|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-573 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 1029.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 1 MRALLPYLALYKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFE 80
Cdd:PRK11160 1 MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFNYMLPAAGVRGAAIGRTAGRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 81 RLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDF 160
Cdd:PRK11160 81 RLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 161 TLAFTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQ 240
Cdd:PRK11160 161 TLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 241 SELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQ 320
Cdd:PRK11160 241 ANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 321 KPEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLN 400
Cdd:PRK11160 321 KPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 401 DSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLE-DAGLNSWLGEGGRQLSGGE 479
Cdd:PRK11160 401 GQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEdDKGLNAWLGEGGRQLSGGE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 480 LRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
570
....*....|....
gi 447124921 560 LARQGRYYQFKQGL 573
Cdd:PRK11160 561 LAQQGRYYQLKQRL 574
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-571 |
0e+00 |
|
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: 769.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 2 RALLPYLALYKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAglysFNYMLPAAGVRGAAITRTAGRYFER 81
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPI----LNLFVPIVGVRAFAIGRTVFRYLER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 82 LVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFT 161
Cdd:COG4987 77 LVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 162 LAFTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQS 241
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 242 ELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQK 321
Cdd:COG4987 237 RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 322 PEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLND 401
Cdd:COG4987 317 PAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 402 SPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGE 479
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAAlpDGLDTWLGEGGRRLSGGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 480 LRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
570
....*....|..
gi 447124921 560 LARQGRYYQFKQ 571
Cdd:COG4987 557 LAQNGRYRQLYQ 568
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-533 |
0e+00 |
|
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: 568.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 4 LLPYLALYKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGvAGLYsfnYMLPAAGVRGAAITRTAGRYFERLV 83
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMP-PVLY---LSVAAVAVRAFGIGRAVFRYLERLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 84 SHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLA 163
Cdd:TIGR02868 77 GHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 164 FTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSEL 243
Cdd:TIGR02868 157 LILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 244 TALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQK-- 321
Cdd:TIGR02868 237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAgp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 322 -PEVTFPDTQTRVADRVSLTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLN 400
Cdd:TIGR02868 317 vAEGSAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 401 DSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGG 478
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 479 ELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRL 533
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-314 |
3.39e-140 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD 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. 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: 350029 [Multi-domain] Cd Length: 290 Bit Score: 407.64 E-value: 3.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 25 AIVTLLASIGLLTLSGWFLSASAVAGVAGlYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLL 104
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAA-PTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 105 PLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAFTLGGIMLLTLFLMPPLFYRA 184
Cdd:cd18585 80 PLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 185 GKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIMLLIGALAVILMLW 264
Cdd:cd18585 160 GKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447124921 265 MASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd18585 240 LGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRL 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-569 |
5.42e-130 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 392.22 E-value: 5.42e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 1 MRALLPYLalyKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYsfnyMLPAAGVRGAAITRTAGRYFE 80
Cdd:COG1132 9 LRRLLRYL---RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSAL----LLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 81 RLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDF 160
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 161 TLAFTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLrGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQ 240
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL-AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 241 SELTALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTD 319
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVlSGSLTVGDLVA-FILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 320 QKPEVT-FPDTQTRVADRVSLTLRDVQFTYPEqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIL 398
Cdd:COG1132 320 EPPEIPdPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 399 LNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLS 476
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEAlpDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 477 GGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTH 556
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|...
gi 447124921 557 AELLARQGRYYQF 569
Cdd:COG1132 559 EELLARGGLYARL 571
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-564 |
1.94e-110 |
|
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: 341.35 E-value: 1.94e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 1 MRALLPYL-ALYKRHKWMLSLGIVLAIVTLLASIGLLtlsgWFLSASAVAGVAGLYSFNYMLPA-AGVRGAAITRTAGRY 78
Cdd:COG4988 1 QKPLDKRLkRLARGARRWLALAVLLGLLSGLLIIAQA----WLLASLLAGLIIGGAPLSALLPLlGLLLAVLLLRALLAW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 79 FERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFL 158
Cdd:COG4988 77 LRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 159 DFTLAFtlggIMLLTLFLMPpLF-----YRAGKSTGQNLTHLrgqyrQQLTA----WLQGQAELTIFGASDRYRTQLent 229
Cdd:COG4988 157 DWLSGL----ILLVTAPLIP-LFmilvgKGAAKASRRQWRAL-----ARLSGhfldRLRGLTTLKLFGRAKAEAERI--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 230 eiqwleaqRRQSEltALSQAIM-LLIGALAVILML-WMASGGVggnaqpgALIALFV---------------FCALAAFE 292
Cdd:COG4988 224 --------AEASE--DFRKRTMkVLRVAFLSSAVLeFFASLSI-------ALVAVYIgfrllggsltlfaalFVLLLAPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 293 ALAPV--TGAFQHLG-QVIASAVRISDLTDQKPEVTFPDTQTRVADR-VSLTLRDVQFTYPEqSQQALKGISLQVNAGEH 368
Cdd:COG4988 287 FFLPLrdLGSFYHARaNGIAAAEKIFALLDAPEPAAPAGTAPLPAAGpPSIELEDVSFSYPG-GRPALDGLSLTIPPGER 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 369 IAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSE 448
Cdd:COG4988 366 VALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 449 ILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTV 526
Cdd:COG4988 446 ALEAAGLDEFVAAlpDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV 525
|
570 580 590
....*....|....*....|....*....|....*...
gi 447124921 527 LMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQG 564
Cdd:COG4988 526 ILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-572 |
1.58e-105 |
|
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: 332.95 E-value: 1.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 2 RALLPYLALYKRH-KWMLSLGIVLAIVTLLASIGLLTLSGWFLSASA-------VAGVAGLYSFNYMLpaAGVRGAAITR 73
Cdd:COG2274 145 RWFLRLLRRYRRLlLQVLLASLLINLLALATPLFTQVVIDRVLPNQDlstlwvlAIGLLLALLFEGLL--RLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 74 TAGRYFERLVSHdatfrvlqhlriyTFSKLLPLSPAGLARYRQGELLNRVvADVDTLDHLylrVISPLVGAFVVIMVVTI 153
Cdd:COG2274 223 LGQRIDLRLSSR-------------FFRHLLRLPLSFFESRSVGDLASRF-RDVESIREF---LTGSLLTALLDLLFVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 154 GLSFLdFTLAFTLGGIMLLTLFLMPPLFYRAGKStGQNLTHLRGQYRQQLTAWL----QGQAELTIFGASDRYRTQLENT 229
Cdd:COG2274 286 FLIVL-FFYSPPLALVVLLLIPLYVLLGLLFQPR-LRRLSREESEASAKRQSLLvetlRGIETIKALGAESRFRRRWENL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 230 EIQWLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVI 308
Cdd:COG2274 364 LAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLViDGQLTLGQLIA-FNILSGRFLAPVAQLIGLLQRFQDAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 309 ASAVRISDLTDQKPEVTFPDTQTRVAD-RVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLT 387
Cdd:COG2274 443 IALERLDDILDLPPEREEGRSKLSLPRlKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 388 RAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLN 465
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEAlpMGYD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 466 SWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVM 545
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
570 580
....*....|....*....|....*..
gi 447124921 546 DNGQIIEQGTHAELLARQGRYYQFKQG 572
Cdd:COG2274 683 DKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
25-315 |
2.16e-89 |
|
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: 277.62 E-value: 2.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 25 AIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLL 104
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 105 PLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDfTLAFTLGGIMLLTLFLMPPLFYRA 184
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLD-PLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 185 GKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIMLLIGALAVILMLW 264
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 447124921 265 MASGGVGGnAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRIS 315
Cdd:cd18561 240 VGALRVLG-GQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
339-554 |
2.23e-89 |
|
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: 273.42 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLnEAALRQTISV 418
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLllaspgssdealseilrrvgleklledaglnswlgegGRQLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 499 DEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-566 |
1.01e-77 |
|
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: 256.18 E-value: 1.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 2 RALLPYLALYKrhkWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFnymLPAaGVRGAAITRTAGRYFER 81
Cdd:TIGR02203 3 RRLWSYVRPYK---AGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWW---VPL-VVIGLAVLRGICSFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 82 LVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDtldhlylRVISPLVGAFVVIM---VVTIGLSFL 158
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSE-------QVASAATDAFIVLVretLTVIGLFIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 159 DFTLAFTLGGIMLLTLFLMPPLFYRAGK---STGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLE 235
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKrlrRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 236 AQRRQSELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRIS 315
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 316 DLTDQKPEvtfPDTQTRVADRVS--LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ 393
Cdd:TIGR02203 309 TLLDSPPE---KDTGTRAIERARgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 394 QGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEAlsEILRRVGLEKLLE-----DAGLNSWL 468
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRA--EIERALAAAYAQDfvdklPLGLDTPI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 469 GEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNG 548
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
570
....*....|....*...
gi 447124921 549 QIIEQGTHAELLARQGRY 566
Cdd:TIGR02203 544 RIVERGTHNELLARNGLY 561
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-569 |
4.67e-74 |
|
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: 246.54 E-value: 4.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 1 MRALLPYLAlykRHKWMLSLGIVLAIVTLLASIGL-----LTLSGWFLSASAvagvaGLYSfNYMLPAAGVRGAAITRTA 75
Cdd:TIGR02204 6 LAALWPFVR---PYRGRVLAALVALLITAAATLSLpyavrLMIDHGFSKDSS-----GLLN-RYFAFLLVVALVLALGTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 76 GRYFerLVSHDATfRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVdTLdhlylrvISPLVGAFVVI----MVV 151
Cdd:TIGR02204 77 ARFY--LVTWLGE-RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDT-TL-------LQSVIGSSLSMalrnALM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 152 TIGLSFLDFTLAFTLGGIMLLT--LFLMPPLFY----RAGKSTGQNLTHLRGQYRQQLTAWLQG-QAeltiFGASDRYRT 224
Cdd:TIGR02204 146 CIGGLIMMFITSPKLTSLVLLAvpLVLLPILLFgrrvRKLSRESQDRIADAGSYAGETLGAIRTvQA----FGHEDAERS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 225 QLENTEIQWLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCAL---AAFEALAPVTGAF 301
Cdd:TIGR02204 222 RFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVmvaGSIGTLSEVWGEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 302 QhlgQVIASAVRISDLTDQKPEVTFPDTQTRVADRVS--LTLRDVQFTYPEQSQQ-ALKGISLQVNAGEHIAILGRTGCG 378
Cdd:TIGR02204 302 Q---RAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRgeIEFEQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 379 KSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKL 458
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 459 LE--DAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGL 536
Cdd:TIGR02204 459 ISalPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
570 580 590
....*....|....*....|....*....|...
gi 447124921 537 SRFQQIIVMDNGQIIEQGTHAELLARQGRYYQF 569
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
339-549 |
1.19e-71 |
|
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: 226.88 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLllaspgssdealseilrrvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447124921 499 DEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQ 549
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
338-554 |
4.73e-70 |
|
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: 224.78 E-value: 4.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-545 |
1.21e-69 |
|
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: 233.72 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 17 MLSLGIVLAIVTLLASIglltLSGWFLSASAVAGVAGLysfnymlpAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLR 96
Cdd:TIGR02857 13 VLGALLIIAQAWLLARV----VDGLISAGEPLAELLPA--------LGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 97 IYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLsfldFTLAFTLGGIMLLTLFL 176
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAV----FPQDWISGLILLLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 177 MPPLFYRAGKSTgQNLTHLRGQYRQQLTAW----LQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIML 252
Cdd:TIGR02857 157 IPIFMILIGWAA-QAAARKQWAALSRLSGHfldrLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 253 LIGALAVilmlwmasggvggnaqpgALIALFV---------------FCALAAFEALAPV--TGAFQHLG-QVIASAVRI 314
Cdd:TIGR02857 236 LFATLSV------------------ALVAVYIgfrllagdldlatglFVLLLAPEFYLPLrqLGAQYHARaDGVAAAEAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 315 SDLTDQKPEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQ 394
Cdd:TIGR02857 298 FAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 395 GEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGG 472
Cdd:TIGR02857 377 GSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAlpQGLDTPIGEGG 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 473 RQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVM 545
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
342-564 |
2.82e-69 |
|
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: 222.87 E-value: 2.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 342 RDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQ 421
Cdd:cd03254 6 ENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 RVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEDA--GLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 500 EPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQG 564
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
340-569 |
2.43e-67 |
|
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: 218.18 E-value: 2.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPEQ-SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03249 2 EFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQF 569
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
339-568 |
2.56e-67 |
|
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: 218.25 E-value: 2.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRfpDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
243-565 |
1.03e-65 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 227.06 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 243 LTALSQAIMLLIGALAVILMLWMASGGvggNAQPGALIAlfvfCALAAFEALAPvtgafqhLGQVIASAVRIS------D 316
Cdd:TIGR03375 371 ATNFAQFIQQLVSVAIVVVGVYLISDG---ELTMGGLIA----CVMLSGRALAP-------LGQLAGLLTRYQqaktalQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 317 LTDQ--KPEVTFPDtQTRVADRVSLT----LRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAW 390
Cdd:TIGR03375 437 SLDElmQLPVERPE-GTRFLHRPRLQgeieFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLY 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 391 DPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWL 468
Cdd:TIGR03375 516 QPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRhpDGLDMQI 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 469 GEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNG 548
Cdd:TIGR03375 596 GERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNG 675
|
330
....*....|....*....
