------------------YELfpRLKErrrqRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 677 VRQPVVLLLDEATSALdaeSEHTVQE--AISKNLK--GKTVILI---AHRLSTVenADKIVVINKGKV 737
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEEifEIIRRLNreGVTILLVeqnARFALEI--ADRAYVLERGRI 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
533-718 |
5.90e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 533 IRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFlHTKVALVGQEPVLYAR 612
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 -SVTENIGYGL---DKYDDDMVQNSakLAnahtfimndttdgyntNVGEKG------SQMSGGQKQRIAIARALVRQPVV 682
Cdd:PRK13538 89 lTALENLRFYQrlhGPGDDEALWEA--LA----------------QVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 17511077 683 LLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAH 718
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAeQGGMVILTTH 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
540-786 |
6.56e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLhtkVALVGQE-------PVLYAR 612
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTE----NIGYGLDKYDDDMVQNSAKLANAhtfimnDTTDGYNTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:PRK15056 100 VVMMgrygHMGWLRRAKKRDRQIVTAALARV------DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 689 TSALDAESEHTVQeAISKNLK--GKTVILIAHRLSTVENADKIVVINKGKVEQLGNHKTLMEQEGLYKQL--VQRQMM-- 762
Cdd:PRK15056 170 FTGVDVKTEARII-SLLRELRdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFsgVLRHVAln 248
|
250 260
....*....|....*....|....
gi 17511077 763 SGEDGLDDEIEEPEPAREGGSGRS 786
Cdd:PRK15056 249 GSEESIITDDERPFISHRPAAVQR 272
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
538-739 |
7.83e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKS-SCIAMLEHFYEP----TSGEVLIDGVPVREYDHKFLH----TKVALVGQEPV 608
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 lyarsVTENIGYGLDK--YDDDMVQNSAKLANAHTFIMN--DTTDGYN--TNVGEKGSQMSGGQKQRIAIARALVRQPVV 682
Cdd:PRK15134 103 -----VSLNPLHTLEKqlYEVLSLHRGMRREAARGEILNclDRVGIRQaaKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 683 LLLDEATSALDAesehTVQEAISKNLK------GKTVILIAHRLSTVEN-ADKIVVINKGK-VEQ 739
Cdd:PRK15134 178 LIADEPTTALDV----SVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRcVEQ 238
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
269-590 |
1.90e-14 |
|
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: 77.15 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 269 TYAHATIDRqIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTrNLTMLFGSLIFMFTLSWKLSM 348
Cdd:COG4615 74 RLGQHAVAR-LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQ-SVALVLGCLAYLAWLSPPLFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 349 ITLINIPI-IFLVNKIFGVWYDMLSE--ETQNSV------------------AKANDVAEEVLSsiRTVKSFACENYESS 407
Cdd:COG4615 152 LTLVLLGLgVAGYRLLVRRARRHLRRarEAEDRLfkhfrallegfkelklnrRRRRAFFDEDLQ--PTAERYRDLRIRAD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 408 RFMTFLNVTLKIAtrkVFVVIGLIwsnellqmgiltiVLWYGGHLVIENKVESGLLVSFLlyqFQLGEnLRELGEVWNGL 487
Cdd:COG4615 230 TIFALANNWGNLL---FFALIGLI-------------LFLLPALGWADPAVLSGFVLVLL---FLRGP-LSQLVGALPTL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 488 MQAVGASRKVFEF---IDRPPRVENTGTYAPDGMT-GKIEFRHVAFSYPIRPDL------PImeDLTFtvEPGEVVALVG 557
Cdd:COG4615 290 SRANVALRKIEELelaLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDegftlgPI--DLTI--RRGELVFIVG 365
|
330 340 350
....*....|....*....|....*....|...
gi 17511077 558 PSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVRE 590
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA 398
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
534-737 |
2.11e-14 |
|
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: 72.68 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHFYEPTSGEVLIDGVPVREYDHKFlHTKVALVGQE---- 606
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVSEEdvhf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 607 PVLyarSVTENIGYGLDKYDDDMVqnsaklanahtfimndttdgyntnvgeKGsqMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:cd03233 96 PTL---TVRETLDFALRCKGNEFV---------------------------RG--ISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 687 EATSALDAESEH---TVQEAISKNLKGKTVI-LIAHRLSTVENADKIVVINKGKV 737
Cdd:cd03233 144 NSTRGLDSSTALeilKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
208-491 |
2.36e-14 |
|
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: 74.57 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTA-VFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRS 286
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNAlTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 287 VVKQEIGFFDMNKTGEICSRLSADCQTMSNTLS-LYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFG 365
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSyLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 366 VWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKIAtRKVFVVIGLI-WSNELLQMGILTI 444
Cdd:cd18560 161 EWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSS-VKVQASLSLLnVGQQLIIQLGLTL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17511077 445 VLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAV 491
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
528-737 |
3.21e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 528 AFSypirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLehfyeptSGEVLIDgvpvreyDHKFLHTK---VALVG 604
Cdd:PRK11147 12 SFS-----DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLD-------DGRIIYEQdliVARLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 605 QEPvlyARSVTENI-----------GYGLDKY--------DDDMVQNSAKLANAHTFImnDTTDGY------NTNVGEKG 659
Cdd:PRK11147 73 QDP---PRNVEGTVydfvaegieeqAEYLKRYhdishlveTDPSEKNLNELAKLQEQL--DHHNLWqlenriNEVLAQLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 660 -------SQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAEsehTVQ--EAISKNLKGkTVILIAHRLSTVEN-ADKI 729
Cdd:PRK11147 148 ldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE---TIEwlEGFLKTFQG-SIIFISHDRSFIRNmATRI 223
|
....*...
gi 17511077 730 VVINKGKV 737
Cdd:PRK11147 224 VDLDRGKL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
539-737 |
3.65e-14 |
|
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: 71.79 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHF--YEPTSGEVLIDGV-----PVREYdhkflhtkvALVG-----QE 606
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditdlPPEER---------ARLGiflafQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 607 PVLYarsvtenigygldkyddDMVQNSaklanahTFIMndttdgyNTNVGekgsqMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:cd03217 86 PPEI-----------------PGVKNA-------DFLR-------YVNEG-----FSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 687 EATSALDAESEHTVQEAISKNL-KGKTVILIAH--RLSTVENADKIVVINKGKV 737
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
241-497 |
4.15e-14 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 73.99 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 241 EKLHKTVFIMGMLSLASTVFGG----LRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADC-QTMS 315
Cdd:cd18554 39 EKVYKLFTIIGIMFFIFLILRPpveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVeQTKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 316 NTLSLYMNVLtRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRT 395
Cdd:cd18554 119 FITTGLMNIW-LDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 396 VKSFACENYESSRF----MTFLNVTLKIA--TRKVFVVIgliwsNELLQMGILtIVLWYGGHLVIENKVESGLLVSFLLY 469
Cdd:cd18554 198 IKSFALEKHEQKQFdkrnGHFLTRALKHTrwNAKTFSAV-----NTITDLAPL-LVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
250 260
....*....|....*....|....*...