gi 447124921 549 QIIEQGTHAELLA--RQGR 565
Cdd:TIGR03375 676 RIVADGPKDQVLEalRKGR 694
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-568 |
2.92e-65 |
|
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: 212.86 E-value: 2.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLE--DAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-568 |
4.28e-65 |
|
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: 223.16 E-value: 4.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 1 MRALLPYLALYKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNyMLPAAGVRGAAITRTAGRYFE 80
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALL-VVPVGLLLAYGLLRLLSVLFG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 81 RLvsHDATF-RVLQH-LRIY---TFSKLLPLSPaglaRY---RQ-GEL---LNRVVADVDTLDHLYLRVISPLVgaFVVI 148
Cdd:COG5265 96 EL--RDALFaRVTQRaVRRLaleVFRHLHALSL----RFhleRQtGGLsrdIERGTKGIEFLLRFLLFNILPTL--LEIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 149 MVVTIGLSFLDFTLAF-TLGGIMLLTLFlmpplFYRAgkstgqnlTHLRGQYRQQLTAwLQGQA-----------ElTI- 215
Cdd:COG5265 168 LVAGILLVKYDWWFALiTLVTVVLYIAF-----TVVV--------TEWRTKFRREMNE-ADSEAntravdsllnyE-TVk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 216 -FGA----SDRYRTQLEnteiQWLEAQRR-QSELTALS--QAimlLIGALAVILMLWMASGGV-GGNAQPGALIALFVFc 286
Cdd:COG5265 233 yFGNeareARRYDEALA----RYERAAVKsQTSLALLNfgQA---LIIALGLTAMMLMAAQGVvAGTMTVGDFVLVNAY- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 287 ALAAFEALapvtgafQHLG-------QVIASAVRISDLTDQKPEVT-FPDTQTRVADRVSLTLRDVQFTYpEQSQQALKG 358
Cdd:COG5265 305 LIQLYIPL-------NFLGfvyreirQALADMERMFDLLDQPPEVAdAPDAPPLVVGGGEVRFENVSFGY-DPERPILKG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLAS 438
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 439 PGSSDEALSEILRRVGLEKLLEDA--GLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILEL 516
Cdd:COG5265 457 PDASEEEVEAAARAAQIHDFIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAA 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 447124921 517 LAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:COG5265 537 LREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-568 |
1.47e-62 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 216.04 E-value: 1.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 2 RALLPYLALYKrhkwmlsLGIVLAIVTL----LASIGLLTL------SGWFLSASAVAGVAGLYSFNYMLpaagVRGaaI 71
Cdd:PRK11176 14 RRLWPTIAPFK-------AGLIVAGVALilnaASDTFMLSLlkplldDGFGKADRSVLKWMPLVVIGLMI----LRG--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 72 TRTAGRYFERLVSHdatfRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDtldhlylRVISPLVGAFVVIM-- 149
Cdd:PRK11176 81 TSFISSYCISWVSG----KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSE-------QVASSSSGALITVVre 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 150 -VVTIGLSFLDFTLAFTLGgimlLTLFLMPPL-----------FYRAGKSTGQNLTHLRGQYRQQLtawlQGQAELTIFG 217
Cdd:PRK11176 150 gASIIGLFIMMFYYSWQLS----LILIVIAPIvsiairvvskrFRNISKNMQNTMGQVTTSAEQML----KGHKEVLIFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 218 ASdryrtQLENTEIQWLEAQRRQSEL-----TALSQAIMLLIGALAVILMLWMAS-GGVGGNAQPGALIALF--VFCALA 289
Cdd:PRK11176 222 GQ-----EVETKRFDKVSNRMRQQGMkmvsaSSISDPIIQLIASLALAFVLYAASfPSVMDTLTAGTITVVFssMIALMR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 290 AFEALAPVTGAFQhlgQVIASAVRISDLTDQKPEVtfpDTQTRVADRVS--LTLRDVQFTYPEQSQQALKGISLQVNAGE 367
Cdd:PRK11176 297 PLKSLTNVNAQFQ---RGMAACQTLFAILDLEQEK---DEGKRVIERAKgdIEFRNVTFTYPGKEVPALRNINFKIPAGK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 368 HIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGS-SDEAL 446
Cdd:PRK11176 371 TVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 447 SEILRRVG----LEKLleDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMR 522
Cdd:PRK11176 451 EEAARMAYamdfINKM--DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 447124921 523 EKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:PRK11176 529 NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
342-555 |
6.24e-60 |
|
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: 198.10 E-value: 6.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 342 RDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQ 421
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 RVHLFSATLRDNLllaSP--GSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:cd03244 86 DPVLFSGTIRSNL---DPfgEYSDEELWQALERVGLKEFVESlpGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGT 555
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
331-569 |
1.05e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 197.49 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 331 TRVADRVslTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA 410
Cdd:PRK13657 329 GRVKGAV--EFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLE--DAGLNSWLGEGGRQLSGGELRRLAIARA 488
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAA 565
|
.
gi 447124921 569 F 569
Cdd:PRK13657 566 L 566
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
277-569 |
3.49e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 193.52 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 277 GALIALFV--FCALAAFEALAPVT--GAFQHL-GQVIASAVRISDLTD-QKPEVTFPDTQTRVADRVSLTLRDVQFTYPe 350
Cdd:PRK11174 282 GTGVTLFAgfFVLILAPEFYQPLRdlGTFYHAkAQAVGAAESLVTFLEtPLAHPQQGEKELASNDPVTIEAEDLEILSP- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTrAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATL 430
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDAT 508
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLlpQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 509 TESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQF 569
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-571 |
6.60e-52 |
|
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: 177.68 E-value: 6.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQFKQ 571
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
339-553 |
1.75e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 176.00 E-value: 1.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYP--EQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQ---LTRawdPQQGEILLNDSPIASLNEAAL- 412
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 413 ---RQTISVVPQRVHLF-SATLRDNLLLA------SPGSSDEALSEILRRVGLEKLLEDaglnswlgeggR--QLSGGEL 480
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLpELTALENVALPlllagvSRKERRERARELLERVGLGDRLDH-----------RpsQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 481 RRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRFQQIIVMDNGQIIEQ 553
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
339-563 |
4.59e-50 |
|
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: 172.52 E-value: 4.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQ--RVHLFSATLRDNLLLaSP---GSSDEalsEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAF-GPenlGLPRE---EIRERV--EEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSR-FQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-550 |
6.45e-50 |
|
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: 171.52 E-value: 6.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQS--QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL---- 412
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 413 RQTISVVPQRVHL---FSAtlRDNLLLA------SPGSSDEALSEILRRVGLEKLLEdaglnswlgEGGRQLSGGELRRL 483
Cdd:cd03255 81 RRHIGFVFQSFNLlpdLTA--LENVELPlllagvPKKERRERAEELLERVGLGDRLN---------HYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRFQQIIVMDNGQI 550
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-549 |
6.41e-49 |
|
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: 168.80 E-value: 6.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVP 420
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 Q--RVHLFSATLRDNLLLaSPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAF-GLENLGLPEEEIEERV--EEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447124921 499 DEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQ 549
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
338-568 |
1.88e-47 |
|
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: 176.47 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:TIGR01193 473 DIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSATLRDNLLL-ASPGSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENmpLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEmMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
243-566 |
1.31e-46 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 173.98 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 243 LTALSQAIMLLIGALAVIlmlwmasggvGGNAQPGALIAlfvFCAL-AAFeaLAPVT---GAFQHLGQVIASAVRISDLT 318
Cdd:TIGR03796 386 LTSLNSALILVVGGLRVM----------EGQLTIGMLVA---FQSLmSSF--LEPVNnlvGFGGTLQELEGDLNRLDDVL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 319 DQKPEVTFPDTQTRVAD-----RVS--LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD 391
Cdd:TIGR03796 451 RNPVDPLLEEPEGSAATsepprRLSgyVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 392 PQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALS----------EILRRVGleklled 461
Cdd:TIGR03796 531 PWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVrackdaaihdVITSRPG------- 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 462 aGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEmmREKTVLMVTHRLRGLSRFQQ 541
Cdd:TIGR03796 604 -GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDE 680
|
330 340
....*....|....*....|....*
gi 447124921 542 IIVMDNGQIIEQGTHAELLARQGRY 566
Cdd:TIGR03796 681 IIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-562 |
2.31e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.54 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLLASpGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFA-RLYGLPRKEARERI--DELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-571 |
3.86e-46 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 170.66 E-value: 3.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 27 VTLLASIGLLTLSGWFLSASAVAGV-AGLYSFNYMLPAAGVRGA-AITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLL 104
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDGVtEQHMTTGQILMWIGTMVLiAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 105 PLSPAGLARYRQGELLNRVVADVDTL----DHLYLRVISPLVGAFVVIMVVTIGLSFldftlaftlgGIMLLTLFLMPpL 180
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVvfaaGEGVLTLVDSLVMGCAVLIVMSTQISW----------QLTLLALLPMP-V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 181 FYRAGKSTGQNLtHLRGQYRQQLTAWL--QGQAELT------IFGASDRYRTQLENTEIQWLEAQRRQSELTA-LSQAIM 251
Cdd:PRK10789 150 MAIMIKRYGDQL-HERFKLAQAAFSSLndRTQESLTsirmikAFGLEDRQSALFAADAEDTGKKNMRVARIDArFDPTIY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 252 LLIGA---LAVILMLWMAsggVGGNAQPGALIALFVFCALAAFEALApVTGAFQHLGQVIASAVRISDLTDQKPEVTfPD 328
Cdd:PRK10789 229 IAIGManlLAIGGGSWMV---VNGSLTLGQLTSFVMYLGLMIWPMLA-LAWMFNIVERGSAAYSRIRAMLAEAPVVK-DG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 329 TQTRVADRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN 408
Cdd:PRK10789 304 SEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 409 EAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRrvgLEKLLED-----AGLNSWLGEGGRQLSGGELRRL 483
Cdd:PRK10789 384 LDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVAR---LASVHDDilrlpQGYDTEVGERGVMLSGGQKQRI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
570
....*....|.
gi 447124921 564 GRY---YQFKQ 571
Cdd:PRK10789 541 GWYrdmYRYQQ 551
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-562 |
8.99e-46 |
|
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: 161.51 E-value: 8.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPE--QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTI 416
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQrvhlfsatlrdnlllaSPGSS-------DEALSEILR-------RVGLEKLLEDAGLN-SWLGEGGRQLSGGELR 481
Cdd:COG1124 82 QMVFQ----------------DPYASlhprhtvDRILAEPLRihglpdrEERIAELLEQVGLPpSFLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAE 558
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVAD 225
|
....
gi 447124921 559 LLAR 562
Cdd:COG1124 226 LLAG 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
339-554 |
1.05e-45 |
|
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: 160.75 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQ--SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA---ALR 413
Cdd:cd03257 2 LEVKNLSVSFPTGggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QTISVVPQrvHLFSA---------TLRDNLLLASPGSSDEALSEI----LRRVGLEKlledaglnSWLGEGGRQLSGGEL 480
Cdd:cd03257 82 KEIQMVFQ--DPMSSlnprmtigeQIAEPLRIHGKLSKKEARKEAvlllLVGVGLPE--------EVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 481 RRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
339-560 |
1.19e-44 |
|
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: 158.67 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHL-FSATLRDNLLL---------ASPGSSDEAL-SEILRRVGLEKLLEdaglnswlgeggR---QLSGGELRRLA 484
Cdd:COG1120 80 VPQEPPApFGLTVRELVALgryphlglfGRPSAEDREAvEEALERTGLEHLAD------------RpvdELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-571 |
1.90e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 163.74 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 32 SIGLLTLSGWFLSASAVAG-VAGLYSFNYM-----LPAAGVRGAAIT-------RTAGRYFERLVSHDATFRVLQHLRIY 98
Cdd:PRK10790 24 PLGLAVLMLWVAAAAEVSGpLLISYFIDNMvakgnLPLGLVAGLAAAyvglqllAAGLHYAQSLLFNRAAVGVVQQLRTD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 99 TFSKLL--PLSpaglARYRQ--GELLNRVVADVDTLDHLYLRVIS------PLVGAFVVIMVVtiglsfLDFTLAftLGG 168
Cdd:PRK10790 104 VMDAALrqPLS----AFDTQpvGQLISRVTNDTEVIRDLYVTVVAtvlrsaALIGAMLVAMFS------LDWRMA--LVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 169 IMLLTLFLMPPLFYragkstgQNL-THLRGQYRQQLTAWLQGQAElTIFGAS--DRYRTQLENTEiQWLEAQRrqSELTA 245
Cdd:PRK10790 172 IMIFPAVLVVMVIY-------QRYsTPIVRRVRAYLADINDGFNE-VINGMSviQQFRQQARFGE-RMGEASR--SHYMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 246 LSQAIML----------LIGALAV--ILMLWMASGGvgGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVR 313
Cdd:PRK10790 241 RMQTLRLdgfllrpllsLFSALILcgLLMLFGFSAS--GTIEVGVLYA-FISYLGRLNEPLIELTTQQSMLQQAVVAGER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 314 ISDLTDQKPEVTFPDTQTRVADRVslTLRDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ 393
Cdd:PRK10790 318 VFELMDGPRQQYGNDDRPLQSGRI--DIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 394 QGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPgSSDEALSEILRRVGLEKLLED--AGLNSWLGEG 471
Cdd:PRK10790 395 EGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSlpDGLYTPLGEQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 472 GRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAeMMREKTVLMV-THRLRGLSRFQQIIVMDNGQI 550
Cdd:PRK10790 474 GNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVViAHRLSTIVEADTILVLHRGQA 552
|
570 580
....*....|....*....|.
gi 447124921 551 IEQGTHAELLARQGRYYQFKQ 571
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQMYQ 573
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
327-562 |
2.90e-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: 161.61 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 327 PDTQTRVADRVSLTLRDVQFTYPEQSQ---QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSP 403
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 404 IASLNEA---ALRQTISVVPQRVhlFSA-----TLRD-------NLLLASPGSSDEALSEILRRVGLEKLLEDAGlnswl 468
Cdd:COG1123 329 LTKLSRRslrELRRRVQMVFQDP--YSSlnprmTVGDiiaeplrLHGLLSRAERRERVAELLERVGLPPDLADRY----- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 469 gegGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVM 545
Cdd:COG1123 402 ---PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFISHDLAVVRYIaDRVAVM 478
|
250
....*....|....*..
gi 447124921 546 DNGQIIEQGTHAELLAR 562
Cdd:COG1123 479 YDGRIVEDGPTEEVFAN 495
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
87-570 |
7.99e-43 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 163.35 E-value: 7.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 87 ATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDhlylRVISPLVGAFVVIMVVTIGLSFLDFTLAFTL 166
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMS----RSLSLNVNVLLRNLVMLLGLLGFMLWLSPRL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 167 GgimLLTLFLMPPLFYragkstgqnLTHLRGQYRQQLTAWLQGQ-AELT--------------IFGA----SDRYRTQLE 227
Cdd:TIGR00958 304 T---MVTLINLPLVFL---------AEKVFGKRYQLLSEELQEAvAKANqvaeealsgmrtvrSFAAeegeASRFKEALE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 228 NTeiqwLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQV 307
Cdd:TIGR00958 372 ET----LQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 308 IASAVRISDLTDQKPEVTFPDTQTRVADRVSLTLRDVQFTYPEQ-SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQL 386
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 387 TRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLED--AGL 464
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEfpNGY 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 465 NSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDAttesQILELLAEMM--REKTVLMVTHRLRGLSRFQQI 542
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRsrASRTVLLIAHRLSTVERADQI 683
|
490 500
....*....|....*....|....*...
gi 447124921 543 IVMDNGQIIEQGTHAELLARQGRYYQFK 570
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
339-550 |
1.02e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLL----LASPGSSDEALSEILRRVGLEKLLEDAGLNswlgeggrQLSGGELRRLAIARALLHDAP 494
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDILDKPVE--------RLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQI 550
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
339-565 |
2.33e-42 |
|
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: 152.32 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQtISV 418
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLLASP--GSSDEalsEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAElyGLFDE---ELKKRI--EELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSR-FQQIIVMDNGQIIEQGTHAELLARQGR 565
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-554 |
2.51e-42 |
|
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: 149.89 E-value: 2.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVV 419
Cdd:cd03214 1 EVENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 420 PQrvhlfsatlrdnlllaspgssdealseILRRVGLEKLLeDAGLNswlgeggrQLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLA-DRPFN--------ELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 500 EPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-565 |
4.54e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.53 E-value: 4.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ---QGEILLNDSPIASLNEAALRQT 415
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQ--RVHLFSATLRDNLLLAsPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:COG1123 85 IGMVFQdpMTQLNPVTVGDQIAEA-LENLGLSRAEARARV--LELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQGR 565
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
339-549 |
7.38e-42 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 149.54 E-value: 7.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQA---LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpiaslneaalrqt 415
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQRVHLFSATLRDNLLLASPgsSDEA-LSEILRRVGLEKLLE--DAGLNSWLGEGGRQLSGGELRRLAIARALLHD 492
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEErYEKVIKACALEPDLEilPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 493 APLVLLDEPTEGLDATTESQILE--LLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQ 549
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
232-562 |
1.39e-41 |
|
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: 157.99 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 232 QWLEAQRRQSELTALSQAIMLLIGALAVILMLWMASG--GVG------GNAQPGALIAlfvfCALAAFEALAPV---TGA 300
Cdd:COG4618 219 RWQRANARALALQARASDRAGGFSALSKFLRLLLQSAvlGLGaylviqGEITPGAMIA----ASILMGRALAPIeqaIGG 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 301 FQHLGQVIASAVRISDLTDqkpevTFPDTQTRV---ADRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGC 377
Cdd:COG4618 295 WKQFVSARQAYRRLNELLA-----AVPAEPERMplpRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGS 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 378 GKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLllA-SPGSSDEALSEILRRVGLE 456
Cdd:COG4618 370 GKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ArFGDADPEKVVAAAKLAGVH 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 457 KL---LEDaGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEM-MREKTVLMVTHR 532
Cdd:COG4618 448 EMilrLPD-GYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHR 526
|
330 340 350
....*....|....*....|....*....|
gi 447124921 533 LRGLSRFQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG4618 527 PSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
339-558 |
2.39e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.66 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE---AALRQT 415
Cdd:COG2884 2 IRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQRVHLFSA-TLRDNLLLA------SPGSSDEALSEILRRVGLEKLLEDAGlnswlgeggRQLSGGELRRLAIARA 488
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALP---------HELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRFQQ-IIVMDNGQIIEQGTHAE 558
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-549 |
8.41e-41 |
|
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: 145.08 E-value: 8.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVV 419
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 420 PQrvhlfsatlrdnlllaspgssdealseilrrvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447124921 500 EPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQ 549
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
342-550 |
1.24e-40 |
|
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: 146.85 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 342 RDVQFTYPEQS-QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVP 420
Cdd:cd03248 15 QNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEDAGLNSW--LGEGGRQLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447124921 499 DEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQI 550
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-563 |
1.67e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.16 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQ----QLTrawdPQQGEILLNDSPIAslneaALRQ 414
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKailgLLP----PTSGTVRLFGKPPR-----RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 415 TISVVPQRVHL---FSATLRD---------NLLLASPGSSD-EALSEILRRVGLEKLLedaglNSWLGEggrqLSGGELR 481
Cdd:COG1121 76 RIGYVPQRAEVdwdFPITVRDvvlmgrygrRGLFRRPSRADrEAVDEALERVGLEDLA-----DRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSR-FQQIIVMdNGQIIEQGTHAEL 559
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEV 225
|
....
gi 447124921 560 LARQ 563
Cdd:COG1121 226 LTPE 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
339-550 |
4.69e-40 |
|
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: 143.51 E-value: 4.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLllaspgssdealseilrrvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447124921 499 DEPTEGLDATTESQILELLAEM-MREKTVLMVTHRLRGLSRFQQIIVMDNGQI 550
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
338-555 |
6.53e-40 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 144.48 E-value: 6.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSATLRDNLllaSPGS--SDEALSEILRrvgleklledaglnswLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL---DPFDeySDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGT 555
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
339-550 |
2.74e-38 |
|
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: 138.68 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLllaspgssdealseilrrvgleklledaglnswlgeggrQLSGGELRRLAIARALLHDAPLVL 497
Cdd:cd03230 78 LPEEPSLYENlTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSR-FQQIIVMDNGQI 550
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-561 |
4.32e-38 |
|
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: 140.50 E-value: 4.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 334 ADRVSLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA--- 410
Cdd:COG1127 1 MSEPMIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQRVHLFSA-TLRDNLLLA-------SPGSSDEALSEILRRVGLEkllEDAGLNSwlgeggRQLSGGELRR 482
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPlrehtdlSEAEIRELVLEKLELVGLP---GAADKMP------SELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 483 LAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEEL 229
|
..
gi 447124921 560 LA 561
Cdd:COG1127 230 LA 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-563 |
5.04e-38 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 140.51 E-value: 5.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFS-ATLRDNLLLAsPGSSDEALSEILRRVglEKLLEDAGL--NSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03295 80 VIQQIGLFPhMTVEENIALV-PKLLKWPKEKIRERA--DELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLaDRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-562 |
2.03e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 138.48 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQ--ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL---R 413
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QTISVVPQRVHLFSA-TLRDN--LLLASPGSSDealSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALL 490
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENvaLPLEIAGVPK---AEIEERV--LELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 491 HDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
339-562 |
2.40e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 141.37 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYP--EQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL---R 413
Cdd:COG1135 2 IELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QTISVVPQRVHLFSA-TLRDN----LLLAspGSSDEalsEILRRVglEKLLEDAGL----NSWLgeggRQLSGGELRRLA 484
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpLEIA--GVPKA---EIRKRV--AELLELVGLsdkaDAYP----SQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 485 IARALLHDaPLVLL-DEPTEGLDATTESQILELLAEMMRE--KTVLMVTH------RLrglsrFQQIIVMDNGQIIEQGT 555
Cdd:COG1135 151 IARALANN-PKVLLcDEATSALDPETTRSILDLLKDINRElgLTIVLITHemdvvrRI-----CDRVAVLENGRIVEQGP 224
|
....*..
gi 447124921 556 HAELLAR 562
Cdd:COG1135 225 VLDVFAN 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-552 |
3.55e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.68 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 334 ADRVSLTLRDVQFTYP--EQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIaslneAA 411
Cdd:COG1116 3 AAAPALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQRVHLFS-ATLRDNLLLA------SPGSSDEALSEILRRVGLEKLledagLNSWlgegGRQLSGGELRRLA 484
Cdd:COG1116 78 PGPDRGVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGF-----EDAY----PHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLR---GLSrfQQIIVMDN--GQIIE 552
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHDVDeavFLA--DRVVVLSArpGRIVE 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-502 |
3.73e-37 |
|
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: 134.70 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSA-TLRDNL 434
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 435 LLA------SPGSSDEALSEILRRVGLEKLLEDAglnswLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLGLGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-554 |
5.40e-37 |
|
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: 136.93 E-value: 5.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD-----PQQGEILLNDSPIASLNEA--A 411
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQRVHLFSATLRDNLLLAsPGSSDEALSEILRRVgLEKLLEDAGLnsWlGE-----GGRQLSGGELRRLAIA 486
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYG-LRLHGIKLKEELDER-VEEALRKAAL--W-DEvkdrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 487 RALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFG 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-562 |
1.05e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 139.03 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRD--VQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ---QGEILLNDSPIASLNEAALR 413
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 Q----TISVVPQ----------RVhlfSATLRDNLLLASPGSSDEALSEILRrvglekLLEDAGLNSWLGEGGR---QLS 476
Cdd:COG0444 82 KirgrEIQMIFQdpmtslnpvmTV---GDQIAEPLRIHGGLSKAEARERAIE------LLERVGLPDPERRLDRyphELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 477 GGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQII 551
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLgvvAEIA--DRVAVMYAGRIV 230
|
250
....*....|.
gi 447124921 552 EQGTHAELLAR 562
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
341-561 |
1.10e-36 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 136.48 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA---ALRQTIS 417
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSA-TLRDNLLLA-------SPGSSDEALSEILRRVGLEklledAGLNSWLGEggrqLSGGELRRLAIARAL 489
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPlrehtrlSEEEIREIVLEKLEAVGLR-----GAEDLYPAE----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 490 LHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLA 561
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
117-564 |
1.43e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.27 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 117 GELLNRVVADVDTLD-------HLYLRVISPLVGAFVVIMVVTiglsfldftlAFTLGGIM-LLTLFLMPPLFYragKST 188
Cdd:PLN03232 1007 GRVINRFSKDIGDIDrnvanlmNMFMNQLWQLLSTFALIGTVS----------TISLWAIMpLLILFYAAYLYY---QST 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 189 GQNLTHLRGQYRQQLTAW----LQGQAELTIFGASDRY------------RTQLENTEI-QWLEAQrrqseLTALSQAIM 251
Cdd:PLN03232 1074 SREVRRLDSVTRSPIYAQfgeaLNGLSSIRAYKAYDRMakingksmdnniRFTLANTSSnRWLTIR-----LETLGGVMI 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 252 LLIGALAVilmlwMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQKPEVTFPDTQT 331
Cdd:PLN03232 1149 WLTATFAV-----LRNGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENN 1223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 332 RVAD----RVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASL 407
Cdd:PLN03232 1224 RPVSgwpsRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 408 NEAALRQTISVVPQRVHLFSATLRDNLllaSPGS--SDEALSEILRRVGLEKLLEDA--GLNSWLGEGGRQLSGGELRRL 483
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSehNDADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLL 1380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
.
gi 447124921 564 G 564
Cdd:PLN03232 1461 T 1461
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
339-553 |
3.14e-36 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 134.52 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPE--QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAalrqtI 416
Cdd:cd03293 1 LEVRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLFS-ATLRDNLLLAsPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-LELQGVPKAEARERA--EELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLR---GLSrfQQIIVMDN--GQIIEQ 553
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVAE 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
352-562 |
3.32e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.12 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIA--SLNEAALRQTISVVPQRVHLFS-A 428
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFNLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLAsP-----GSSDEALS---EILRRVGL-EKLledaglNSWLGeggrQLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:COG1126 93 TVLENVTLA-PikvkkMSKAEAEEramELLERVGLaDKA------DAYPA----QLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 500 EPTEGLDATTESQILELLAEMMREK-TVLMVTHRLrglsRF-----QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGmTMVVVTHEM----GFarevaDRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
339-559 |
4.30e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.18 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQ---T 415
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQ--------------------RVHLFSATLRdnllLASPGSSDEALsEILRRVGL-EKLLEDAGlnswlgeggrQ 474
Cdd:COG3638 82 IGMIFQqfnlvprlsvltnvlagrlgRTSTWRSLLG----LFPPEDRERAL-EALERVGLaDKAYQRAD----------Q 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 475 LSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLrGLSR--FQQIIVMDNGQI 550
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQV-DLARryADRIIGLRDGRV 225
|
....*....
gi 447124921 551 IEQGTHAEL 559
Cdd:COG3638 226 VFDGPPAEL 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
339-563 |
2.20e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.57 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQAlkgiSLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAalRQTISV 418
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLLA-SPG---SSDE--ALSEILRRVGLEKLLEdaglnswlgeggR---QLSGGELRRLAIARA 488
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPGlklTAEQraQVEQALERVGLAGLLD------------RlpgQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGE 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
53-567 |
1.84e-34 |
|
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: 139.70 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 53 GLYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDAtfrvLQHLRIYTFSKLLPLSPAGlaryrqgELLNRVVADVDTLDH 132
Cdd:TIGR00957 1009 SVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQD----LLHNKLRSPMSFFERTPSG-------NLVNRFSKELDTVDS 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 133 LYLRVISPLVGA-FVVIMVVTIGLsfldftLAFTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQ----QLTAWL 207
Cdd:TIGR00957 1078 MIPPVIKMFMGSlFNVIGALIVIL------LATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSpvysHFNETL 1151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 208 QGQAELTIFGASDRYRTQ--LENTEIQ-----------WLEAQrrqseLTALSQAIMLLIGALAVIlmlwmasggvGGNA 274
Cdd:TIGR00957 1152 LGVSVIRAFEEQERFIHQsdLKVDENQkayypsivanrWLAVR-----LECVGNCIVLFAALFAVI----------SRHS 1216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 275 QPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQKPEVTFPDTQTRVAD----RVSLTLRDVQFTYPE 350
Cdd:TIGR00957 1217 LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSgwppRGRVEFRNYCLRYRE 1296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATL 430
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLllaSPGS--SDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLD 506
Cdd:TIGR00957 1377 RMNL---DPFSqySDEEVWWALELAHLKTFVSAlpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 507 ATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYY 567
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
339-561 |
2.50e-34 |
|
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: 129.48 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTIS 417
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLF-SATLRDNLLLASPGSSDEALSEILRRVgLE---KLLEDaglnswLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGAYARRRAKRKARLERV-YElfpRLKER------RKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLRG-LSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGvTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
334-552 |
4.98e-34 |
|
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: 129.09 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 334 ADRVSLTLRDvqftyPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE---A 410
Cdd:COG4181 11 LRGLTKTVGT-----GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALR-QTISVVPQRVHLFSA-TLRDN----LLLASPGSSDEALSEILRRVGLEKLLEDAGlnswlgeggRQLSGGELRRLA 484
Cdd:COG4181 86 RLRaRHVGFVFQSFQLLPTlTALENvmlpLELAGRRDARARARALLERVGLGHRLDHYP---------AQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRFQQIIVMDNGQIIE 552
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-554 |
5.23e-34 |
|
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: 5.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 343 DVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAslneaALRQTISVVPQR 422
Cdd:cd03235 4 DLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 423 VHL---FSATLRDNLLLA---------SPGSSD-EALSEILRRVGLEKLLEDAglnswLGEggrqLSGGELRRLAIARAL 489
Cdd:cd03235 77 RSIdrdFPISVRDVVLMGlyghkglfrRLSKADkAKVDEALERVGLSELADRQ-----IGE----LSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 490 LHDAPLVLLDEPTEGLDATTESQILELLAEM-MREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-551 |
1.16e-33 |
|
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: 126.99 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIaslNEAALRQTISVV 419
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 420 PQRV--HLFSATLRDNLLLASPGSSD--EALSEILRRVGLEKLLEDAGLNswlgeggrqLSGGELRRLAIARALLHDAPL 495
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPLS---------LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 496 VLLDEPTEGLDATTesqiLELLAEMMRE-----KTVLMVTHRLRGLSRF-QQIIVMDNGQII 551
Cdd:cd03226 148 LIFDEPTSGLDYKN----MERVGELIRElaaqgKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-561 |
2.97e-33 |
|
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: 127.02 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTIS 417
Cdd:COG0410 4 LEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSA-TLRDNLLL-ASPGSSDEALSEILRRVgLE---KLLEDaglnswLGEGGRQLSGGELRRLAIARALLHD 492
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLgAYARRDRAEVRADLERV-YElfpRLKER------RRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLR-GLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGvTILLVEQNARfALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
300-549 |
1.21e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 132.24 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 300 AFQHLGQVIASAVRISDLTD---QKPEVTFPDTQTRVADRVSLTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTG 376
Cdd:COG4178 321 NYQSLAEWRATVDRLAGFEEaleAADALPEAASRIETSEDGALALEDLTLRTP-DGRPLLEDLSLSLKPGERLLITGPSG 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 377 CGKSTLLQQLTRAWDPQQGEILLNDspiaslneaalRQTISVVPQRVHLFSATLRDNLLLASPGS--SDEALSEILRRVG 454
Cdd:COG4178 400 SGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 455 LEKLLE--DAGLNsWlgegGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHR 532
Cdd:COG4178 469 LGHLAErlDEEAD-W----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
250
....*....|....*..
gi 447124921 533 LRGLSRFQQIIVMDNGQ 549
Cdd:COG4178 544 STLAAFHDRVLELTGDG 560
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
329-554 |
1.25e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 329 TQTRVADRVSLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD--PQQ---GEILLNDSP 403
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 404 I--ASLNEAALRQTISVVPQRVHLFSATLRDNLLLA-------SPGSSDEalseilrRVglEKLLEDAGLnsW------L 468
Cdd:COG1117 80 IydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDE-------IV--EESLRKAAL--WdevkdrL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 469 GEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLrglsrfQQ------- 541
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM------QQaarvsdy 222
|
250
....*....|...