gi 17511077 470 QFQLGENLRELGEVWNGLMQAVGASRKV 497
Cdd:cd18554 272 MERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
552-748 |
5.89e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.57 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 552 VVALVGPSGGGKSSCIAMLEHFYE-----PTSGEVLIDGVPV--REYDHKFLHTKVALVGQEPVLYAR-SVTENIGYGLd 623
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFPHlTIYDNVAIGV- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 624 KYDDdMVQNSAKLANAHTFIMNDTT--DGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQ 701
Cdd:PRK14267 111 KLNG-LVKSKKELDERVEWALKKAAlwDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17511077 702 EAISKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLME 748
Cdd:PRK14267 190 ELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
518-742 |
7.62e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIRPDLP-------------------IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTS 578
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 579 GEVLIDGvpvreydhkflhtKVA-L----VGQEPVLYARsvtENIG-----YGLDKYD-DDMVQNSAKLANAHTFImnDT 647
Cdd:COG1134 81 GRVEVNG-------------RVSaLlelgAGFHPELTGR---ENIYlngrlLGLSRKEiDEKFDEIVEFAELGDFI--DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 648 ---TdgYntnvgekgsqmSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLSTV 723
Cdd:COG1134 143 pvkT--Y-----------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|
gi 17511077 724 EN-ADKIVVINKGKVEQLGN 742
Cdd:COG1134 210 RRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-746 |
7.70e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.82 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 517 GMTGKIEFRHVAFSYPIRPdlpimedltftvepgeVVALVGPSGGGKSSCIAMLEHFYEPTSG-----EVLIDGVPVREY 591
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 592 -DHKFLHTKVALVGQEPVLYARSVTENIGYGLDKYDDDMVQNSAKLANAHTFIMNdTTDGYNTNVGEKGSQMSGGQKQRI 670
Cdd:PRK14271 94 rDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVG-LWDAVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
521-763 |
1.12e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.81 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFRHVAFSYpiRPDLPI----MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEV--------------- 581
Cdd:PRK13651 2 QIKVKNIVKIF--NKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 582 ----LIDGVPVREYDHKF-----LHTKVALVGQ--EPVLYARSVTENI-----GYGLDKydddmvQNSAKLANAHTFIMn 645
Cdd:PRK13651 80 kekvLEKLVIQKTRFKKIkkikeIRRRVGVVFQfaEYQLFEQTIEKDIifgpvSMGVSK------EEAKKRAAKYIELV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 646 dttdGYNTNVGEKGS-QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTV 723
Cdd:PRK13651 153 ----GLDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17511077 724 -ENADKIVVINKGKVEQLGNHKTLMEQEglyKQLVQRQMMS 763
Cdd:PRK13651 229 lEWTKRTIFFKDGKIIKDGDTYDILSDN---KFLIENNMEP 266
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
543-765 |
1.23e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 543 LTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYePTSGEVLIDGVPVREYDHK-------FLHTKVALVGQEPV-----LY 610
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFAMPVfqylaLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 ARSVTEnigygLDKYDDDMVQNSAKLanahtfimnDTTDGYNTNVgekgSQMSGGQKQRIAIARALVR-------QPVVL 683
Cdd:COG4138 94 QPAGAS-----SEAVEQLLAQLAEAL---------GLEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 684 LLDEATSALDaesehTVQEAISKNL------KGKTVILIAHRLS-TVENADKIVVINKGKVEQLGNHKTLMEQEGL---Y 753
Cdd:COG4138 156 LLDEPMNSLD-----VAQQAALDRLlrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPENLsevF 230
|
250
....*....|..
gi 17511077 754 KQLVQRQMMSGE 765
Cdd:COG4138 231 GVKFRRLEVEGH 242
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
251-471 |
1.27e-13 |
|
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: 72.11 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 251 GMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSA--DCQ-TMSNTL-SLYMNVLt 326
Cdd:cd18567 49 GLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGSldEIQqTLTTGFvEALLDGL- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 327 rnltMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFaceNYES 406
Cdd:cd18567 128 ----MAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLF---GREA 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 407 SRFMTFLNVTLK-----IATRKVFVVIGLIwsNELLQMGILTIVLWYGGHLVIENKVESGLLVSFLLY--QF 471
Cdd:cd18567 201 EREARWLNLLVDainadIRLQRLQILFSAA--NGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYkdQF 270
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
522-741 |
1.38e-13 |
|
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: 70.64 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPI-------------------RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVL 582
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 583 IDGvpvreydhkflhtKVAL-----VGQEPVLyarSVTENIG-----YGLD-KYDDDMVQNSAKLAnahtfimnDTTDGY 651
Cdd:cd03220 81 VRG-------------RVSSllglgGGFNPEL---TGRENIYlngrlLGLSrKEIDEKIDEIIEFS--------ELGDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 652 NTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAI-SKNLKGKTVILIAHRLSTV-ENADKI 729
Cdd:cd03220 137 DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIkRLCDRA 212
|
250
....*....|..
gi 17511077 730 VVINKGKVEQLG 741
Cdd:cd03220 213 LVLEKGKIRFDG 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
530-792 |
1.39e-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: 74.20 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 530 SYPirPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLI-DGVpvreydhkflhtKVALVGQEPV 608
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI------------KVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 L-YARSVTENIGYG-------LDKY----------DDDMVQNSAKLANAHTFImnDTTDGYN------------------ 652
Cdd:TIGR03719 79 LdPTKTVRENVEEGvaeikdaLDRFneisakyaepDADFDKLAAEQAELQEII--DAADAWDldsqleiamdalrcppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 653 TNVgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAES----EHTVQEaisknLKGkTVILIAHRLSTVEN-AD 727
Cdd:TIGR03719 157 ADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTHDRYFLDNvAG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 728 KIVVINKGK-VEQLGNHKTLMEQEGlyKQLVQRQmmSGEDGLDDEIE-EPEPAREGGSGRSTRAGAR 792
Cdd:TIGR03719 227 WILELDRGRgIPWEGNYSSWLEQKQ--KRLEQEE--KEESARQKTLKrELEWVRQSPKGRQAKSKAR 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
538-759 |
1.52e-13 |
|
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: 75.05 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVrEYDHKFLHTKVALVGQEPVLYAR-SVTE 616
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 617 NIGYGLD----KYDDDMVQNSAklanahtfIMNDTtdGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSAL 692
Cdd:TIGR01257 1023 HILFYAQlkgrSWEEAQLEMEA--------MLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 693 DAESEHTVQEAISKNLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLME--QEGLYKQLVQR 759
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVRK 1162
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
545-737 |
2.58e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 545 FTVEPGEVVALVGPSGGGKSSciaMLEHFyeptSGevLIDGVPVREYDHKFLHTKVALVGQepvlYARSVTEN---IGYG 621
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKST---LLRHL----SG--LITGDKSAGSHIELLGRTVQREGR----LARDIRKSranTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 622 LDKYDddMVQNSAKLANA---------------HTFIMNDTTDGYN--TNVG------EKGSQMSGGQKQRIAIARALVR 678
Cdd:PRK09984 92 FQQFN--LVNRLSVLENVligalgstpfwrtcfSWFTREQKQRALQalTRVGmvhfahQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEA---ISKNlKGKTVILIAHRLS-TVENADKIVVINKGKV 737
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTlrdINQN-DGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
534-742 |
2.99e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH--------------TK 599
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 VALVGQEPVLYAR---SVTENIGYGLDKYDDdmVQNSAKLANAHTFIMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARAL 676
Cdd:PRK10261 106 MAMIFQEPMTSLNpvfTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 677 VRQPVVLLLDEATSALDAesehTVQEAISKNLK------GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGN 742
Cdd:PRK10261 184 SCRPAVLIADEPTTALDV----TIQAQILQLIKvlqkemSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
539-772 |
3.20e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV-REYDHKflHTK-VALVGQEPVL------- 609
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYK--RAKyIGRVFQDPMMgtapsmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 --------YARSVTENIGYGLDKYDDDMVQNSAKLANahtfimNDTTDGYNTNVGekgsQMSGGQKQRIAIARALVRQPV 681
Cdd:COG1101 99 ieenlalaYRRGKRRGLRRGLTKKRRELFRELLATLG------LGLENRLDTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGK--TVILIAHRLS-TVENADKIVVINKGKV--EQLGNHKTLMEQEGLYKQL 756
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRIilDVSGEEKKKLTVEDLLELF 248
|
250
....*....|....*.
gi 17511077 757 vqrQMMSGEDGLDDEI 772
Cdd:COG1101 249 ---EEIRGEELADDRL 261
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
543-752 |
3.44e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 543 LTFTVEPGEVVALVGPSGGGKS---SCIAMLehfyEPTSGEVLIDGVPVREYDHKFL-HTKVALVGQEPVLYARSV---- 614
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKStllARMAGL----LPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 615 TENIGYGLDKYDD----DMVQNSAKLanahtfimndtTDGYNTNVGekgsQMSGGQKQRIAIArALVRQ--PVV------ 682
Cdd:PRK03695 91 TLHQPDKTRTEAVasalNEVAEALGL-----------DDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwPDInpagql 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 683 LLLDEATSALDaesehTVQEAISKNL------KGKTVILIAHRLS-TVENADKIVVINKGKVEQLGNHKTLMEQEGL 752
Cdd:PRK03695 155 LLLDEPMNSLD-----VAQQAALDRLlselcqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
520-737 |
5.19e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.29 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDhkfLHtK 599
Cdd:COG1137 2 MTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---MH-K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 VALVG-----QEPVLYAR-SVTENI-----GYGLDKYD-----DDMVQ--NSAKLANAhtfimndttdgyntnvgeKGSQ 661
Cdd:COG1137 75 RARLGigylpQEASIFRKlTVEDNIlavleLRKLSKKEreerlEELLEefGITHLRKS------------------KAYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 662 MSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLKGKTV-ILIA-HR----LSTVenaDKIVVINKG 735
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKII-RHLKERGIgVLITdHNvretLGIC---DRAYIISEG 212
|
..
gi 17511077 736 KV 737
Cdd:COG1137 213 KV 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
536-749 |
1.07e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.66 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAML--EHFYEPTSGEVLIDGVPVREYD--------------------- 592
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedragegifmafqypveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 593 ---HKFLHTKVALV----GQEPvlyarsvtenigygLDKYD-DDMVQNSAKLANahtfiMNDTTDGYNTNVGekgsqMSG 664
Cdd:PRK09580 93 vsnQFFLQTALNAVrsyrGQEP--------------LDRFDfQDLMEEKIALLK-----MPEDLLTRSVNVG-----FSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 665 GQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGK-TVILIAH--RLSTVENADKIVVINKGKVEQLG 741
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSG 228
|
250
....*....|.