gi 447124921 542 IIVMDNGQIIEQG 554
Cdd:COG1117 223 TAFFYLGELVEFG 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
339-549 |
1.72e-32 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 123.07 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE--AALRQTI 416
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLFS-ATLRDNLLLAspgssdealseilrrvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPL 495
Cdd:cd03229 79 GMVFQDFALFPhLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQ 549
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-559 |
2.24e-32 |
|
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: 124.15 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLLASP--GSSDEALSEILrrvglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYARlkGLPKSEIKEEV-----ELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
339-550 |
4.40e-32 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 123.02 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI--ASLNEAALRQTI 416
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLFS-ATLRDNLLLA-------SPGSSDEALSEILRRVGLEkllEDAglNSWlgegGRQLSGGELRRLAIARA 488
Cdd:cd03262 79 GMVFQQFNLFPhLTVLENITLApikvkgmSKAEAEERALELLEKVGLA---DKA--DAY----PAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLrGLSR--FQQIIVMDNGQI 550
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEM-GFARevADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
338-562 |
5.33e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.75 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLqqltRA----WDPQQGEILLNDSPIASLnEAALR 413
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL----RMiagfETPDSGRILLDGRDVTGL-PPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QtISVVPQRV----HLfsaTLRDN------LLLASPGSSDEALSEILRRVGLEKLledaglnswlgeGGR---QLSGGEL 480
Cdd:COG3842 78 N-VGMVFQDYalfpHL---TVAENvafglrMRGVPKAEIRARVAELLELVGLEGL------------ADRyphQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 481 RRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRlrglsrfQ--------QIIVMDNGQI 550
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHD-------QeealaladRIAVMNDGRI 214
|
250
....*....|..
gi 447124921 551 IEQGTHAELLAR 562
Cdd:COG3842 215 EQVGTPEEIYER 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
339-562 |
7.13e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.75 E-value: 7.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQS---QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAS----LNEAA 411
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQ--RVHLFSATLRDNLLLASPG---SSDEAL---SEILRRVGL-EKLLEDAGLnswlgeggrQLSGGELRR 482
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgvSEEDAKqkaREMIELVGLpEELLARSPF---------ELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 483 LAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
...
gi 447124921 560 LAR 562
Cdd:PRK13634 234 FAD 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
334-560 |
8.07e-32 |
|
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: 123.76 E-value: 8.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 334 ADRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA--- 410
Cdd:TIGR02769 5 VRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQ-RVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEDAGLNS-WLGEGGRQLSGGELRRLAIARA 488
Cdd:TIGR02769 85 AFRRDVQLVFQdSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
355-561 |
1.44e-31 |
|
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: 122.16 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL-RQTISVVPQRVHLFSA-TLRD 432
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 NLLLASPGSSDEALS----------------EILRRVGLEKLLED-AGlnswlgeggrQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03219 95 NVMVAAQARTGSGLLlararreereareraeELLERVGLADLADRpAG----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLA 561
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGiTVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
339-554 |
2.07e-31 |
|
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: 121.09 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLneAALRQTISV 418
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLF-SATLRDNLLLAsPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFG-LKLRGVPKAEIRARV--RELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLR-GLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
339-560 |
2.10e-31 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 122.12 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRawdpqqgeillnDSPIASLNEA-------- 410
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG------------DLPPTYGNDVrlfgerrg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 -----ALRQTISVVPQRVHLF---SATLRDNLL---LASPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGE 479
Cdd:COG1119 70 gedvwELRKRIGLVSPALQLRfprDETVLDVVLsgfFDSIGLYREPTDEQRERA--RELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 480 LRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLR-GLSRFQQIIVMDNGQIIEQGTH 556
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPK 227
|
....
gi 447124921 557 AELL 560
Cdd:COG1119 228 EEVL 231
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
339-559 |
2.92e-31 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 121.63 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD-----PQQGEILLNDSPIAS--LNEAA 411
Cdd:TIGR00972 2 IEIENLNLFYGEK--EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDkkIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQRVHLFSATLRDNLLLA--SPGSSDEA-LSEILrrvglEKLLEDAGLnsW------LGEGGRQLSGGELRR 482
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFPMSIYDNIAYGprLHGIKDKKeLDEIV-----EESLKKAAL--WdevkdrLHDSALGLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 483 LAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFYDGELVEYGPTEQI 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
339-542 |
3.30e-31 |
|
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: 120.28 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLLAS----PGSSDEALSEILRRVGLEKLLEDAGlnswlgeggRQLSGGELRRLAIARALLHDA 493
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV---------RQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRFQQI 542
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
351-561 |
3.63e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.10 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA---ALRQTISVVPQRVhlFS 427
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDS--IS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 428 A-----TLRDnlLLASPGSSDEALSEILRRVGLEKLLEDAGLN-SWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEP 501
Cdd:PRK10419 101 AvnprkTVRE--IIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 502 TEGLDATTESQILELLAEMMREKTV--LMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLA 561
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKLT 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-559 |
4.60e-31 |
|
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: 121.14 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQT--- 415
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQRVHL----------------FSATLRDNLLLASPGSSDEALsEILRRVGL-EKLLEDAGlnswlgeggrQLSGG 478
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvlsgrlgRRSTWRSLFGLFPKEEKQRAL-AALERVGLlDKAYQRAD----------QLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 479 ELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLrGLSR--FQQIIVMDNGQIIEQG 554
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQV-DLAReyADRIVGLKDGRIVFDG 227
|
....*
gi 447124921 555 THAEL 559
Cdd:cd03256 228 PPAEL 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-564 |
6.21e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 128.70 E-value: 6.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSATLRDNLllaSPGS--SDEALSEILRRVGLEKLLE--DAGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNL---DPFNehNDADLWESLERAHLKDVIRrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQG 564
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
338-562 |
8.38e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 128.36 E-value: 8.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSATLRDNLLLASPGSSDEALSEiLRRVGLEKLL--EDAGLNSWLGEGGRQLSGGELRRLAIARALL-HDAP 494
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDPFLEASSAEVWAA-LELVGLRERVasESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSG 1466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-561 |
1.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.57 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL--RQTI 416
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRV--HLFSATLRDNLLLaspGSSDEALS--EILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHD 492
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAF---GPLNLGLSkeEVEKRV--KEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLA 561
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-562 |
1.37e-30 |
|
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: 125.68 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 10 LYKRHKWMLSLGIVLAIVTLLASIGLLtlsgWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFERLvSHDATF 89
Cdd:COG4615 7 LLRESRWLLLLALLLGLLSGLANAGLI----ALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRL-GQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 90 RvlqhLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRvispLVGAFVVIMVVTIGLSFLdFTLAFTLGGI 169
Cdd:COG4615 82 R----LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR----LPELLQSVALVLGCLAYL-AWLSPPLFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 170 MLLTLFLMPPLFYRAGKSTGQNLTHLR---GQYRQQLTAWLQGQAELTIfgASDR----YRTQLENTEIQW----LEAQR 238
Cdd:COG4615 153 TLVLLGLGVAGYRLLVRRARRHLRRAReaeDRLFKHFRALLEGFKELKL--NRRRrrafFDEDLQPTAERYrdlrIRADT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 239 RQSELTALSQAIMLliGALAVILMLWMASGGVGGNAQPG-ALIALFVFCALAAfealapVTGAFQHLGQVIASAVRISDL 317
Cdd:COG4615 231 IFALANNWGNLLFF--ALIGLILFLLPALGWADPAVLSGfVLVLLFLRGPLSQ------LVGALPTLSRANVALRKIEEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 318 TDQ----KPEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQQ---ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAW 390
Cdd:COG4615 303 ELAlaaaEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 391 DPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFsatlrDNLLLASPGSSDEALSEILRRVGLEKLLEDaglnswlgE 470
Cdd:COG4615 383 RPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLERLELDHKVSV--------E 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 471 GGR----QLSGGELRRLAIARALLHDAPLVLLDE------PT------EgldattesqilELLAEMMRE-KTVLMVTHRL 533
Cdd:COG4615 450 DGRfsttDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPEfrrvfyT-----------ELLPELKARgKTVIAISHDD 518
|
570 580
....*....|....*....|....*....
gi 447124921 534 RGLSRFQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG4615 519 RYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
354-561 |
4.18e-30 |
|
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: 118.60 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL-RQTISVVPQRVHLFSA-TLR 431
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLA--------------SPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:COG0411 98 ENVLVAaharlgrgllaallRLPRARREEREARERA--EELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 498 LDEPTEGLDAtTESQ-ILELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQIIEQGTHAELLA 561
Cdd:COG0411 176 LDEPAAGLNP-EETEeLAELIRRLRDERgiTILLIEHDMdlvMGLA--DRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
356-562 |
4.73e-30 |
|
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: 117.82 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAalRQTISVVPQRVHLF-SATLRDNL 434
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 435 LLASPGSSDEAlSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQIL 514
Cdd:cd03299 93 AYGLKKRKVDK-KEIERKV--LEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447124921 515 ELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:cd03299 170 EELKKIRKEFgvTVLHVTHDFeeaWALA--DKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-562 |
1.01e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPiasLNEAA---LRQT 415
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETvwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQRV--HLFSATLRDNLL--LASPGSSDEalsEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLH 491
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAfgLENIGVPRE---EMVERV--DQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 492 DAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
338-558 |
1.46e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 118.23 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQS---QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIA--SLNEAAL 412
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 413 RQTISVVPQ--RVHLFSATL-RD------NLllaspGSSDEalsEILRRVglEKLLEDAGL--NSWLGEGGRQLSGGELR 481
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIeKDiafgpiNL-----GLSEE---EIENRV--KRAMNIVGLdyEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAE 558
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
337-573 |
1.66e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.96 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 337 VSLTLRDVQFTYPEQS---QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE---- 409
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 410 AALRQTISVVPQ--RVHLFSATLRDNLLLAsPGSSDEALSEILRRVglEKLLEDAGLN-SWLGEGGRQLSGGELRRLAIA 486
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 487 RALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKDK 237
|
250
....*....|
gi 447124921 564 GRYYQFKQGL 573
Cdd:PRK13646 238 KKLADWHIGL 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
338-560 |
1.99e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQrVHLF--SATLRDnlLLA---SP--------GSSDEALseilrrvgLEKLLEDAGLNSWLGEGGRQLSGGELRRLA 484
Cdd:PRK11231 80 LLPQ-HHLTpeGITVRE--LVAygrSPwlslwgrlSAEDNAR--------VNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYcDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-550 |
3.68e-29 |
|
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: 114.81 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAA---LRQTIS 417
Cdd:cd03292 3 FINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSA-TLRDNLLLASPgSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:cd03292 82 VVFQDFRLLPDrNVYENVAFALE-VTGVPPREIRKRV--PAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 497 LLDEPTEGLDATTESQILELLAEM-MREKTVLMVTHRLRGLSRFQ-QIIVMDNGQI 550
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
338-569 |
4.58e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 123.13 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIllndspiaslneaALRQTIS 417
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSATLRDNLLLASPgssdeaLSEILRRVGLE--KLLED-----AGLNSWLGEGGRQLSGGELRRLAIARALL 490
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKA------LNEKYYQQVLEacALLPDleilpSGDRTEIGEKGVNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 491 HDAPLVLLDEPTEGLDATTESQILELL---AEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYY 567
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
..
gi 447124921 568 QF 569
Cdd:TIGR00957 857 EF 858
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-562 |
4.77e-29 |
|
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: 120.94 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAwDPQQGEILLNDSPIASLNEAA---LRQTISVVPQ---------- 421
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQdpfgslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 RVhlfSATLRDNLLLASPGSSDEalsEILRRVglEKLLEDAGLN-SWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDE 500
Cdd:COG4172 380 TV---GQIIAEGLRVHGPGLSAA---ERRARV--AEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 501 PTEGLDATTESQILELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHglAYLFISHDLavvRALA--HRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
339-563 |
5.93e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA--ALRQTI 416
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRV--HLFSATLRDNLllaSPGSSDEAL--SEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHD 492
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDV---SFGAVNLKLpeDEVRKRV--DNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
336-554 |
6.15e-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: 113.41 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 336 RVSLTLRDVQFTYPEQSQQA----LKGISLQVNAGEHIAILGRTGCGKSTLLQQLT--RAWDPQQGEILLNDSPiasLNE 409
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRP---LDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 410 AALRQTISVVPQRVHLFSA-TLRDNLLLAspgssdealseilrrvgleklledAGLnswlgeggRQLSGGELRRLAIARA 488
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETLMFA------------------------AKL--------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGL--SRFQQIIVMDNGQIIEQG 554
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-560 |
6.89e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 335 DRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQ 414
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 415 TISVVPQRV--HLFSATLRDNLLLA------SPGSSDEALSEILRRVGLEKLLEDAGLNswlgeggrqLSGGELRRLAIA 486
Cdd:PRK13632 84 KIGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN---------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 487 RALLHDAPLVLLDEPTEGLDATTESQILELLAEM--MREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
340-562 |
6.94e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.59 E-value: 6.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPEQSQQ--ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL---RQ 414
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 415 TISVVPQRVHLFSA-TLRDN----LLLAspGSSDEalsEILRRVglEKLLEDAGL----NSWLGeggrQLSGGELRRLAI 485
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNvalpLELA--GTPKA---EIKARV--TELLELVGLsdkaDRYPA----QLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 486 ARALLHDaPLVLL-DEPTEGLD-ATTESqILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK11153 152 ARALASN-PKVLLcDEATSALDpATTRS-ILELLKDINRELglTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSEVF 229
|
..
gi 447124921 561 AR 562
Cdd:PRK11153 230 SH 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
355-564 |
3.05e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 114.79 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISVVPQRVHLFSA-TLRDN 433
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDlTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 434 LLLASpgsSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQI 513
Cdd:TIGR01188 87 LEMMG---RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447124921 514 LELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQG 564
Cdd:TIGR01188 164 WDYIRALKEEgVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-554 |
4.30e-28 |
|
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: 111.82 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQalkgISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAalRQTISV 418
Cdd:cd03298 1 VRLDKIRFSYGEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFS-ATLRDNLLLA-SPG-----SSDEALSEILRRVGLeklledAGLNSWLGeggRQLSGGELRRLAIARALLH 491
Cdd:cd03298 75 LFQENNLFAhLTVEQNVGLGlSPGlkltaEDRQAIEVALARVGL------AGLEKRLP---GELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 492 DAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSR-FQQIIVMDNGQIIEQG 554
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
339-563 |
4.96e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 112.37 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQalkgISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAalRQTISV 418
Cdd:PRK10771 2 LKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFS-ATLRDNLLLA-SPG-----SSDEALSEILRRVGLEKLLEDagLNSwlgeggrQLSGGELRRLAIARALLH 491
Cdd:PRK10771 76 LFQENNLFShLTVAQNIGLGlNPGlklnaAQREKLHAIARQMGIEDLLAR--LPG-------QLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 492 DAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
338-562 |
5.80e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.17 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLqqltRAW----DPQQGEILLNDSPIASLnEAALR 413
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLL----RMIagleDPTSGEILIGGRDVTDL-PPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QtISVVPQRVHLF-SATLRDNllLASP----GSS----DEALSEILRRVGLEKLLEdaglnswlgeggR---QLSGGELR 481
Cdd:COG3839 76 N-IAMVFQSYALYpHMTVYEN--IAFPlklrKVPkaeiDRRVREAAELLGLEDLLD------------RkpkQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDA----TTESQILELLAEMmrEKTVLMVTHRlrglsrfQ--------QIIVMDNGQ 549
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHD-------QveamtladRIAVMNDGR 211
|
250
....*....|...