gi 17511077 742 NH---KTLMEQ 749
Cdd:PRK09580 229 DFtlvKQLEEQ 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
522-722 |
1.12e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIdGVPVreydhkflhtKVA 601
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQ--EPVLYARSVTENIGYGLDKYDDDMVQ-NSAKLANAHTFIMNDTtdgyntnvGEKGSQMSGGQKQRIAIARALVR 678
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLDIIKLGKREiPSRAYVGRFNFKGSDQ--------QKKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEAIsKNLKGKTVIlIAH------RLST 722
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVV-ISHdrwfldRIAT 508
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
539-737 |
1.23e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLE-HFYEP-------TSGEVLIDGVPVREYDHKFLHTKVALVGQ--EPV 608
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 lYARSVTENIGYG----------LDKYDDDMVQNSAKLANAHTFIMNDTTdgyntnvgekgsQMSGGQKQRIAIARAL-- 676
Cdd:PRK13547 96 -FAFSAREIVLLGrypharragaLTHRDGEIAWQALALAGATALVGRDVT------------TLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 677 -------VRQPVVLLLDEATSALDAESEH----TVQeAISKNLKgKTVILIAHRLS-TVENADKIVVINKGKV 737
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHrlldTVR-RLARDWN-LGVLAIVHDPNlAARHADRIAMLADGAI 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
539-750 |
1.81e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDG-----VPVreydHKFLHTKVALVGQEPVLYAR- 612
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPL----HARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGLDKYDDDMVQNSAKLANA--HTFIMNDTTDGYntnvgekGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANElmEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 691 ALDAESEHTVQEAIsKNLK--GKTVILIAHRL-STVENADKIVVINKGKVEQLGNHKTLMEQE 750
Cdd:PRK10895 167 GVDPISVIDIKRII-EHLRdsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
522-687 |
3.82e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSypiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHT--- 598
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 KVALVGQEPVLYAR-SVTENIGYGLDKYdddmVQNSAKLANAhTFIMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALV 677
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLREH----TQLPAPLLHS-TVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170
....*....|
gi 17511077 678 RQPVVLLLDE 687
Cdd:PRK11831 160 LEPDLIMFDE 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
541-761 |
3.99e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 541 EDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYePT---SGEVLIDGVPVREYDHK--------FLHTKVALVgqePVL 609
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRdsealgivIIHQELALI---PYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 yarSVTENI-------GYGLDKYDDDMVQNSAKLA------NAHTFImndttdgynTNVGEkgsqmsgGQKQRIAIARAL 676
Cdd:NF040905 94 ---SIAENIflgneraKRGVIDWNETNRRARELLAkvgldeSPDTLV---------TDIGV-------GKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 677 VRQPVVLLLDEATSAL-DAESEHTVQeaISKNLKGK--TVILIAHRLSTVEN-ADKIVVINKGK-VEQLGNHKTLMEQEG 751
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQgiTSIIISHKLNEIRRvADSITVLRDGRtIETLDCRADEVTEDR 232
|
250
....*....|
gi 17511077 752 LYKQLVQRQM 761
Cdd:NF040905 233 IIRGMVGRDL 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
519-742 |
4.48e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 519 TGKIEFRHVAFSYPIRP--DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLID--GVP-----VR 589
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPanlkkIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 590 EYdhKFLHTKVALVGQEP--VLYARSVTENIGYGLDKYDDDMVQNSAKLANahtfiMNDTTDGYNTNVGEKGSQMSGGQK 667
Cdd:PRK13645 84 EV--KRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPE-----LLKLVQLPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 668 QRIAIARALVRQPVVLLLDEATSALDAESEH---TVQEAISKNlKGKTVILIAHRLSTV-ENADKIVVINKGKVEQLGN 742
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKE-YKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
537-746 |
6.03e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 537 LPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLHTK---VALVGQEPV--LYA 611
Cdd:PRK15079 34 LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLasLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 R-SVTENIGYGLDKYDDDMVQNSAKlanahtfimnDTTDGYNTNVG-------EKGSQMSGGQKQRIAIARALVRQPVVL 683
Cdd:PRK15079 114 RmTIGEIIAEPLRTYHPKLSRQEVK----------DRVKAMMLKVGllpnlinRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 684 LLDEATSALDAesehTVQEAISKNLK------GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTL 746
Cdd:PRK15079 184 ICDEPVSALDV----SIQAQVVNLLQqlqremGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
537-718 |
1.74e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 537 LPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDH----KFLHTKVALVGQE----PV 608
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSfmliPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 LYARSVTENIGYGLDKYDDDMVQNSAKLAnahtfimndTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEA 688
Cdd:PRK10584 103 LNALENVELPALLRGESSRQSRNGAKALL---------EQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|..
gi 17511077 689 TSALDAES-EHTVQEAISKNLK-GKTVILIAH 718
Cdd:PRK10584 174 TGNLDRQTgDKIADLLFSLNREhGTTLILVTH 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
521-740 |
2.05e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFRHVAFSYP-----IRPdlpimedLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV-----RE 590
Cdd:PRK10522 322 TLELRNVTFAYQdngfsVGP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqpED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 591 YDHKF--LHTKVALVGQepvlyarsVTENIGYGLDKYDDDMVQNSAKLANAHTFimndtTDGYNTNVgekgsQMSGGQKQ 668
Cdd:PRK10522 395 YRKLFsaVFTDFHLFDQ--------LLGPEGKPANPALVEKWLERLKMAHKLEL-----EDGRISNL-----KLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17511077 669 RIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLSTVENADKIVVINKGKVEQL 740
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSEL 530
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
522-749 |
2.23e-11 |
|
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: 67.16 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPT-SGEVLIDGVPVREYD-HKFLHTK 599
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 VALVGQE-------PVLyarSVTENIGYG-LDKYDDDMVQNSA-------------KLANAHTFImndttdgyntnvgeK 658
Cdd:TIGR02633 338 IAMVPEDrkrhgivPIL---GVGKNITLSvLKSFCFKMRIDAAaelqiigsaiqrlKVKTASPFL--------------P 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 659 GSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGK 736
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGK 480
|
250
....*....|....
gi 17511077 737 VE-QLGNHKTLMEQ 749
Cdd:TIGR02633 481 LKgDFVNHALTQEQ 494
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
534-716 |
2.39e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 534 RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKflhTKVALVGQEPVLYAR- 612
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGY--GLDKYDDDMVQNSAklanahtFIMNDTTDGYNTNVgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:PRK13543 98 STLENLHFlcGLHGRRAKQMPGSA-------LAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*.
gi 17511077 691 ALDAESEHTVQEAISKNLKGKTVILI 716
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLRGGGAALV 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
535-736 |
2.84e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 535 PDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHK-FLHTKVALVGQE-PVLYAR 612
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTENIGYGldKYD-DDMVQNSAKLANAHTFIMNDTtdGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSA 691
Cdd:PRK10982 89 SVMDNMWLG--RYPtKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17511077 692 L-DAESEHTVQeaISKNLK--GKTVILIAHRLSTV-ENADKIVVINKGK 736
Cdd:PRK10982 165 LtEKEVNHLFT--IIRKLKerGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
518-737 |
2.92e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGkiefRHVAFSYPIRPDL---PIME-----------DLTFTVEPGEVVALVGPSGGGKS---SCIAMLEHfyePTSGE 580
Cdd:COG1129 236 MVG----RELEDLFPKRAAApgeVVLEveglsvggvvrDVSFSVRAGEILGIAGLVGAGRTelaRALFGADP---ADSGE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 581 VLIDGVPVReydhkfLHT-------KVALV----GQEPVLYARSVTENIGYG-LDKYDDDMVQNSAKL-ANAHTFI--MN 645
Cdd:COG1129 309 IRLDGKPVR------IRSprdairaGIAYVpedrKGEGLVLDLSIRENITLAsLDRLSRGGLLDRRRErALAEEYIkrLR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 646 DTTDGYNTNVGekgsQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKnL--KGKTVILIahrlST- 722
Cdd:COG1129 383 IKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE-LaaEGKAVIVI----SSe 453
|
250
....*....|....*....
gi 17511077 723 ----VENADKIVVINKGKV 737
Cdd:COG1129 454 lpelLGLSDRILVMREGRI 472
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
549-722 |
3.96e-11 |
|
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: 61.62 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 549 PGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIdgvpvreydhkflhtkvalvgqepvlyarsvtenigygldkyddd 628
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 629 mvqnsaklANAHTFIMNDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNL 708
Cdd:smart00382 36 --------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|.
gi 17511077 709 -------KGKTVILIAHRLST 722
Cdd:smart00382 108 llllkseKNLTVILTTNDEKD 128
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
539-736 |
1.56e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTS--GEVLIDGVPVReydhKFLHTKVALVGQEPVLYAR-SVT 615
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGY-GLDKYDDDMVQNSAKLANAHTFIMNDTTDGYNTNVGEKGSQ-MSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:PLN03211 159 ETLVFcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17511077 694 AESEHT-VQEAISKNLKGKTVILIAHRLST--VENADKIVVINKGK 736
Cdd:PLN03211 239 ATAAYRlVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
541-737 |
2.63e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 541 EDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLI---DGVPVR-----EYDHKFLH-TKVALVGQEPVLYA 611
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDlyalsEAERRRLLrTEWGFVHQHPRDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 R---SVTENIG----------YG----------------LDKYDDDmvqnsaklanAHTFimndttdgyntnvgekgsqm 662
Cdd:PRK11701 103 RmqvSAGGNIGerlmavgarhYGdiratagdwlerveidAARIDDL----------PTTF-------------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 663 SGGQKQRIAIARALVRQPVVLLLDEATSALDAesehTVQEAISKNLKGKT------VILIAHRLSTVEN-ADKIVVINKG 735
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVrelglaVVIVTHDLAVARLlAHRLLVMKQG 228
|
..
gi 17511077 736 KV 737
Cdd:PRK11701 229 RV 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
535-718 |
3.94e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 535 PDLPIMEDLTFTVEPGEVVALVGPSGGGKSSC---IAMLEHFYEptsGE-VLIDGVpvreydhkflhtKVALVGQEPVL- 609
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLlriMAGVDKEFE---GEaRPAPGI------------KVGYLPQEPQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 610 YARSVTENIGYG-------LDKY----------DDDMVQNSAKLANAHTFImnDTTDGYNTNvgekgSQM---------- 662
Cdd:PRK11819 83 PEKTVRENVEEGvaevkaaLDRFneiyaayaepDADFDALAAEQGELQEII--DAADAWDLD-----SQLeiamdalrcp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 663 ---------SGGQKQRIAIARALVRQPVVLLLDEATSALDAES----EHTVQEaisknLKGkTVILIAH 718
Cdd:PRK11819 156 pwdakvtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD-----YPG-TVVAVTH 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
540-748 |
4.39e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPV---REYDHKFLHTKVALVGQEPvlYAR-SVT 615
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDP--YASlDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGYGLDK--YDDDMVQNSAKLANAHTFImndttdgynTNVGEKGS-------QMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:PRK10261 418 QTVGDSIMEplRVHGLLPGKAAAARVAWLL---------ERVGLLPEhawryphEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 687 EATSALDAesehTVQEAISKNL------KGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLME 748
Cdd:PRK10261 489 EAVSALDV----SIRGQIINLLldlqrdFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
542-764 |
5.01e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFLHTKVALVGQEP-----VLyARSVT 615
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP-DMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIGygLDKYDDDMVQN----SAKLANAHTF-IMND---TTDGYNTNVGekgsQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:COG3845 355 ENLI--LGRYRRPPFSRggflDRKAIRAFAEeLIEEfdvRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 688 ATSALDAESehtvQEAISKNL-----KGKTVILIAHRLSTVEN-ADKIVVINKGK-VEQLGNHKTLMEQEGLykqlvqrq 760
Cdd:COG3845 429 PTRGLDVGA----IEFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRiVGEVPAAEATREEIGL-------- 496
|
....
gi 17511077 761 MMSG 764
Cdd:COG3845 497 LMAG 500
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
207-414 |
5.88e-10 |
|
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: 61.39 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 207 MAFFFLFCYSLSR----VFIPYYTGEVVTAVFGDKASYEKLHKTVFimGMLSLASTVFGGLRggSFTYAHATI--DRQIR 280
Cdd:cd18605 3 LILLSLILMQASRnlidFWLSYWVSHSNNSFFNFINDSFNFFLTVY--GFLAGLNSLFTLLR--AFLFAYGGLraARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 281 NDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLV 360
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 361 NKifgvWYDMLSEETQ--NSVAKAN--DVAEEVLSSIRTVKSFACENYESSRFMTFLN 414
Cdd:cd18605 159 QR----YYRATSRELKrlNSVNLSPlyTHFSETLKGLVTIRAFRKQERFLKEYLEKLE 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
538-750 |
7.74e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFLHTKVALVGQE---PVLYAR- 612
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrsTGIYAYl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 -----SVTENIGYGLDKY----DDDMVQNSAKLANAhtfiMNDTTDGYNTNVGekgsQMSGGQKQRIAIARALVRQPVVL 683
Cdd:PRK10982 342 digfnSLISNIRNYKNKVglldNSRMKSDTQWVIDS----MRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 684 LLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQE 750
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAGIVDTKTTTQNE 482
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
542-742 |
1.06e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVE---PGE-VVALVGPSGGGKSSCIAMLEHFYEPTSGE-VLIDGVPVREYDHKFLHT---KVALVGQEpvlyAR- 612
Cdd:PRK11144 12 DLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRiVLNGRVLFDAEKGICLPPekrRIGYVFQD----ARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 ----SVTENIGYGLDKYD----DDMVQnsaKLANAHTFimndttDGYNtnvgekgSQMSGGQKQRIAIARALVRQPVVLL 684
Cdd:PRK11144 88 fphyKVRGNLRYGMAKSMvaqfDKIVA---LLGIEPLL------DRYP-------GSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 685 LDEATSALDAESEHTVQ---EAISKNLkgKTVIL-IAHRLSTVEN-ADKIVVINKGKVEQLGN 742
Cdd:PRK11144 152 MDEPLASLDLPRKRELLpylERLAREI--NIPILyVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
522-735 |
1.22e-09 |
|
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: 58.41 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPI-RPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEP--TSGEVLIDGVPVREYdhkFLHT 598
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKN---FQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 599 kVALVGQEPVLYARS-VTENIGYgldkydddmvqnSAKLanahtfimndttdgyntnvgeKGsqMSGGQKQRIAIARALV 677
Cdd:cd03232 81 -TGYVEQQDVHSPNLtVREALRF------------SALL---------------------RG--LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAIsKNL--KGKTVILIAHRLSTV--ENADKIVVINKG 735
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFL-KKLadSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
536-742 |
1.24e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLE-H-FYEPTSGEVLIDGVPVREYD-HKFLHTKVALVGQEPV---- 608
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHpAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIeipg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 609 ------LYARSVTENIGYGLDKYDD----DMVQNSAKLANahtfiMNDTTDGYNTNVGekgsqMSGGQKQRIAIARALVR 678
Cdd:CHL00131 99 vsnadfLRLAYNSKRKFQGLPELDPleflEIINEKLKLVG-----MDPSFLSRNVNEG-----FSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 679 QPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAH--RLSTVENADKIVVINKGKVEQLGN 742
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
540-718 |
1.42e-09 |
|
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: 59.34 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPG-----EVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVrEYDHKFLHTKvalvgQEPVLYA--R 612
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKAD-----YEGTVRDllS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 613 SVTEniGYGLDKYDDDMVQNSAKLanahtfimndtTDGYNTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLDEATSAL 692
Cdd:cd03237 84 SITK--DFYTHPYFKTEIAKPLQI-----------EQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180
....*....|....*....|....*...
gi 17511077 693 DAESEHTVQEAISKNL--KGKTVILIAH 718
Cdd:cd03237 147 DVEQRLMASKVIRRFAenNEKTAFVVEH 174
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
518-733 |
1.51e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPIRPdlpIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLH 597
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALvgqePVLYARSVTenIGYGLDKYDDDMVQNSAKLANAHTFIMNdttdgyntnvgekgsQMSGGQKQRIAIARALV 677
Cdd:PRK09544 78 LDTTL----PLTVNRFLR--LRPGTKKEDILPALKRVQAGHLIDAPMQ---------------KLSGGETQRVLLARALL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAIS--KNLKGKTVILIAHRLSTV-ENADKIVVIN 733
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLVmAKTDEVLCLN 195
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
526-742 |
2.09e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 526 HVAFSYPiRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEP---TSGEVLIDG-----VPVREYDhKFLH 597
Cdd:PRK09473 19 RVTFSTP-DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGreilnLPEKELN-KLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 598 TKVALVGQEPVL----YARsVTENI------GYGLDKydDDMVQNSAKLANAhtfimndttdgynTNVGEKGSQM----- 662
Cdd:PRK09473 97 EQISMIFQDPMTslnpYMR-VGEQLmevlmlHKGMSK--AEAFEESVRMLDA-------------VKMPEARKRMkmyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 663 --SGGQKQRIAIARALVRQPVVLLLDEATSALDAesehTVQEAIS---KNLK---GKTVILIAHRLSTVEN-ADKIVVIN 733
Cdd:PRK09473 161 efSGGMRQRVMIAMALLCRPKLLIADEPTTALDV----TVQAQIMtllNELKrefNTAIIMITHDLGVVAGiCDKVLVMY 236
|
....*....