gi 447124921 550 IIEQGTHAELLAR 562
Cdd:COG3839 212 IQQVGTPEELYDR 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-568 |
8.04e-28 |
|
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: 113.03 E-value: 8.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDpQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLllaSPGS--SDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-559 |
8.28e-28 |
|
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: 111.31 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIasLNEAA-LRQTISVVPQRVHLFSA-TLRD 432
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPReVRRRIGIVFQDLSVDDElTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 NLLLAS-----PGSS-DEALSEILRRVGL----EKLLedaglnswlgeggRQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:cd03265 93 NLYIHArlygvPGAErRERIDELLDFVGLleaaDRLV-------------KTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 503 EGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
352-560 |
1.18e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHL-FSATL 430
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLL-ASPGSS-----DEALSEILRRVGLEKLledaglnswlgeGGR---QLSGGELRRLAIARALL------HDAPL 495
Cdd:PRK13548 94 EEVVAMgRAPHGLsraedDALVAAALAQVDLAHL------------AGRdypQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-551 |
1.41e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 108.67 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTIS 417
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQrvhlfsatlrdnlllaspgssdealseilrrvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPLVL 497
Cdd:cd03216 79 MVYQ-----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQII 551
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
339-554 |
2.52e-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: 109.59 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeqSQQALKGISLQVNAGEHiAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFS-----------ATLRDnlllASPGSSDEALSEILRRVGLEKLLEDAglnswLGeggrQLSGGELRRLAIAR 487
Cdd:cd03264 77 LPQEFGVYPnftvrefldyiAWLKG----IPSKEVKARVDEVLELVNLGDRAKKK-----IG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 488 ALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-562 |
4.84e-27 |
|
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: 115.17 E-value: 4.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRD--VQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKS----TLLQQLTRAWDPQQGEILLNDSPIASLNEAAL 412
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 413 RQ----TISVVPQR-------VHLFSATLRDNLLLASPGSSDEALSEI---LRRVGLEkllEDAG-LNSWlgegGRQLSG 477
Cdd:COG4172 87 RRirgnRIAMIFQEpmtslnpLHTIGKQIAEVLRLHRGLSGAAARARAlelLERVGIP---DPERrLDAY----PHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 478 GELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFaDRVAVMRQGEIVEQG 239
|
....*...
gi 447124921 555 THAELLAR 562
Cdd:COG4172 240 PTAELFAA 247
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
355-561 |
6.95e-27 |
|
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: 110.04 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQ----TISVVPQRVHLF-SAT 429
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 430 LRDNlllASPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:cd03294 119 VLEN---VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 510 ----ESQILELLAEMmrEKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLA 561
Cdd:cd03294 196 rremQDELLRLQAEL--QKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
353-569 |
1.07e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.07 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 353 QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI---ASLNEA-----ALRQTISVVPQRVH 424
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 425 LFS-ATLRDNLLLA------SPGSSDEALS-EILRRVGLEKlLEDAglnswlgeGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:PRK11264 96 LFPhRTVLENIIEGpvivkgEPKEEATARArELLAKVGLAG-KETS--------YPRRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLrGLSR--FQQIIVMDNGQIIEQGTHAELLA--RQGRYYQF 569
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEM-SFARdvADRAIFMDQGRIVEQGPAKALFAdpQQPRTRQF 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
339-568 |
1.11e-26 |
|
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: 115.78 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDpQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLllaSPGS--SDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQfpDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQ 568
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
352-559 |
1.71e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 107.71 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLneAALRQTISVVPQRVHLFS-ATL 430
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLLA------SPGSSDEALSEILRRVGLEklledaglnswlGEGGR---QLSGGELRRLAIARALLHDAPLVLLDEP 501
Cdd:cd03300 90 FENIAFGlrlkklPKAEIKERVAEALDLVQLE------------GYANRkpsQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 502 TEGLDATTESQILELLAEMMRE--KTVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKElgITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
339-561 |
2.34e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.41 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQ---QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEI--LLNDSPIASLNEA--- 410
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 -------------------ALRQTISVVPQ--RVHLFSATLRDNLLLA--SPGSSDEALSEILRrvgleKLLEDAGLN-S 466
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEEAKKRAA-----KYIELVGLDeS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 467 WLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRL-RGLSRFQQIIV 544
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTIF 237
|
250
....*....|....*..
gi 447124921 545 MDNGQIIEQGTHAELLA 561
Cdd:PRK13651 238 FKDGKIIKDGDTYDILS 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
357-562 |
3.21e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 107.86 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 357 KGISLQVNAGEHIAILGRTGCGKS----TLLQQLTRAWDPQQGEILLNDSPIASlneAALR-QTISVVPQR-------VH 424
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRgRKIATIMQNprsafnpLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 425 LFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEDAGLNSWlgeggrQLSGGELRRLAIARALLHDAPLVLLDEPTEG 504
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPF------EMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 505 LDATTESQILELLAEMMREKT--VLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNA 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
339-531 |
5.01e-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: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPE--QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlnEAALRqti 416
Cdd:COG4525 4 LTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLFS-ATLRDNLLLA------SPGSSDEALSEILRRVGLEKLledAGLNSWlgeggrQLSGGELRRLAIARAL 489
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlrgvPKAERRARAEELLALVGLADF---ARRRIW------QLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447124921 490 LHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTH 531
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
345-554 |
7.72e-26 |
|
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: 105.82 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 345 QFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLT---RAWDPQQGEILLNDSPiasLNEAALRQTISVVPQ 421
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQP---RKPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 ----------RVHL-FSATLRDNLLLASPGSSDEALSEILRRVGLEKLledaglnswlgeGG---RQLSGGELRRLAIAR 487
Cdd:cd03234 89 ddillpgltvRETLtYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRI------------GGnlvKGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 488 ALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRG--LSRFQQIIVMDNGQIIEQG 554
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRnRIVILTIHQPRSdlFRLFDRILLLSSGEIVYSG 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
354-562 |
1.18e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.90 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALR------QTI------SVVP- 420
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrrrmQMVfqdpyaSLNPr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRVhlfSATLRDNLL---LASPGSSDEALSEILRRVGLEKllEDAglnswlgegGR---QLSGGELRRLAIARALLHDAP 494
Cdd:COG4608 112 MTV---GDIIAEPLRihgLASKAERRERVAELLELVGLRP--EHA---------DRyphEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDELglTYLFISHDLsvvRHIS--DRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-563 |
1.40e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.20 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAlRQTISV 418
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHL---FsaTLRDNLLLASpgsSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK13537 85 VPQFDNLdpdF--TVRENLLVFG---RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMM-REKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-560 |
4.40e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 109.75 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLT--RAWDPQ-QGEILLNDSPIaslnEAALRQTISVVPQRVHLF--SATL 430
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrSPKGVKgSGSVLLNGMPI----DAKEMRAISAYVQQDDLFipTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLLASPGSSDEALSEILRRVGLEKLLEDAGL----NSWLGEGGRQ--LSGGELRRLAIARALLHDAPLVLLDEPTEG 504
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 505 LDATTESQILELLAEM-MREKTVLMVTH----RLRGLsrFQQIIVMDNGQIIEQGTHAELL 560
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLaQKGKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGSPDQAV 255
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
77-559 |
1.36e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 109.30 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 77 RYFERLVShdATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMvvTIGLS 156
Cdd:PLN03232 360 QYFQNVGR--VGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIV--SMVLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 157 FLDFTLAFTLGGimlLTLFLMPP----LFYRAGKSTGQNL--THLRGQYRQQLTAWLQgQAELTIFGASDRYRTQ-LENT 229
Cdd:PLN03232 436 YQQLGVASLFGS---LILFLLIPlqtlIVRKMRKLTKEGLqwTDKRVGIINEILASMD-TVKCYAWEKSFESRIQgIRNE 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 230 EIQWLeaqrRQSELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGAlialfVFCALAAFEAL-APVTGAFQHLGQVI 308
Cdd:PLN03232 512 ELSWF----RKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPAR-----AFTSLSLFAVLrSPLNMLPNLLSQVV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 309 ASAV---RISDL--TDQKPEVTFPDTQTRVAdrvSLTLRDVQFTYPEQ-SQQALKGISLQVNAGEHIAILGRTGCGKSTL 382
Cdd:PLN03232 583 NANVslqRIEELllSEERILAQNPPLQPGAP---AISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSL 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 383 LQQLtrawdpqqgeilLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSdealSEILRRVGLEKLLEDA 462
Cdd:PLN03232 660 ISAM------------LGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFES----ERYWRAIDVTALQHDL 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 463 GL-----NSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILE-LLAEMMREKTVLMVTHRLRGL 536
Cdd:PLN03232 724 DLlpgrdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTNQLHFL 803
|
490 500
....*....|....*....|...
gi 447124921 537 SRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:PLN03232 804 PLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-554 |
1.47e-24 |
|
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: 101.52 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpIASLNEAALRQtISV 418
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK-SYQKNIEALRR-IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLLAS--PGSSDEALSEILRRVGLEklledaglnswlGEGGR---QLSGGELRRLAIARALLHD 492
Cdd:cd03268 77 LIEAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVVGLK------------DSAKKkvkGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
338-531 |
2.11e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ---QGEILLNDSPIASLNeAALRQ 414
Cdd:COG4136 1 MLSLENLTITL--GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP-AEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 415 tISVVPQRVHLFS-ATLRDNLLLASPgssdEALSEILRRVGLEKLLEDAGLNswlGEGGR---QLSGGELRRLAIARALL 490
Cdd:COG4136 78 -IGILFQDDLLFPhLSVGENLAFALP----PTIGRAQRRARVEQALEEAGLA---GFADRdpaTLSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447124921 491 HDAPLVLLDEPTEGLDATTESQILELLAEMMREKT--VLMVTH 531
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGipALLVTH 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
339-559 |
4.89e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTIS 417
Cdd:COG1129 5 LEMRGISKSFG--GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSA-TLRDNLLL----ASPGSSD-----EALSEILRRVGLE----KLLEDaglnswLGEGGRQLsggelrrL 483
Cdd:COG1129 83 IIHQELNLVPNlSVAENIFLgrepRRGGLIDwramrRRARELLARLGLDidpdTPVGD------LSVAQQQL-------V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLdatTESQIlELLAEMMRE-----KTVLMVTHRL---RGLSrfQQIIVMDNGQIIEQGT 555
Cdd:COG1129 150 EIARALSRDARVLILDEPTASL---TEREV-ERLFRIIRRlkaqgVAIIYISHRLdevFEIA--DRVTVLRDGRLVGTGP 223
|
....
gi 447124921 556 HAEL 559
Cdd:COG1129 224 VAEL 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
352-561 |
5.04e-24 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 100.81 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN--EAAlRQTISVVPQRVHLFSA- 428
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERA-RLGIGYLPQEASIFRKl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLASPGSSDeaLSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDAT 508
Cdd:TIGR04406 92 TVEENIMAVLEIRKD--LDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 509 TES---QILELLAEmmREKTVLMVTHRLR-GLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:TIGR04406 170 AVGdikKIIKHLKE--RGIGVLITDHNVReTLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
355-569 |
7.12e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.40 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD-----PQQGEILLNDSPI--ASLNEAALRQTISVVPQRVHLFS 427
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 428 ATLRDNL-----LLASPGSSDEALSEILRRVGLEKLLEDAglnswLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:PRK14243 105 KSIYDNIaygarINGYKGDMDELVERSLRQAALWDEVKDK-----LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 503 EGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGThaellaRQGRYYQF 569
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLVEF 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-554 |
7.74e-24 |
|
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: 99.68 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNaGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI----ASLNEAALRQTISVVPQRVHLFS-ATLRDN 433
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPhLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 434 LLLASPGSSDealSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQI 513
Cdd:cd03297 96 LAFGLKRKRN---REDRISV--DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447124921 514 LELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03297 171 LPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-563 |
8.19e-24 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 106.53 E-value: 8.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpiaslneaalrqtISVVPQRVHLFSATLRDNLL 435
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 436 LASpgSSDE-ALSEILRRVGLEkllEDAGL-----NSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:TIGR01271 509 FGL--SYDEyRYTSVIKACQLE---EDIALfpekdKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 510 ESQILE-LLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:TIGR01271 584 EKEIFEsCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-559 |
8.52e-24 |
|
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: 100.49 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNeaALRQTISVVPQRVHLFS-ATLRD 432
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERNVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 NL---LLASPGSSDEALSEILRRVglEKLLEDAGLnSWLGEggR---QLSGGELRRLAIARALLHDAPLVLLDEPTEGLD 506
Cdd:cd03296 94 NVafgLRVKPRSERPPEAEIRAKV--HELLKLVQL-DWLAD--RypaQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 507 ATTESQILELLAEMMREK--TVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:cd03296 169 AKVRKELRRWLRRLHDELhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-563 |
8.72e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVP 420
Cdd:PRK13647 7 VEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRV--HLFSATLRDNLLLAsPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLL 498
Cdd:PRK13647 86 QDPddQVFSSTVWDDVAFG-PVNMGLDKDEVERRV--EEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 499 DEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLR-GLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
338-557 |
9.04e-24 |
|
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: 9.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI---ASLNEAA--- 411
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQRVHLFS-ATLRDNLLLA-------SPGSSDEALSEILRRVGLEKLLEDAGLnswlgeggrQLSGGELRRL 483
Cdd:COG4161 80 LRQKVGMVFQQYNLWPhLTVMENLIEApckvlglSKEQAREKAMKLLARLRLTDKADRFPL---------HLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMR-EKTVLMVTHRLrGLSR--FQQIIVMDNGQIIEQGTHA 557
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEV-EFARkvASQVVYMEKGRIIEQGDAS 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
339-531 |
1.05e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.52 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIaslneAALRQTISV 418
Cdd:PRK11247 13 LLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFS-ATLRDNLLLASPGSSDEALSEILRRVGLEkllEDAglNSWLGeggrQLSGGELRRLAIARALLHDAPLVL 497
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLA---DRA--NEWPA----ALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMREK--TVLMVTH 531
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTH 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
341-568 |
1.12e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.27 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSQQAL-KGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD---------------------------- 391
Cdd:PTZ00265 1168 IMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdee 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 392 --------------------------PQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEA 445
Cdd:PTZ00265 1248 qnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATRED 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 446 LSEILRRVGLEKLLEDA--GLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEM--M 521
Cdd:PTZ00265 1328 VKRACKFAAIDEFIESLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdK 1407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447124921 522 REKTVLMVTHRLRGLSRFQQIIVMDN----GQIIE-QGTHAELLARQGRYYQ 568
Cdd:PTZ00265 1408 ADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYK 1459
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
337-563 |
1.14e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 337 VSLTLRDVQFTY-PEQSQQA--LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI----ASLNE 409
Cdd:PRK13641 1 MSIKFENVDYIYsPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 410 AALRQTISVVPQ--RVHLFSATLRDNLLL------ASPGSSDEALSEILRRVGL-EKLLEDAGLnswlgeggrQLSGGEL 480
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFgpknfgFSEDEAKEKALKWLKKVGLsEDLISKSPF---------ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 481 RRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAE 558
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYaDDVLVLEHGKLIKHASPKE 231
|
....*
gi 447124921 559 LLARQ 563
Cdd:PRK13641 232 IFSDK 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
352-555 |
1.41e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAA---LR-QTISVVPQRVHL-- 425
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLlp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 426 -FSA--TLRDNLLL--ASPGSSDEALSEILRRVGLEKLLEdaglnswlgEGGRQLSGGELRRLAIARALLHDAPLVLLDE 500
Cdd:PRK11629 101 dFTAleNVAMPLLIgkKKPAEINSRALEMLAAVGLEHRAN---------HRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 501 PTEGLDATTESQILELLAEM-MREKTV-LMVTHRLRGLSRFQQIIVMDNGQIIEQGT 555
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
356-560 |
1.77e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.53 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWdPQQGEILLNDSPIASLNEAALRQTISVVPQR-VHLFSATLRDNL 434
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 435 LLASPGSSDEALSEILrrvgLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLH-------DAPLVLLDEPTEGLDA 507
Cdd:COG4138 91 ALHQPAGASSEAVEQL----LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 508 TTESQILELLAEMMRE-KTVLMVTHRL-RGLSRFQQIIVMDNGQIIEQGTHAELL 560
Cdd:COG4138 167 AQQAALDRLLRELCQQgITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
339-563 |
1.89e-23 |
|
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: 99.98 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLllaSP--GSSDEALSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:cd03288 100 ILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSlpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
338-573 |
2.28e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLND------SPIASLNEAA 411
Cdd:PRK11124 2 SIQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQRVHLFS-ATLRDNLLLAsPG-----SSDEALS---EILRRVGLEKLLEDAGLnswlgeggrQLSGGELRR 482
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLIEA-PCrvlglSKDQALAraeKLLERLRLKPYADRFPL---------HLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 483 LAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRLrGLSR--FQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEV-EVARktASRVVYMENGHIVEQGDASCF 228
|
250
....*....|....