gi 17511077 734 KGKVEQLGN 742
Cdd:PRK09473 237 AGRTMEYGN 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
499-731 |
3.08e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 499 EFIDRPPRVEntgtyapdgmtgkiEFRHVAFSYP-IRPDLPimeDLTFTVEPG-----EVVALVGPSGGGKSSCIAMLEH 572
Cdd:PRK13409 325 EFEERPPRDE--------------SERETLVEYPdLTKKLG---DFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAG 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 573 FYEPTSGEVLIDgvpVR-EYDHKFLHTKValvgQEPV-LYARSVTenigyglDKYDDDMVQNSaklanahtfIMN--DTT 648
Cdd:PRK13409 388 VLKPDEGEVDPE---LKiSYKPQYIKPDY----DGTVeDLLRSIT-------DDLGSSYYKSE---------IIKplQLE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 649 DGYNTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN- 725
Cdd:PRK13409 445 RLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaEEREATALVVDHDIYMIDYi 520
|
....*.
gi 17511077 726 ADKIVV 731
Cdd:PRK13409 521 SDRLMV 526
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
518-692 |
3.88e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 518 MTGKIEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFL 596
Cdd:PRK11614 2 EKVMLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 597 HTKVALVGQEPVLYAR-SVTENIGYGldKYDDDMVQNSAKLANAHTFImndttdgynTNVGEKGSQ----MSGGQKQRIA 671
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMG--GFFAERDQFQERIKWVYELF---------PRLHERRIQragtMSGGEQQMLA 147
|
170 180
....*....|....*....|.
gi 17511077 672 IARALVRQPVVLLLDEATSAL 692
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGL 168
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
239-468 |
4.39e-09 |
|
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: 58.68 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 239 SYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSAdCQTMSNTL 318
Cdd:cd18783 37 SYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 319 S--LYMNVLtrNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTV 396
Cdd:cd18783 116 TgqLFGTLL--DATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTV 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 397 KSFAcenYESSRFMTFLNVTLKIATRKVFVVIGLIWSNEL---LQMGILTIVLWYGGHLVIENKVESGLLVSFLL 468
Cdd:cd18783 194 KSLA---LEPRQRREWDERVARAIRARFAVGRLSNWPQTLtgpLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNM 265
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
255-466 |
6.08e-09 |
|
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: 57.98 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 255 LASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLsADCQTMSNTLSLYMNVLTRNLTMLFG 334
Cdd:cd18566 53 LLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 335 SLIFMFTLSWKLSMITLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLN 414
Cdd:cd18566 132 FLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQA 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 415 VTLKiATRKVfVVIGLIWSN--ELLQMGILTIVLWYGGHLVIENKVESGLLVSF 466
Cdd:cd18566 212 NAAY-AGFKV-AKINAVAQTlgQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
207-368 |
6.42e-09 |
|
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: 57.90 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 207 MAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASYeklhkTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRS 286
Cdd:cd18580 7 LLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYY-----LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 287 VVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWklsmITLINIPIIFLVNKIFGV 366
Cdd:cd18580 82 VLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQR 157
|
..
gi 17511077 367 WY 368
Cdd:cd18580 158 YY 159
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
546-721 |
6.54e-09 |
|
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: 57.38 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 546 TVEPGEVVALVGPSGGGKSSCIAML---------EHFYEPTSGEVL--IDGVPVREYDHKFLHTKVALVgQEPV---LYA 611
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILagklkpnlgKFDDPPDWDEILdeFRGSELQNYFTKLLEGDVKVI-VKPQyvdLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RSVTENIGYGLDKYDDDMVQNsaklanahtfIMNDTTDgyNTNVGEKG-SQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLD----------ELVDQLE--LRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|..
gi 17511077 691 ALDAESEHTVQEAISKNLK-GKTVILIAHRLS 721
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
539-721 |
1.73e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYePTSGEVL-------IDGVPVREYdhkflHTKVALVGQepVLYA 611
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLtkpakgkLFYVPQRPY-----MTLGTLRDQ--IIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RSVTENIGYGLDkyDDDMVQnsaKLANAH-TFIMndTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATS 690
Cdd:TIGR00954 539 DSSEDMKRRGLS--DKDLEQ---ILDNVQlTHIL--EREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|...
gi 17511077 691 ALDAEsehtVQEAISKNLK--GKTVILIAHRLS 721
Cdd:TIGR00954 612 AVSVD----VEGYMYRLCRefGITLFSVSHRKS 640
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
522-704 |
1.82e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIdGVPVreydhkflhtKVA 601
Cdd:PRK11819 325 IEAENLSKSFG---DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 LVGQ-----EPvlyARSVTENIGYGLDkydddmvqnSAKLANahtFIMNdtTDGYNTNVGEKGS-------QMSGGQKQR 669
Cdd:PRK11819 391 YVDQsrdalDP---NKTVWEEISGGLD---------IIKVGN---REIP--SRAYVGRFNFKGGdqqkkvgVLSGGERNR 453
|
170 180 190
....*....|....*....|....*....|....*
gi 17511077 670 IAIARALVRQPVVLLLDEATSALDAESEHTVQEAI 704
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEAL 488
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
539-736 |
3.18e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSS---CIAM-LEHFYEPTSGEVLIDGVPVREYDHKF-----------LHTKVALV 603
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllkTIASnTDGFHIGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 604 GQEPVLYARSVT-ENIGYGLDKydDDMVQNSAKLANAhTFIMNDTtdgYNTNVGE---KGsqMSGGQKQRIAIARALVRQ 679
Cdd:TIGR00956 156 GETLDFAARCKTpQNRPDGVSR--EEYAKHIADVYMA-TYGLSHT---RNTKVGNdfvRG--VSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 680 PVVLLLDEATSALDAEsehTVQEAIsKNLKGKTVILIAHRLSTV----ENA----DKIVVINKGK 736
Cdd:TIGR00956 228 AKIQCWDNATRGLDSA---TALEFI-RALKTSANILDTTPLVAIyqcsQDAyelfDKVIVLYEGY 288
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
538-751 |
3.43e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhKFLHTKVALVGQepvlyarsvteN 617
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG--------KSILTNISDVHQ-----------N 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 IGY--GLDKYDDDMVQNS-----AKLANAHTFIMNDTTD------GYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLL 684
Cdd:TIGR01257 2014 MGYcpQFDAIDDLLTGREhlylyARLRGVPAEEIEKVANwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 685 LDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQEG 751
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
541-737 |
4.01e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 541 EDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFLHTKVALV----GQEPVLYARSVT 615
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGIMLCpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 616 ENIG---------YGLdkydddMVQNSAKLANAHTFI--MNDTTDGYNTNVGekgsQMSGGQKQRIAIARALVRQPVVLL 684
Cdd:PRK11288 350 DNINisarrhhlrAGC------LINNRWEAENADRFIrsLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17511077 685 LDEATSALDAESEHTVQEAISkNL--KGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIY-ELaaQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
543-741 |
4.04e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 543 LTFTVEPGEVVALVGPSGGGKS-SCIAMLEHFYEPtsGEVLIDGVPVREYDHKFLHTK---------VALVGQEPVLY-- 610
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDLQRISEKerrnlvgaeVAMIFQDPMTSln 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 611 -ARSVTENIGYGLDKYdddmvQNSAKLANAHTFIMNDTTDGY---NTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:PRK11022 104 pCYTVGFQIMEAIKVH-----QGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 687 EATSALDAesehTVQEAISKNL------KGKTVILIAHRLSTV-ENADKIVVINKGKVEQLG 741
Cdd:PRK11022 179 EPTTALDV----TIQAQIIELLlelqqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
539-738 |
7.96e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEV-LIDGVpvreydhkflhtKVALVGQEPVLYARSvten 617
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQHQLEFLRA---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 618 igygldkyDDDMVQNSAKLANAHT-FIMNDTTDGYNTN---VGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:PRK10636 391 --------DESPLQHLARLAPQELeQKLRDYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17511077 694 AESEHTVQEAISkNLKGKTVILIAHRLSTVENADKIVVINKGKVE 738
Cdd:PRK10636 463 LDMRQALTEALI-DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
542-726 |
9.02e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDHKFLhtkvALVGQEPVLYAR-SVTENIGY 620
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLKLEmTVFENLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 621 GLDKYdddmvqNSAKLANA--HTFIMNDTTDgyntnvgEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEH 698
Cdd:PRK13541 94 WSEIY------NSAETLYAaiHYFKLHDLLD-------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|....*....
gi 17511077 699 TVQEAIS-KNLKGKTVILIAHRLSTVENA 726
Cdd:PRK13541 161 LLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
203-360 |
1.21e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 54.25 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 203 KYYGMAFFFLFCYSLSRVFI---------------PYYTGEVVTAVFGDKASYEKLHKT--VFIMGMLSLASTVFGGLRG 265
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVlsdwwlsywanleekLNDTTDRVQGENSTNVDIEDLDRDfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 266 GSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIF-MFTLSW 344
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLaVVVNPW 160
|
170
....*....|....*.
gi 17511077 345 KLsmITLINIPIIFLV 360
Cdd:cd18601 161 VL--IPVIPLVILFLF 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
521-731 |
1.49e-07 |
|
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: 54.79 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 521 KIEFR-HVAFSYPIRPDL---PIME----DLTFTVEPG-----EVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDgvp 587
Cdd:COG1245 324 PIEFEvHAPRREKEEETLveyPDLTksygGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 588 vreydhkflhTKVALVGQepvlyarsvtenigYGLDKYDDDMVQNsakLANAHTFIMNDTTdgYNTNVGEK--------- 658
Cdd:COG1245 401 ----------LKISYKPQ--------------YISPDYDGTVEEF---LRSANTDDFGSSY--YKTEIIKPlgleklldk 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 659 -GSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK--NLKGKTVILIAHRLSTVEN-ADKIVV 731
Cdd:COG1245 452 nVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfaENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
539-762 |
2.12e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 539 IMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreydhkflHTKVALVGQEPVLYARSVTEni 618
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQETPALPQPALE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 619 gYGLDKyDDDMVQNSAKLANAhtfimNDTTDGY-------------------------------NTNVGEKGSQMSGGQK 667
Cdd:PRK10636 83 -YVIDG-DREYRQLEAQLHDA-----NERNDGHaiatihgkldaidawtirsraasllhglgfsNEQLERPVSDFSGGWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 668 QRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAIsKNLKGkTVILIAHRLSTVEN-ADKIVVINKGKV-EQLGNHKT 745
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISHDRDFLDPiVDKIIHIEQQSLfEYTGNYSS 233
|
250
....*....|....*..
gi 17511077 746 LMEQEGlyKQLVQRQMM 762
Cdd:PRK10636 234 FEVQRA--TRLAQQQAM 248
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
520-725 |
2.97e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 520 GKIEFRHVAFSYPIrPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVlidgvpvreydHKFLHTK 599
Cdd:PRK11147 316 GKIVFEMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------HCGTKLE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 600 VALVGQ-----EPvlyARSVTENIGYGldkYDDDMVQNSAKlanaHTFimndttdGY-----------NTNVgekgSQMS 663
Cdd:PRK11147 384 VAYFDQhraelDP---EKTVMDNLAEG---KQEVMVNGRPR----HVL-------GYlqdflfhpkraMTPV----KALS 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17511077 664 GGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISkNLKGkTVILIAHRLSTVEN 725
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD-SYQG-TVLLVSHDRQFVDN 502
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
523-749 |
3.74e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 523 EFRHVAFSYPIRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYE-PTSGEVLIDGVPVR-EYDHKFLHTKV 600
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 ALV-------GQEPVLyarSVTENIGYG-LDKYDD-DMVQNSAKLANAHTFI--MNDTTDGYNTNVGekgsQMSGGQKQR 669
Cdd:PRK13549 341 AMVpedrkrdGIVPVM---GVGKNITLAaLDRFTGgSRIDDAAELKTILESIqrLKVKTASPELAIA----RLSGGNQQK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 670 IAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLSTVEN-ADKIVVINKGKVE-QLGNHKTL 746
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLVMHEGKLKgDLINHNLT 493
|
...
gi 17511077 747 MEQ 749
Cdd:PRK13549 494 QEQ 496
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
546-732 |
3.94e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 546 TVEPGEVVALVGPSGGGKSSCIAML---------EHFYEPTSGEVLidgvpvREYDHKFLHT----------KVALVGQE 606
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVL------KRFRGTELQNyfkklyngeiKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 607 PVLYARSVTENIGYGLDKYD-----DDMVQnsaKLANAHtfIMNdttdgyntnvgEKGSQMSGGQKQRIAIARALVRQPV 681
Cdd:PRK13409 169 VDLIPKVFKGKVRELLKKVDergklDEVVE---RLGLEN--ILD-----------RDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17511077 682 VLLLDEATSALDAESEHTVQEAISKNLKGKTVILIAHRLSTVEN-ADKIVVI 732
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
522-758 |
4.14e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPIRPDLpiMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVlidgvpvreydhkFLHTKV- 600
Cdd:PLN03073 509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------FRSAKVr 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 601 -ALVGQEPVlyarsvtenigYGLDkydddmVQNSAKLANAHTF--IMNDTTDGYNTNVGEKGS-------QMSGGQKQRI 670
Cdd:PLN03073 574 mAVFSQHHV-----------DGLD------LSSNPLLYMMRCFpgVPEQKLRAHLGSFGVTGNlalqpmyTLSGGQKSRV 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 671 AIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLKGktVILIAHRLSTVENA-DKIVVINKGKVEQLgnHKTLMEq 749
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPF--HGTFHD- 711
|
....*....
gi 17511077 750 eglYKQLVQ 758
Cdd:PLN03073 712 ---YKKTLQ 717
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
650-735 |
4.35e-07 |
|
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: 50.78 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 650 GYNTnVGEKGSQMSGGQKQRIAIARALVRQP--VVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVENA 726
Cdd:cd03238 77 GYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSA 155
|
....*....
gi 17511077 727 DKIVVINKG 735
Cdd:cd03238 156 DWIIDFGPG 164
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
538-737 |
7.10e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 538 PIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYD-HKFLHTKVALVGQEP-----VLyA 611
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdglVL-G 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 RSVTENIGY-GLDKYDDDMVQ--NSAKLANAHTFIM--NDTTDGYNTNVGEkgsqMSGGQKQRIAIARALVRQPVVLLLD 686
Cdd:PRK10762 345 MSVKENMSLtALRYFSRAGGSlkHADEQQAVSDFIRlfNIKTPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17511077 687 EATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQfKAEGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
656-737 |
8.05e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 656 GEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLSTVEN-ADKIVVIN 733
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVID 218
|
....
gi 17511077 734 KGKV 737
Cdd:NF000106 219 RGRV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
533-758 |
9.69e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 533 IRPDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGV---PVREYDHkfLHTKVALVGQ---E 606
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDA--VKKGMAYITEsrrD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 607 PVLYAR-SVTENI---------GYG--LDKYDDDMVQnsaKLANAHTFIMNDTTDGYNTNVGEkgsqMSGGQKQRIAIAR 674
Cdd:PRK09700 350 NGFFPNfSIAQNMaisrslkdgGYKgaMGLFHEVDEQ---RTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 675 ALVRQPVVLLLDEATSALD--AESE-HTVQEAISKnlKGKTVILIAHRLSTVENA-DKIVVINKGKVEQ-LGNHKTLMEQ 749
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDvgAKAEiYKVMRQLAD--DGKVILMVSSELPEIITVcDRIAVFCEGRLTQiLTNRDDMSEE 500
|
....*....