gi 447124921 560 LARQGRyyQFKQGL 573
Cdd:PRK11124 229 TQPQTE--AFKNYL 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
339-531 |
2.73e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTypEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:PRK10247 8 LQLQNVGYL--AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLL----LASPGSSDEALSEILRRVGLEKLLEDAGLNswlgeggrQLSGGELRRLAIARALLHDAP 494
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIfpwqIRNQQPDPAIFLDDLERFALPDTILTKNIA--------ELSGGEKQRISLIRNLQFMPK 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTH 531
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTH 196
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-551 |
2.77e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.39 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVV---PQRVHLFSATLR 431
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVfqdPMMGTAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLA---------SPGSSD---EALSEILRRV--GLEKLLED-AGLnswlgeggrqLSGGELRRLAIARALLHDAPLV 496
Cdd:COG1101 101 ENLALAyrrgkrrglRRGLTKkrrELFRELLATLglGLENRLDTkVGL----------LSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLR-----GlSRfqqIIVMDNGQII 551
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqaldyG-NR---LIMMHEGRII 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
354-554 |
3.12e-23 |
|
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: 97.74 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAslneAALRQTISVVPQRVHLF-SATLRD 432
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYpKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 NLL-LASpgSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTES 511
Cdd:cd03269 90 QLVyLAQ--LKGLKKEEARRRI--DEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447124921 512 QILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03269 166 LLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-562 |
3.27e-23 |
|
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: 101.33 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 353 QQALKGISLQVN----AGEHIAILGRTGCGKSTLLQQ---LTRawdPQQGEILLNDSPI----ASLNEAALRQTISVVPQ 421
Cdd:COG4148 8 RLRRGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 RVHLFS-ATLRDNLLL----ASPGSSDEALSEILRRVGLEKLLEdaglnswlgeggR---QLSGGELRRLAIARALLHDA 493
Cdd:COG4148 85 EARLFPhLSVRGNLLYgrkrAPRAERRISFDEVVELLGIGHLLD------------RrpaTLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLaEMMREKT---VLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYL-ERLRDELdipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
339-554 |
3.69e-23 |
|
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: 97.71 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLnEAALRQtISV 418
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLF-SATLRDNLL--LASPGSSDEALSEILRRVGleKLLedaGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAfgLKLRKVPKDEIDERVREVA--ELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTH-RLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
339-560 |
4.07e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:PRK09536 4 IDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHL-FSATLRDNLLLA-SPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGrTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
338-562 |
4.40e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.61 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQ---QLTRawdPQQGEILLNDSpIASLNEAALRQ 414
Cdd:COG1118 2 SIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRiiaGLET---PDSGRIVLNGR-DLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 415 TISVVPQ-----RvHLfsaTLRDNL---LLASPGSSDealsEILRRVglEKLLEDAGLnSWLGEggR---QLSGGELRRL 483
Cdd:COG1118 76 RVGFVFQhyalfP-HM---TVAENIafgLRVRPPSKA----EIRARV--EELLELVQL-EGLAD--RypsQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTH------RLRglsrfQQIIVMDNGQIIEQGT 555
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGT 217
|
....*..
gi 447124921 556 HAELLAR 562
Cdd:COG1118 218 PDEVYDR 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-561 |
5.74e-23 |
|
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: 97.61 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASL--NEAAlRQTI 416
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRA-RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLF-SATLRDNLLLA--SPGSSDEALSEILrrvglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:cd03218 78 GYLPQEASIFrKLTVEENILAVleIRGLSKKEREEKL-----EELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEmMREKT--VLMVTHRLR-GLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGigVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-561 |
6.10e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 104.05 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQSQQ-ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTrawdpqqGEIllndsPIASLNEAALRQTI 416
Cdd:PLN03130 614 AISIKNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GEL-----PPRSDASVVIRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLFSATLRDNLLLASPGSSDEALSEIlRRVGLEKLLE--DAGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDPERYERAI-DVTALQHDLDllPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 495 LVLLDEPTEGLDATTESQILE-LLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDkCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-560 |
6.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQS---QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAA---- 411
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQ--RVHLFSATLRDNLLLaspGSSDEALS-EILRRVGLEKlLEDAGLNSWLGEGGR-QLSGGELRRLAIAR 487
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAF---GPQNFGIPkEKAEKIAAEK-LEMVGLADEFWEKSPfELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 488 ALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRFQQ-IIVMDNGQIIEQGTHAELL 560
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
356-559 |
7.43e-23 |
|
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: 98.78 E-value: 7.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpiaslneaalrqtISVVPQRVHLFSATLRDNLL 435
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 436 LASpgSSDE-ALSEILRRVGLE----KLLEDAglNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTE 510
Cdd:cd03291 120 FGV--SYDEyRYKSVVKACQLEeditKFPEKD--NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447124921 511 SQILE-LLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:cd03291 196 KEIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-565 |
7.67e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.03 E-value: 7.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN--------- 408
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 409 EAALRQTISVVPQRVHLfsATLRdnlllaspGSSdeaLSEILRRvgLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARA 488
Cdd:COG4152 79 ERGLYPKMKVGEQLVYL--ARLK--------GLS---KAEAKRR--ADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQGR 565
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-562 |
8.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 342 RDVQFTYpEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQ 421
Cdd:PRK13652 7 RDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 RV--HLFSATLRDNLLLA--SPGSSDEAL----SEILRRVGLEKLLEDAglnswlgegGRQLSGGELRRLAIARALLHDA 493
Cdd:PRK13652 86 NPddQIFSPTVEQDIAFGpiNLGLDEETVahrvSSALHMLGLEELRDRV---------PHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRFQQ-IIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
207-562 |
8.14e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 102.36 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 207 LQGQAELTIfgasDRYRTQL--ENTEIQWLEAQRRQS------ELTALSQAIMLLIGALAVILmlWMASGGVGGNAQPGA 278
Cdd:PRK10522 193 LEGRKELTL----NRERAEYvfENEYEPDAQEYRHHIiradtfHLSAVNWSNIMMLGAIGLVF--YMANSLGWADTNVAA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 279 LIALFVF-------CALAAFEALAPVTGAFQHLGQViasavrisDLTDQKPEvtFPDTQTrVADRVSLTLRDVQFTYPEQ 351
Cdd:PRK10522 267 TYSLTLLflrtpllSAVGALPTLLSAQVAFNKLNKL--------ALAPYKAE--FPRPQA-FPDWQTLELRNVTFAYQDN 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFsatlr 431
Cdd:PRK10522 336 GF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF----- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASPGSSDEALSEI-LRRVGLEKLLEDaglnswlgEGGR----QLSGGELRRLAIARALLHDAPLVLLDEPTEGLD 506
Cdd:PRK10522 410 DQLLGPEGKPANPALVEKwLERLKMAHKLEL--------EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 507 ATTESQILELLAEMMRE--KTVLMVTHRLRGLSRFQQIIVMDNGQIIE-QGTHAELLAR 562
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
339-559 |
9.72e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKST---LLQQLTRAWDPQQGEILLNDSPIASLNEAALRQT 415
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 ISVVPQRV--HLFSATLRDNLL--LASPGSSDEALSEILRRVgleklLEDAGLNSWLGEGGRQLSGGELRRLAIARALLH 491
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAfgLENRAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 492 DAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
339-559 |
1.09e-22 |
|
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: 96.83 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTIS 417
Cdd:TIGR03410 1 LEVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFSA-TLRDNLLL---ASPGSSDEALSEILrrvGLEKLLEDAglnswLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTglaALPRRSRKIPDEIY---ELFPVLKEM-----LGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQIIEQGTHAEL 559
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLdfaRELA--DRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
348-531 |
1.15e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 95.57 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 348 YPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIA----SLNEAalRQTISVVPQRV 423
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkGLLER--RQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 424 --HLFSATLRDNLLLaSP---GSSDEalsEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLL 498
Cdd:TIGR01166 78 ddQLFAADVDQDVAF-GPlnlGLSEA---EVERRV--REALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 447124921 499 DEPTEGLDATTESQILELLAEMMRE-KTVLMVTH 531
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEgMTVVISTH 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
354-562 |
1.19e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI--ASLNEAALRQTISVVPQRVHLF-SATL 430
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLL-------ASPGSSDEALSEILRRVGLEkllEDAglNSWLGEggrqLSGGELRRLAIARALLHDAPLVLLDEPTE 503
Cdd:PRK09493 95 LENVMFgplrvrgASKEEAEKQARELLAKVGLA---ERA--HHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 504 GLDATTESQILELLAEMMRE-KTVLMVTHRLrGLSR--FQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEgMTMVIVTHEI-GFAEkvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
339-572 |
1.20e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA-------- 410
Cdd:PRK10619 6 LNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 -----ALRQTISVVPQRVHLFS-ATLRDNLLLA-------SPGSSDEALSEILRRVGLEKLLEdaglnswlGEGGRQLSG 477
Cdd:PRK10619 84 knqlrLLRTRLTMVFQHFNLWShMTVLENVMEApiqvlglSKQEARERAVKYLAKVGIDERAQ--------GKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 478 GELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLrGLSRF--QQIIVMDNGQIIEQG 554
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEM-GFARHvsSHVIFLHQGKIEEEG 234
|
250 260
....*....|....*....|
gi 447124921 555 THAELLA--RQGRYYQFKQG 572
Cdd:PRK10619 235 APEQLFGnpQSPRLQQFLKG 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-566 |
1.54e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.62 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLND-SPiaSLNEAALRQTISVV-PQRVHLF-SATL 430
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVP--FKRRKEFARRIGVVfGQRSQLWwDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLL--ASPGSSDEA-------LSEILrrvGLEKLLEDAGlnswlgeggRQLSGGELRRLAIARALLHDAPLVLLDEP 501
Cdd:COG4586 114 IDSFRLlkAIYRIPDAEykkrldeLVELL---DLGELLDTPV---------RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 502 TEGLDATTESQILELLAEMMREK--TVLMVTHRLRGL----SRfqqIIVMDNGQIIEQGTHAELLARQGRY 566
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIealcDR---VIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
352-531 |
2.00e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIllndspiaslnEAALRQTISVVPQRVHL---FSA 428
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNL---------LLASPGSSDEA-LSEILRRVGLEKLLEDAglnswLGEggrqLSGGELRRLAIARALLHDAPLVLL 498
Cdd:NF040873 73 TVRDLVamgrwarrgLWRRLTRDDRAaVDDALERVGLADLAGRQ-----LGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....
gi 447124921 499 DEPTEGLDATTESQILELLAEMMREK-TVLMVTH 531
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGaTVVVVTH 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
346-554 |
2.09e-22 |
|
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: 95.90 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 346 FTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLnDSPIASLNEAALRQTISVVPQRVHL 425
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDVVKEPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 426 FS-ATLRDNLLLASpGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEG 504
Cdd:cd03266 90 YDrLTARENLEYFA-GLYGLKGDELTARL--EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447124921 505 LDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03266 167 LDVMATRALREFIRQLRALgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
354-531 |
4.54e-22 |
|
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: 95.19 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDS----PIASLNE----AALRQTISVVPQ---- 421
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPreilALRRRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 --RVhlfSAtlRD---NLLLASPGSSDEAL---SEILRRVGLEKLLedaglnsWlgeggrQL-----SGGELRRLAIARA 488
Cdd:COG4778 105 ipRV---SA--LDvvaEPLLERGVDREEARaraRELLARLNLPERL-------W------DLppatfSGGEQQRVNIARG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKT-VLMVTH 531
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFH 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-568 |
5.69e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRD--VQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKS-TLLQQLTRAWDPQ----QGEILLNDSPIASLNEAA 411
Cdd:PRK15134 6 LAIENlsVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQT----ISVVPQR-------VHLFSATLRDNLLLASPGSSDEALSEILR---RVGLEKLledaglNSWLGEGGRQLSG 477
Cdd:PRK15134 86 LRGVrgnkIAMIFQEpmvslnpLHTLEKQLYEVLSLHRGMRREAARGEILNcldRVGIRQA------AKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 478 GELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQN 239
|
250
....*....|....*
gi 447124921 555 THAELLAR-QGRYYQ 568
Cdd:PRK15134 240 RAATLFSApTHPYTQ 254
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-555 |
5.76e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISV 418
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRvhlfsatlRDNLLLASPGSSDEAL---------SEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PRK13648 88 VFQN--------PDNQFVGSIVKYDVAFglenhavpyDEMHRRV--SEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 490 LHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGT 555
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-561 |
6.32e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSQqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE-AALRQTISVV 419
Cdd:PRK13644 4 LENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 420 PQ--RVHLFSATLRDNLLLaspGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:PRK13644 83 FQnpETQFVGRTVEEDLAF---GPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 498 LDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
339-551 |
6.49e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.80 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYP--EQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL---- 412
Cdd:PRK10535 5 LELKDIRRSYPsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 413 RQTISVVPQRVHLFS-ATLRDNLLLAS--PGSSDEAlseilRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEVPAvyAGLERKQ-----RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 490 LHDAPLVLLDEPTEGLDATTESQILELLAEMM-REKTVLMVTHRLRGLSRFQQIIVMDNGQII 551
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-554 |
7.20e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.23 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD--PQ---QGEILLNDSPIAS--LNEAA 411
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSprTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQTISVVPQRVHLFSATLRDNLL--LASPGSS-----DEALSEILRRVGLEKLLEDAGLNSWLGeggrqLSGGELRRLA 484
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVygLRLKGIKdkqvlDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYN 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
328-563 |
7.86e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.82 E-value: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 328 DTQTRVADRVSLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASL 407
Cdd:PRK13536 31 ASIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 408 NEAAlRQTISVVPQRVHL-FSATLRDNLLLASP--GSSDEALSEILrrvglEKLLEDAGLNSWLGEGGRQLSGGELRRLA 484
Cdd:PRK13536 109 ARLA-RARIGVVPQFDNLdLEFTVRENLLVFGRyfGMSTREIEAVI-----PSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMM-REKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALIDE 262
|
.