gi 17511077 750 EGLYKQLVQ 758
Cdd:PRK09700 501 EIMAWALPQ 509
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
523-735 |
1.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 523 EFRHVAFSYPIRP-DLPIMEDLTFTVEPGEVVALVGPSGGGKSS---CIAMLEHFYEPTSGEVLIDGvpvREYDHKF--- 595
Cdd:TIGR00956 761 HWRNLTYEVKIKKeKRVILNNVDGWVKPGTLTALMGASGAGKTTllnVLAERVTTGVITGGDRLVNG---RPLDSSFqrs 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 596 --------LHTKVALVGQEPVLYAR-----SVTenigyglDKYDDDMVQNSAKLANahtfiMNDTTDGYntnVGEKGSQM 662
Cdd:TIGR00956 838 igyvqqqdLHLPTSTVRESLRFSAYlrqpkSVS-------KSEKMEYVEEVIKLLE-----MESYADAV---VGVPGEGL 902
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17511077 663 SGGQKQRIAIARALVRQPVVLL-LDEATSALDAESEHTVQEAISKNLK-GKTVILIAHRLSTV--ENADKIVVINKG 735
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
661-730 |
1.68e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 1.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 661 QMSGGQKQRIAIARAL----VRQPVVLLLDEATSALDAESEHTVQEAISKNLKGK-TVILIAHRLSTVENADKIV 730
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLI 151
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
546-732 |
1.90e-06 |
|
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: 51.32 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 546 TVEPGEVVALVGPSGGGKSSCIAML---------EHFYEPTSGEVLidgvpvREYDHKFLHT----------KVALVGQE 606
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILsgelkpnlgDYDEEPSWDEVL------KRFRGTELQDyfkklangeiKVAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 607 PVLYARSVTENIGYGLDKYD-----DDMVQnsaKLANAHtfIMNDTTdgyntnvgekgSQMSGGQKQRIAIARALVRQPV 681
Cdd:COG1245 169 VDLIPKVFKGTVRELLEKVDergklDELAE---KLGLEN--ILDRDI-----------SELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 682 VLLLDEATSALDAESEHTVQEAIsKNL--KGKTVILIAHRLSTVEN-ADKIVVI 732
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLI-RELaeEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
522-693 |
2.40e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 522 IEFRHVAFSYPirpDLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAmlehfyeptsgevLIDGvpvreyDHkflhtkva 601
Cdd:PRK10938 261 IVLNNGVVSYN---DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS-------------LITG------DH-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 602 lvgqePVLYARSVT----------------ENIGYgldkydddmVQNSAKL-----ANAHTFIMNDTTD----------- 649
Cdd:PRK10938 311 -----PQGYSNDLTlfgrrrgsgetiwdikKHIGY---------VSSSLHLdyrvsTSVRNVILSGFFDsigiyqavsdr 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 650 ------------GYNTNVGEKGSQ-MSGGQkQRIA-IARALVRQPVVLLLDEATSALD 693
Cdd:PRK10938 377 qqklaqqwldilGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
231-364 |
3.33e-06 |
|
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: 49.87 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 231 TAVFGDKASYEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSAD 310
Cdd:cd18599 45 TVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKD 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 311 CQTMSNTLSLYMNVLTRNLTMLFGSLIF-MFTLSWKLSMITLINIpIIFLVNKIF 364
Cdd:cd18599 125 LDEVDVRLPFTLENFLQNVLLVVFSLIIiAIVFPWFLIALIPLAI-IFVFLSKIF 178
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
536-718 |
6.80e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 536 DLPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVlidgvpvreydhKFlhTKVALVGQEPVLYA---- 611
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW--SENANIGYYAQDHAydfe 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 612 --RSVTENIG-YGLDKYDDDMVQNS-AKLanahTFIMNDttdgyntnVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDE 687
Cdd:PRK15064 397 ndLTLFDWMSqWRQEGDDEQAVRGTlGRL----LFSQDD--------IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190
....*....|....*....|....*....|.
gi 17511077 688 ATSALDAESEHTVQEAIsKNLKGkTVILIAH 718
Cdd:PRK15064 465 PTNHMDMESIESLNMAL-EKYEG-TLIFVSH 493
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
292-471 |
1.03e-05 |
|
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: 48.24 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 292 IGFFDMNKTGEICSRLSAdCQTMSNTLS--LYMNVLtrNLTMLFGSLIFMFTLSWKLSMI----TLINIPIIFLVNKifg 365
Cdd:cd18569 90 VEFFSQRYAGDIASRVQS-NDRVANLLSgqLATTVL--NLVMAVFYALLMLQYDVPLTLIgiaiALLNLLVLRLVSR--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 366 vWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTF----LNVTLKIAtrkvfvVIGLIWSN--ELLQM 439
Cdd:cd18569 164 -KRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSRWAGYqakvLNAQQELG------RTNQLLGAlpTLLSA 236
|
170 180 190
....*....|....*....|....*....|....
gi 17511077 440 GILTIVLWYGGHLVIENKVESGLLVSF--LLYQF 471
Cdd:cd18569 237 LTNAAILGLGGLLVMDGALTIGMLVAFqsLMASF 270
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
208-491 |
1.53e-05 |
|
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: 47.49 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVFIPYYTGEVVTAvFGDKASYEKLHKTVFIM--GMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFR 285
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDA-LSAPASALLAVPLLLLLayGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 286 SVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLS-LYMNVLTRNLTMLFGSLIFMFTLSWKLSMITLINIPIIFLVNKIF 364
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRfLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 365 GVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLnVTLKIATRKVFvvigliWSNELLQMGI--- 441
Cdd:cd18582 160 TEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKAL-AKYEKAAVKSQ------TSLALLNIGQali 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17511077 442 ----LTIVLWYGGHLVIENKVESGLLVSFLLYQFQLGENLRELGEVWNGLMQAV 491
Cdd:cd18582 233 islgLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
542-737 |
1.86e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 542 DLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGVPVREYDhkflhTKVALvgQEPVLYARSVTENIGYG 621
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS-----TAQRL--ARGLVYLPEDRQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 622 LDkydddmvqnsAKLA-NAHTFIMND------------TTDGYNTNVGEKGSQ-------MSGGQKQRIAIARALVRQPV 681
Cdd:PRK15439 354 LD----------APLAwNVCALTHNRrgfwikparenaVLERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 682 VLLLDEATSALDAESEHTVQEAIsKNL--KGKTVILIAHRLSTVEN-ADKIVVINKGKV 737
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLI-RSIaaQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
540-797 |
2.27e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreyDHKFLHTKVALVGQepvlyaRSVTENIG 619
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 620 -----YGLDKYD-DDMVQNSAKLANAHTFImNDTTDGYntnvgekgsqmSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:PRK13545 108 lkglmMGLTKEKiKEIIPEIIEFADIGKFI-YQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 694 AESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVEQLGNHKTLMEQEGLY------------KQLVQR 759
Cdd:PRK13545 176 QTFTKKCLDKMNEfKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFlkkynqmsveerKDFREE 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 17511077 760 QMMSGEDGLddeIEEPEPAREggsgRSTRAGARRIRSP 797
Cdd:PRK13545 256 QISQFQHGL---LQEDQTGRE----RKRKKGKKTSRKF 286
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
661-718 |
2.82e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAeseHTVQEAISKNLK-GKTVILIAH 718
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKwPKTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
645-732 |
2.94e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 645 NDTTDGYNTNVGEKGSQMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISKNLK--GKTVILIAHRLST 722
Cdd:cd03222 55 NDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAV 134
|
90
....*....|.
gi 17511077 723 VEN-ADKIVVI 732
Cdd:cd03222 135 LDYlSDRIHVF 145
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
249-428 |
3.46e-05 |
|
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: 46.31 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 249 IMGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRN 328
Cdd:cd18606 40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 329 LTMLFGSLIFMF-TLSWklsmiTLINIPIIFLVNKIFGVWYDMLSEETQ--NSVAKANDVAE--EVLSSIRTVKSFAcen 403
Cdd:cd18606 120 LSSIIGTFILIIiYLPW-----FAIALPPLLVLYYFIANYYRASSRELKrlESILRSFVYANfsESLSGLSTIRAYG--- 191
|
170 180
....*....|....*....|....*
gi 17511077 404 yESSRFMTFLNVTLKIATRKVFVVI 428
Cdd:cd18606 192 -AQDRFIKKNEKLIDNMNRAYFLTI 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
661-761 |
3.54e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALdaesEHTVQEAISKNL------KGKTVILIAHRLSTVEN-ADKIVVIN 733
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAM----EPTTQAQIFRLLtrlnqnNNTTILLISHDLQMLSQwADKINVLY 233
|
90 100
....*....|....*....|....*....
gi 17511077 734 KGK-VEQLGNHKTLMEQEGLYKQLVQRQM 761
Cdd:PRK15093 234 CGQtVETAPSKELVTTPHHPYTQALIRAI 262
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
656-730 |
4.07e-05 |
|
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: 46.07 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 656 GEKGSQMSGGQKQRIAIARALVRQ---PVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLSTVENADKIV 730
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWII 242
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
253-337 |
9.84e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 45.29 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 253 LSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTML 332
Cdd:cd18602 59 LSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLC 138
|
....*
gi 17511077 333 FGSLI 337
Cdd:cd18602 139 LSAII 143
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
207-368 |
1.20e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 44.77 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 207 MAFFFLFCYSLSRVFIPYYTGEVVTAVFGDKASYEKLHKTVFIMGM---LSLASTVFGGLRggSFTYAHATID--RQIRN 281
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIyalISLLSVLLGTLR--YLLFFFGSLRasRKLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 282 DLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWklsmitLINIPIIFLVn 361
Cdd:cd18604 81 RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSP------AFLLPAVVLA- 153
|
....*..