gi 447124921 563 Q 563
Cdd:PRK13536 263 H 263
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
359-570 |
7.95e-22 |
|
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: 97.10 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAS----LNEAALRQTISVVPQRVHLFS-ATLRDN 433
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 434 LLLaspGSSDEALSEilRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQI 513
Cdd:TIGR02142 96 LRY---GMKRARPSE--RRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 514 LELLAEMMREKT--VLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLARQGRYYQFK 570
Cdd:TIGR02142 171 LPYLERLHAEFGipILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-562 |
7.95e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.57 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 349 PEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAA---LRQTISVVPQ---- 421
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQnpyg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 ----RvHLFSATLRDNLLLASPGSSDE----ALsEILRRVGLEKllEDAglnswlgegGR---QLSGGELRRLAIARALL 490
Cdd:PRK11308 104 slnpR-KKVGQILEEPLLINTSLSAAErrekAL-AMMAKVGLRP--EHY---------DRyphMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 491 HDAPLVLLDEPTEGLDATTESQILELLAEMMREKTV--LMVTHrlrGLSRFQQI----IVMDNGQIIEQGTHAELLAR 562
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISH---DLSVVEHIadevMVMYLGRCVEKGTKEQIFNN 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
319-552 |
8.67e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 319 DQKPEVTFPDTQtRVADRVsLTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIl 398
Cdd:COG0488 298 DKTVEIRFPPPE-RLGKKV-LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 399 lndspiaslnEAALRQTISVVPQRVHLF--SATLRDNLLLASPGSSDEALSEILRRVGL--EKLLEDAGlnswlgeggrQ 474
Cdd:COG0488 373 ----------KLGETVKIGYFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGRFLFsgDDAFKPVG----------V 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 475 LSGGELRRLAIARALLHDAPLVLLDEPTEGLDatTESqiLELLAEMMR--EKTVLMVTH-R--LRGLSrfQQIIVMDNGQ 549
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLD--IET--LEALEEALDdfPGTVLLVSHdRyfLDRVA--TRILEFEDGG 506
|
...
gi 447124921 550 IIE 552
Cdd:COG0488 507 VRE 509
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
356-548 |
8.99e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.07 E-value: 8.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASL--NEAALRQTISVVPQRvhlfsaTLRDN 433
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNYSLLPWL------TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 434 LLLASpGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQI 513
Cdd:TIGR01184 75 IALAV-DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 447124921 514 LELLAEMMREK--TVLMVTHRL-RGLSRFQQIIVMDNG 548
Cdd:TIGR01184 154 QEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-531 |
2.37e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDspiaslneaalRQTISVVP 420
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRVHLFS-ATLRDNLLlaspgSSDEALSEILRRvgLEKLLEDAGLNSWLGE------------GG--------------- 472
Cdd:COG0488 68 QEPPLDDdLTVLDTVL-----DGDAELRALEAE--LEELEAKLAEPDEDLErlaelqeefealGGweaearaeeilsglg 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 473 ----------RQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTesqiLELLAEMMR--EKTVLMVTH 531
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKnyPGTVLVVSH 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
339-555 |
2.96e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.78 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLneAALRQTISV 418
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFS-ATLRDN----LLLASPGSSD--EALSEILRRVGLEKLledaglnswlgeGGR---QLSGGELRRLAIARA 488
Cdd:PRK09452 91 VFQSYALFPhMTVFENvafgLRMQKTPAAEitPRVMEALRMVQLEEF------------AQRkphQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGT 555
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
351-554 |
3.68e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.78 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpIASLNEAALRQTISVV-PQRVHL-FSA 428
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfGQKTQLwWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLaspgssdeaLSEILR------RVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:cd03267 111 PVIDSFYL---------LAAIYDlpparfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 503 EGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
339-549 |
3.99e-21 |
|
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: 89.82 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDspiaslneaalRQTISV 418
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQrvhlfsatlrdnlllaspgssdealseilrrvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03221 68 FEQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447124921 499 DEPTEGLDATTesqiLELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQ 549
Cdd:cd03221 95 DEPTNHLDLES----IEALEEALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-560 |
4.98e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTR---AWDPQ---QGEILLNDSPIASLNEAALRQTISVVPQRVHLFS-A 428
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieIYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPhL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLL--LASPGSSDE-----ALSEILRRVGLEKLLEDAgLNSwlgeGGRQLSGGELRRLAIARALLHDAPLVLLDEP 501
Cdd:PRK14246 106 SIYDNIAypLKSHGIKEKreikkIVEECLRKVGLWKEVYDR-LNS----PASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 502 TEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIV-MDNGQIIEQGTHAELL 560
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAfLYNGELVEWGSSNEIF 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
337-560 |
6.07e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 337 VSLTLRDVQFTYPEQSqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTI 416
Cdd:PRK10575 10 TTFALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRVHLFSA-TLRDNL---------LLASPGSSD-EALSEILRRVGLEKL---LEDAglnswlgeggrqLSGGELRR 482
Cdd:PRK10575 88 AYLPQQLPAAEGmTVRELVaigrypwhgALGRFGAADrEKVEEAISLVGLKPLahrLVDS------------LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 483 LAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
|
.
gi 447124921 560 L 560
Cdd:PRK10575 236 M 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
339-547 |
2.11e-20 |
|
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: 88.36 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIllnDSPiaslneaaLRQTISV 418
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP--------EGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSATLRDNLLLAspgssdealseilrrvgleklledaglnsWlgegGRQLSGGELRRLAIARALLHDAPLVLL 498
Cdd:cd03223 69 LPQRPYLPLGTLREQLIYP-----------------------------W----DDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447124921 499 DEPTEGLDATTESQILELLAEMMreKTVLMVTHRLRGLSRFQQIIVMDN 547
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELG--ITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
355-550 |
2.98e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 88.26 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTISVVP---QRVHLF-SAT 429
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPedrKREGLVlDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 430 LRDNLLLaspgssdealseilrrvgleklledaglnswlgegGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:cd03215 95 VAENIAL-----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447124921 510 ESQILELLAEMMRE-KTVLMVT---HRLRGLSrfQQIIVMDNGQI 550
Cdd:cd03215 140 KAEIYRLIRELADAgKAVLLISselDELLGLC--DRILVMYEGRI 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
370-554 |
3.09e-20 |
|
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: 95.47 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 370 AILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISVVPQRVHLFS-ATLRDNLLLASP---GSSDEA 445
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQlkgRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 446 LSEilrrvgLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKT 525
Cdd:TIGR01257 1039 QLE------MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180
....*....|....*....|....*....
gi 447124921 526 VLMVTHRLRglsrfQQIIVMDNGQIIEQG 554
Cdd:TIGR01257 1113 IIMSTHHMD-----EADLLGDRIAIISQG 1136
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
328-561 |
3.50e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 328 DTQTRVADRVSLTLRDVQFTYPE-QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpias 406
Cdd:PTZ00243 647 HEATPTSERSAKTPKMKTDDFFElEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS---- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 407 lneaalrqtISVVPQRVHLFSATLRDNLLLASPgsSDEA-LSEILRRVGLEKLLED--AGLNSWLGEGGRQLSGGELRRL 483
Cdd:PTZ00243 723 ---------IAYVPQQAWIMNATVRGNILFFDE--EDAArLADAVRVSQLEADLAQlgGGLETEIGEKGVNLSGGQKARV 791
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQIL-ELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGERVVeECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-562 |
4.31e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI--ASLNEAALRQTI 416
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRvhlfsatlRDNLLLASPGSSDEALS---------EILRRVGLEKLLEDAglnswlgEGGRQ-----LSGGELRR 482
Cdd:PRK13638 80 ATVFQD--------PEQQIFYTDIDSDIAFSlrnlgvpeaEITRRVDEALTLVDA-------QHFRHqpiqcLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 483 LAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRFQQ-IIVMDNGQIIEQGTHAELL 560
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEISDaVYVLRQGQILTHGAPGEVF 224
|
..
gi 447124921 561 AR 562
Cdd:PRK13638 225 AC 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-560 |
5.24e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.76 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVV 419
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 420 PQRVHLFSA-TLRDnlLLA---------SPGSSDEAL-SEILRRVGLEKlLEDAGLNswlgeggrQLSGGELRRLAIARA 488
Cdd:COG4604 81 RQENHINSRlTVRE--LVAfgrfpyskgRLTAEDREIiDEAIAYLDLED-LADRYLD--------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDINFASCYaDHIVAMKDGRVVAQGTPEEII 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
338-555 |
5.56e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.19 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQS---QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE----A 410
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQ--RVHLFSATLRDNLLLA------SPGSSDEALSEILRRVGL-EKLLEDAGLnswlgeggrQLSGGELR 481
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGpqnfgvSQEEAEALAREKLALVGIsESLFEKNPF---------ELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGT 555
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-562 |
9.30e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 336 RVSLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWD--PQ---QGEILLNDSPIASLNEA 410
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQ------RVHLFSAT---LRDNLLLASPGSSDEALSEILRRVGLEKLLEDAglnswLGEGGRQLSGGELR 481
Cdd:PRK14247 79 ELRRRVQMVFQipnpipNLSIFENValgLKLNRLVKSKKELQERVRWALEKAQLWDEVKDR-----LDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIV-MDNGQIIEQGTHAELL 560
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAfLYKGQIVEWGPTREVF 233
|
..
gi 447124921 561 AR 562
Cdd:PRK14247 234 TN 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-553 |
1.05e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.30 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 350 EQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE---AALR-QTISVVPQRVHL 425
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 426 F-SATLRDNLLLAS--PGSSDEAlseilRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:PRK10584 100 IpTLNALENVELPAllRGESSRQ-----SRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447124921 503 EGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRFQQIIVMDNGQIIEQ 553
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-563 |
1.16e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.68 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQ---QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPI-ASLNEAA--- 411
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 -LRQTISVVPQ--RVHLFSATLRDNLLLAS---PGSSDEALSEILRRVGLEKLLEDAGLNSWLgeggrQLSGGELRRLAI 485
Cdd:PRK13645 87 rLRKEIGLVFQfpEYQLFQETIEKDIAFGPvnlGENKQEAYKKVPELLKLVQLPEDYVKRSPF-----ELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 486 ARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSPFEIFSN 241
|
.
gi 447124921 563 Q 563
Cdd:PRK13645 242 Q 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-559 |
1.78e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 342 RDVQFTYPEQSQQ----ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDspIASLNEAAL---RQ 414
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLwdiRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 415 TISVVPQRvhlfsatlRDNLLLASPGSSDEAL---------SEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAI 485
Cdd:PRK13633 86 KAGMVFQN--------PDNQIVATIVEEDVAFgpenlgippEEIRERV--DESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 486 ARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
312-531 |
2.05e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 91.79 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 312 VRISDltdqkPEVTFPDTQTRVADRvsltlRDVQFTYPEQSQQaLKGISLQVNAG-----EHIAILGRTGCGKSTLLQQL 386
Cdd:PRK13409 317 MRIRP-----EPIEFEERPPRDESE-----RETLVEYPDLTKK-LGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 387 TRAWDPQQGEILLNdspiaslneaalrQTISVVPQRV-HLFSATLRDNLLLASPGSSDEAL-SEILRRVGLEKLLEdagl 464
Cdd:PRK13409 386 AGVLKPDEGEVDPE-------------LKISYKPQYIkPDYDGTVEDLLRSITDDLGSSYYkSEIIKPLQLERLLD---- 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 465 nSWLGEggrqLSGGELRRLAIARALLHDAPLVLLDEPTEGLDA---TTESQILELLAEmMREKTVLMVTH 531
Cdd:PRK13409 449 -KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRIAE-EREATALVVDH 512
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
356-548 |
2.35e-19 |
|
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: 87.00 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLN----DSPIASLNEAALRQTISVVPQRVHLFSATLR 431
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnkneSEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASPgSSDEALSEILRRVGLEKLLE--DAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDA-- 507
Cdd:cd03290 97 ENITFGSP-FNKQRYKAVTDACSLQPDIDllPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447124921 508 ---TTESQILELLAEMMRekTVLMVTHRLRGLSRFQQIIVMDNG 548
Cdd:cd03290 176 sdhLMQEGILKFLQDDKR--TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
351-531 |
2.68e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIA--SLNEAALRQTISVVPQRVHLFSA 428
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLASPGSSDEALSEILRRVGLEklledaglnswlGEGGR---QLSGGELRRLAIARALLHDAPLVLLDEPTEGL 505
Cdd:PRK11248 92 AFGLQLAGVEKMQRLEIAHQMLKKVGLE------------GAEKRyiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 447124921 506 DATTESQILELLAEMMRE--KTVLMVTH 531
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
339-561 |
3.04e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQ-QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRV--HLFSATLRDNLLLaspGSSDEAL--SEILRRVGlEKLLEDAGLNSWLGEGGRqLSGGELRRLAIARALLHDA 493
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAF---GMENQGIprEEMIKRVD-EALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEmMREK---TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-554 |
3.49e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQ-----GEILLNDSPIAS--LNEAALRQTISVVPQRVH 424
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 425 LFS-ATLRDNL--------LLASPGSSDEALSEILRRVGLEKLLEDAgLNSWLGeggrQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK14267 96 PFPhLTIYDNVaigvklngLVKSKKELDERVEWALKKAALWDEVKDR-LNDYPS----NLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIV-MDNGQIIEQG 554
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAfLYLGKLIEVG 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
351-561 |
4.88e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.15 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTI---------SVVP- 420
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIrmifqdpstSLNPr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRV-HLFSATLRDNLLLaSPGSSDEALSEILRRVGLeklledagLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:PRK15112 104 QRIsQILDFPLRLNTDL-EPEQREKQIIETLRQVGL--------LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 500 EPTEGLDATTESQILELLAEMMREKTV--LMVTHRLRGLSRFQ-QIIVMDNGQIIEQGTHAELLA 561
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
341-560 |
6.41e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVP 420
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QrvhlfSATlrdnlllaSPGssDEALSEILRR-----------------VGLEKLLEDAGLNSWLGEGGRQLSGGELRRL 483
Cdd:PRK10253 88 Q-----NAT--------TPG--DITVQELVARgryphqplftrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
327-559 |
1.00e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 327 PDTQTRVADRVSLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAS 406
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 407 LneAALRQTISVVPQRVHLFS-ATLRDNLLLaspGSSDEALS--EILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRL 483
Cdd:PRK11607 86 V--PPYQRPINMMFQSYALFPhMTVEQNIAF---GLKQDKLPkaEIASRV--NEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQI-LELLAEMMR-EKTVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
353-538 |
1.39e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 353 QQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAA---LRQTISVVPQRVHLF-SA 428
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDN--LLLASPGSSDEalsEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLD 506
Cdd:PRK10908 95 TVYDNvaIPLIIAGASGD---DIRRRV--SAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190
....*....|....*....|....*....|...