gi 17511077 362 kIFGVWY 368
Cdd:cd18604 154 -ALYVYI 159
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
537-735 |
1.89e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 537 LPIMEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEH-----FYEptsGEVLIDGVPVREY---------DHKFLHTKVAL 602
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrktggYIE---GDIRISGFPKKQEtfarisgycEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 603 VgQEPVLYarSVTENIGYGLDKYDD----DMVQNSAKLANAHTFImndttdgyntnVGEKG-SQMSGGQKQRIAIARALV 677
Cdd:PLN03140 970 V-RESLIY--SAFLRLPKEVSKEEKmmfvDEVMELVELDNLKDAI-----------VGLPGvTGLSTEQRKRLTIAVELV 1035
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 678 RQPVVLLLDEATSALDAESEHTVQEAISKNL-KGKTVILIAHRLS--TVENADKIVVINKG 735
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
270-497 |
2.27e-04 |
|
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: 43.81 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 270 YAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIFMFTLSWKLSMI 349
Cdd:cd18561 62 RAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 350 TLINIPIIFLVNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFAcenyESSRFMTFLNVT---LKIATRKVFV 426
Cdd:cd18561 142 LLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFG----ASKRRGNELAARaedLRQATMKVLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 427 VigliwsnELLQMGIL--------TIVLWYGGHLVIENKVE--SGLLVSFLLYQ-FQLgenLRELGEVWNGLMQAVGASR 495
Cdd:cd18561 218 V-------SLLSSGIMglatalgtALALGVGALRVLGGQLTlsSLLLILFLSREfFRP---LRDLGAYWHAGYQGISAAD 287
|
..
gi 17511077 496 KV 497
Cdd:cd18561 288 SI 289
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
540-749 |
5.14e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 540 MEDLTFTVEPGEVVALVGPSGGGKSSCIAMLEHFYEPTSGEVLIDGvpvreyDHKFLHTKVALVGQepvlyaRSVTENIG 619
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 620 YGL------DKYDDDMVQNSAKLANAHTFIMNDTtdgyntnvgekgSQMSGGQKQRIAIARALVRQPVVLLLDEATSALD 693
Cdd:PRK13546 108 FKMlcmgfkRKEIKAMTPKIIEFSELGEFIYQPV------------KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511077 694 aesEHTVQEAISK----NLKGKTVILIAHRLSTV-ENADKIVVINKGKVEQLGNHKTLMEQ 749
Cdd:PRK13546 176 ---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
656-730 |
5.63e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 656 GEKGSQMSGGQKQRIAIARALVRQ---PVVLLLDEATSALdaeseHTvqEAISKNL--------KGKTVILIAHRLSTVE 724
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL-----HF--DDIKKLLevlqrlvdKGNTVVVIEHNLDVIK 896
|
....*.
gi 17511077 725 NADKIV 730
Cdd:TIGR00630 897 TADYII 902
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
660-730 |
8.32e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 660 SQMSGGQKQRIAIAraLV-----RQPVVL-LLDEATSALDAEseHTvqEAISKNLKGKT----VILIAHRLSTVENADKI 729
Cdd:pfam02463 1076 DLLSGGEKTLVALA--LIfaiqkYKPAPFyLLDEIDAALDDQ--NV--SRVANLLKELSknaqFIVISLREEMLEKADKL 1149
|
.
gi 17511077 730 V 730
Cdd:pfam02463 1150 V 1150
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
662-735 |
9.17e-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: 41.47 E-value: 9.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 662 MSGGQKQRIAIARALVRQ--PVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVENADKIVVINKG 735
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETL-KRLRdlGNTVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
660-730 |
1.11e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17511077 660 SQMSGGQKQRIAIARAL---VRQPVVLLLDEATSALDAeseHTVQEAI----SKNLKGKTVILIAHRLSTVENADKIV 730
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHT---HDIKALIyvlqSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
250-467 |
1.12e-03 |
|
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: 41.76 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 250 MGMLSLASTVFGGLRGGSFTYAHATIDRQIRNDLFRSVVKQEIGFFDMNKTGEICSRLSAdcQTM------SNTLSLymn 323
Cdd:cd18779 48 LAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSS--NATirelltSQTLSA--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 324 VLtrNLTMLFGSLIFMFTLSWKLSMITL----INIPIIFLVNKifgvwydMLSEETQNSV---AKANDVAEEVLSSIRTV 396
Cdd:cd18779 123 LL--DGTLVLGYLALLFAQSPLLGLVVLglaaLQVALLLATRR-------RVRELMARELaaqAEAQSYLVEALSGIETL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17511077 397 KSFACENYE----SSRFMTFLNVTLKiATRKVFVVIGLIwsnELLQMGILTIVLWYGGHLVIENKVESGLLVSFL 467
Cdd:cd18779 194 KASGAEDRAldrwSNLFVDQLNASLR-RGRLDALVDALL---ATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
661-756 |
1.68e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 661 QMSGGQKQRIAIARALVRQPVVLLLDEATSALDAESEHTVQEAISK-NLKGKTVILIAHRLSTVEN-ADKIVVINKGKVE 738
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLA 214
|
90
....*....|....*...
gi 17511077 739 QLGNHKTLMeQEGLYKQL 756
Cdd:PRK10938 215 ETGEREEIL-QQALVAQL 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
640-741 |
2.68e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 640 HTFIMNDTtdGYnTNVGEKGSQMSGGQKQRIAIARALV---RQPVVLLLDEATSALDAESEHTVQEAIsKNL--KGKTVI 714
Cdd:PRK00635 1681 QALIDNGL--GY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQL-RTLvsLGHSVI 1756
|
90 100
....*....|....*....|....*..
gi 17511077 715 LIAHRLSTVENADKIVVINKGKVEQLG 741
Cdd:PRK00635 1757 YIDHDPALLKQADYLIEMGPGSGKTGG 1783
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
662-792 |
4.97e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 662 MSGGQKQRIAIAR----ALVrqPVVLLLDEATSALDAESEHTVQEAIsKNLK--GKTVILIAHRLSTVENADKIVVINKG 735
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLT--GVLYVLDEPSIGLHQRDNRRLINTL-KRLRdlGNTLIVVEHDEDTIRAADYVIDIGPG 565
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17511077 736 KveqlGNHKTLMEQEGLYKQLVQR------QMMSGEdgldDEIEEPEPAREGGSGRSTRAGAR 792
Cdd:TIGR00630 566 A----GEHGGEVVASGTPEEILANpdsltgQYLSGR----KKIEVPAERRPGNGKFLTLKGAR 620
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
208-359 |
6.89e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 39.38 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 208 AFFFLFCYSLSRVF-------IPYYTGEVVTAVFGDKasyEKLHKTVFIMGMLSLASTVFGGLRGGSFTYAHATIDRQIR 280
Cdd:cd18603 1 SLLILLLYLLSQAFsvgsniwLSEWSDDPALNGTQDT---EQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLH 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17511077 281 NDLFRSVVKQEIGFFDMNKTGEICSRLSADCQTMSNTLSLYMNVLTRNLTMLFGSLIfmfTLSWKLSMITLINIPIIFL 359
Cdd:cd18603 78 NKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLV---VISISTPIFLVVIIPLAIL 153
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
212-473 |
7.51e-03 |
|
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: 39.05 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 212 LFCYSLSRVF---IPYYTGEVVtavfgdkasyEKLHKTVFIMGMLSLAstVFGGLR----GGSFTYAHAT--------ID 276
Cdd:cd18583 2 FLCLLAERVLnvlVPRQLGIIV----------DSLSGGSGKSPWKEIG--LYVLLRflqsGGGLGLLRSWlwipveqySY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 277 RQIRNDLFRSVVKQEIGFFDMNKTGEIcsrLSADCQ-----TMSNTLSLYMNVLTRNLTMLFGSLIFMFtlSWKLSMITL 351
Cdd:cd18583 70 RALSTAAFNHVMNLSMDFHDSKKSGEV---LKAIEQgssinDLLEQILFQIVPMIIDLVIAIVYLYYLF--DPYMGLIVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 352 INIpIIFL-VNKIFGVWYDMLSEETQNSVAKANDVAEEVLSSIRTVKSFACENYESSRFMTFLNVTLKiATRKVFvvIGL 430
Cdd:cd18583 145 VVM-VLYVwSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQK-AERKYL--FSL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17511077 431 IWSNeLLQMGILT----IVLWYGGHLVIENKVESGLLVSFLLYQFQL 473
Cdd:cd18583 221 NLLN-AVQSLILTlgllAGCFLAAYQVSQGQATVGDFVTLLTYWAQL 266
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
663-745 |
9.49e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511077 663 SGGQKQRIAIARALVRQPV---VLLLDEATSALdaeseHTvqEAISKNL--------KGKTVILIAHRLSTVENADKIV- 730
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRSTgktLYILDEPTTGL-----HF--EDIRKLLevlhrlvdKGNTVVVIEHNLDVIKTADWIId 904
|
90 100
....*....|....*....|....*.
gi 17511077 731 -----------VINKGKVEQLGNHKT 745
Cdd:PRK00349 905 lgpeggdgggeIVATGTPEEVAKVEA 930
|
|
| |