gi 447124921 507 ATTESQILELLAEMMREK-TVLMVTHRLRGLSR 538
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGvTVLMATHDIGLISR 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-563 |
1.64e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAS----------------LNEAALRQTISV 418
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpyskkiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQ--RVHLFSATLRDNLLLaspGSSDEALSEILRRVGLEKLLEDAGLN-SWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMF---GPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRG-LSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-531 |
1.70e-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: 84.08 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLL 435
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 436 LASPGSSDEALSEILRRVGLEKLlEDAGLNswlgeggrQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILE 515
Cdd:cd03231 96 FWHADHSDEQVEEALARVGLNGF-EDRPVA--------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*..
gi 447124921 516 LLA-EMMREKTVLMVTH 531
Cdd:cd03231 167 AMAgHCARGGMVVLTTH 183
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
338-554 |
2.88e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.93 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIaslNEAALRQTIS 417
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHL---FSATLRDNLL---------LASPGSSD-EALSEILRRVGLEKLLedaglNSWLGEggrqLSGGELRRLA 484
Cdd:PRK15056 82 YVPQSEEVdwsFPVLVEDVVMmgryghmgwLRRAKKRDrQIVTAALARVDMVEFR-----HRQIGE----LSGGQKKRVF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-563 |
3.33e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTISVVPQRVHLFSA- 428
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLASPGSSDeaLSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDAT 508
Cdd:PRK10895 94 SVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 509 TESQILELLaEMMREK--TVLMVTHRLR-GLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK10895 172 SVIDIKRII-EHLRDSglGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-555 |
3.61e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ-----QGEILLNDSPIAS--LNEA 410
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVglEKLLEDAGLnsW------LGEGGRQLSGGELRRLA 484
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIV--ESALKDADL--WdeikhkIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTESQILELL--AEMMREKTVLMVTHRLRGLSRFQQIIVMDNG------QIIEQGT 555
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGL 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-554 |
6.55e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWdPQQGEILLNDSPIASLNEAAL---RQTISVVPQR-------- 422
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 423 ---VHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKlledAGLNSWLGEggrqLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:PRK15134 379 lnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDP----ETRHRYPAE----FSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 500 EPTEGLDATTESQILELLAEMMREKTV--LMVTHRLRGL-SRFQQIIVMDNGQIIEQG 554
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVrALCHQVIVLRQGEVVEQG 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-547 |
6.85e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.78 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 316 DLTDQKPEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQ-QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQ 394
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 395 GEILLNDS-PIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSD-EALSEILRRVGLE---------------- 456
Cdd:PTZ00265 440 GDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDlEALSNYYNEDGNDsqenknkrnscrakca 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 457 ----------------------KLLEDAGL--------------------NSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:PTZ00265 520 gdlndmsnttdsneliemrknyQTIKDSEVvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMM--REKTVLMVTHRLRGLSRFQQIIVMDN 547
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
339-554 |
9.92e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILL-----NDSPIASLNEAALR 413
Cdd:PRK11701 7 LSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QTI----SVVPQRVhlfsatlRDNLLLA-SPGSSdeaLSEILRRVGLE---KLLEDAGlnSWLGE----------GGRQL 475
Cdd:PRK11701 85 RLLrtewGFVHQHP-------RDGLRMQvSAGGN---IGERLMAVGARhygDIRATAG--DWLERveidaariddLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 476 SGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRL---RGLSrfQQIIVMDNGQI 550
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLavaRLLA--HRLLVMKQGRV 230
|
....
gi 447124921 551 IEQG 554
Cdd:PRK11701 231 VESG 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
342-531 |
1.10e-17 |
|
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: 86.38 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 342 RDVQFTYPEQSQQaLKGISLQVNAG-----EHIAILGRTGCGKSTLLQQLTRAWDPQQGEIllndspiaslnEAALRqtI 416
Cdd:COG1245 338 EETLVEYPDLTKS-YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK--I 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRV-HLFSATLRDNLLLASPGSSDEAL--SEILRRVGLEKLLEdaglnSWLGEggrqLSGGELRRLAIARALLHDA 493
Cdd:COG1245 404 SYKPQYIsPDYDGTVEEFLRSANTDDFGSSYykTEIIKPLGLEKLLD-----KNVKD----LSGGELQRVAIAACLSRDA 474
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447124921 494 PLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTH 531
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENrgKTAMVVDH 514
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
354-563 |
1.49e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAA-LRQTISVVPQRVHLFS-ATLR 431
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASPGSSDEALSEILRRVG------LEKLLEDAGlnswlgeggrQLSGGELRRLAIARALLHDAPLVLLDEPTEGL 505
Cdd:PRK11614 99 ENLAMGGFFAERDQFQERIKWVYelfprlHERRIQRAG----------TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 506 DATTESQILELLAEMMRE-KTVLMVTHRL-RGLSRFQQIIVMDNGQIIEQGTHAELLARQ 563
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQgMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
354-554 |
1.62e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.81 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAlrqtiSVVPqrvhlfSATLRDN 433
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----GFNP------ELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 434 LLL------ASPGSSDEALSEIlrrvgleklLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDA 507
Cdd:cd03220 105 IYLngrllgLSRKEIDEKIDEI---------IEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447124921 508 TTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:cd03220 176 AFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
354-534 |
1.86e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSP--IASLNEaALRQTISVVPQRVHLFSA-TL 430
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPRD-AIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLLASPGSSD---------EALSEILRRVGLE----KLLEDaglnswlgeggrqLSGGELRRLAIARALLHDAPLVL 497
Cdd:COG3845 98 AENIVLGLEPTKGgrldrkaarARIRELSERYGLDvdpdAKVED-------------LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447124921 498 LDEPTEGLdatTESQILELLAEM--MRE--KTVLMVTHRLR 534
Cdd:COG3845 165 LDEPTAVL---TPQEADELFEILrrLAAegKSIIFITHKLR 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-559 |
2.62e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASL-NEAALRQTISVVPQRVHLF-SATLRD 432
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFrEMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 NLLLA---------------SPG---SSDEALSEI---LRRVGLEKLL-EDAGlnswlgeggrQLSGGELRRLAIARALL 490
Cdd:PRK11300 100 NLLVAqhqqlktglfsgllkTPAfrrAESEALDRAatwLERVGLLEHAnRQAG----------NLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 491 HDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLR---GLSrfQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKlvmGIS--DRIYVVNQGTPLANGTPEEI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
354-533 |
2.63e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTISVVPQRVHLF-SATLR 431
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQELHLVpEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLL----ASPGSSDEalSEILRRVG--LEKLLEDAGLNSWLGEggrqLSGGELRRLAIARALLHDAPLVLLDEPTEGL 505
Cdd:PRK11288 98 ENLYLgqlpHKGGIVNR--RLLNYEAReqLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180
....*....|....*....|....*....
gi 447124921 506 DATTESQILELLAEMMRE-KTVLMVTHRL 533
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEgRVILYVSHRM 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
338-562 |
3.15e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.35 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTGCGKSTL------LQQLTrawdpqQGEILLNDSPIASLnEAA 411
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmvagLERIT------SGEIWIGGRVVNEL-EPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 LRQtISVVPQRVHLFS-ATLRDNLL--LASPGSSDEalsEILRRVgLE--KLLEdagLNSWLGEGGRQLSGGELRRLAIA 486
Cdd:PRK11650 75 DRD-IAMVFQNYALYPhMSVRENMAygLKIRGMPKA---EIEERV-AEaaRILE---LEPLLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 487 RALLHDAPLVLLDEPTEGLDATTESQI-LELLAEMMREKTV-LMVTH-RLRGLSRFQQIIVMdNGQIIEQ-GTHAELLAR 562
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKLRVQMrLEIQRLHRRLKTTsLYVTHdQVEAMTLADRVVVM-NGGVAEQiGTPVEVYEK 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
355-542 |
4.18e-17 |
|
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: 79.71 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNE------------AALRQTISVvpqr 422
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephenilylghlPGLKPELSA---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 423 vhlfsatlRDNLLLASPGSSDEALSeilrrvgLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:TIGR01189 91 --------LENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447124921 503 EGLDAttesQILELLAEMMREKT-----VLMVTHRLRGLSRFQQI 542
Cdd:TIGR01189 156 TALDK----AGVALLAGLLRAHLarggiVLLTTHQDLGLVEAREL 196
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
354-561 |
4.80e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKST-------LLQqltrawdPQQGEILLNDSPIASL--NEAAlRQTISVVPQRVH 424
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVK-------PDSGRIFLDGEDITHLpmHKRA-RLGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 425 LF-SATLRDNLLLA---SPGSSDEalseilRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDE 500
Cdd:COG1137 89 IFrKLTVEDNILAVlelRKLSKKE------REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 501 PTEGLDATTESQILELLAEmMREK--TVLMVTHRLR-GLSrfqqII----VMDNGQIIEQGTHAELLA 561
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRH-LKERgiGVLITDHNVReTLG----ICdrayIISEGKVLAEGTPEEILN 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-562 |
8.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.93 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTY-PEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTIS 417
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRV--HLFSATLRDNLL--LASPGSSdeaLSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAfgLENKGIP---HEEMKERV--NEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 494 PLVLLDEPTEGLDATTEsqiLELLA--EMMREK---TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK13650 160 KIIILDEATSMLDPEGR---LELIKtiKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-531 |
8.72e-17 |
|
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: 80.14 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 346 FTYPEQSQqALKGISLQVNAG-----EHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLndspiaslneaaLRQTISVVP 420
Cdd:cd03237 1 YTYPTMKK-TLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------------ELDTVSYKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRVHL-FSATLRDNL--LLASPGSSDEALSEILRRVGLEKLLEDAGLNswlgeggrqLSGGELRRLAIARALLHDAPLVL 497
Cdd:cd03237 68 QYIKAdYEGTVRDLLssITKDFYTHPYFKTEIAKPLQIEQILDREVPE---------LSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 447124921 498 LDEPTEGLDATTE---SQILELLAEmMREKTVLMVTH 531
Cdd:cd03237 139 LDEPSAYLDVEQRlmaSKVIRRFAE-NNEKTAFVVEH 174
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
355-560 |
9.01e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.39 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQT----ISVVPQRVHLFS-AT 429
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 430 LRDNLLLaspGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:PRK10070 123 VLDNTAF---GMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447124921 510 ESQILELLAEMM--REKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK10070 200 RTEMQDELVKLQakHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-573 |
1.48e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.81 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQSqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAAL---RQTIS 417
Cdd:PRK11831 10 MRGVSFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 418 VVPQRVHLFS-ATLRDNLllASPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:PRK11831 88 MLFQSGALFTdMNVFDNV--AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRL-RGLSRFQQIIVMDNGQIIEQGTHAELLARQG-RYYQFKQG 572
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPDpRVRQFLDG 245
|
.
gi 447124921 573 L 573
Cdd:PRK11831 246 I 246
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
356-560 |
1.86e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLT--RAWDPQQGEILLNDSPIASLNeaalrqtisvVPQRVH--LFSA--- 428
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELS----------PDERARagIFLAfqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 -------TLRDNLLLA---------SPGSSDEALSEILRRVGLEKLLedagLNSWLGEGgrqLSGGELRRLAIARALLHD 492
Cdd:COG0396 86 pveipgvSVSNFLRTAlnarrgeelSAREFLKLLKEKMKELGLDEDF----LDRYVNEG---FSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 493 APLVLLDEPTEGLDATTesqiLELLAEM---MR--EKTVLMVTHRLRGLSRFQ--QIIVMDNGQIIEQGThAELL 560
Cdd:COG0396 159 PKLAILDETDSGLDIDA----LRIVAEGvnkLRspDRGILIITHYQRILDYIKpdFVHVLVDGRIVKSGG-KELA 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
352-533 |
2.40e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILlndspiaslNEAALRqtISVVPQRVHLfSATLR 431
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGYVPQKLYL-DTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 ---DNLLLASPGSSDEALSEILRRVGLEKLLEdaglnswlgEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDAT 508
Cdd:PRK09544 84 ltvNRFLRLRPGTKKEDILPALKRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180
....*....|....*....|....*..
gi 447124921 509 TESQILELLAEMMREK--TVLMVTHRL 533
Cdd:PRK09544 155 GQVALYDLIDQLRRELdcAVLMVSHDL 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-562 |
2.92e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQL--TRAWDPQQGEILLN----------DSP------------------ 403
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyvERPskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 404 -----IASLNEAALRQTISVVPQRVHLF--SATLRDNLLLASPGSSDEALSEILRRVgleKLLEDAGLNSWLGEGGRQLS 476
Cdd:TIGR03269 94 vdfwnLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAV---DLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 477 GGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVThrlrgLSRFQQI--------IVMDNG 548
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVL-----TSHWPEViedlsdkaIWLENG 245
|
250
....*....|....
gi 447124921 549 QIIEQGTHAELLAR 562
Cdd:TIGR03269 246 EIKEEGTPDEVVAV 259
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
356-554 |
3.12e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.18 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLT--RAWDPQQGEILLNDSPIASL--NEAAlRQTISVVPQRVhlfsatlr 431
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLppEERA-RLGIFLAFQYP-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 dnllLASPGSSdeaLSEILRRVGleklledaglnswlgEGgrqLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTES 511
Cdd:cd03217 87 ----PEIPGVK---NADFLRYVN---------------EG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447124921 512 QILELLAEMMREKT-VLMVTH--RLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03217 142 LVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
353-554 |
3.45e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.30 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 353 QQALKGISLQVNA---GEHI-AILGRTGCGKSTL---LQQLTRawdPQQGEILLNDSpiaSLNEAAlrQTISVVPQRVH- 424
Cdd:PRK11144 7 KQQLGDLCLTVNLtlpAQGItAIFGRSGAGKTSLinaISGLTR---PQKGRIVLNGR---VLFDAE--KGICLPPEKRRi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 425 --------LFSA-TLRDNLLLASPGSSDEALSEILRRVGLEKLLEdaglnswlgeggR---QLSGGELRRLAIARALLHD 492
Cdd:PRK11144 79 gyvfqdarLFPHyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLD------------RypgSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMRE-KT-VLMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:PRK11144 147 PELLLMDEPLASLDLPRKRELLPYLERLAREiNIpILYVSHSLDEILRLaDRVVVLEQGKVKAFG 211
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
356-564 |
4.19e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.14 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLT--RAWDPQQGEILLNDSPIASLN-EAALRQTISVVPQR-VHLFSATLR 431
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYpIEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLA-------------SPGSSDEALSEILRRVGLEKLLedagLNSWLGEGgrqLSGGELRRLAIARALLHDAPLVLL 498
Cdd:CHL00131 103 DFLRLAynskrkfqglpelDPLEFLEIINEKLKLVGMDPSF----LSRNVNEG---FSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 499 DEPTEGLDATTESQILELLAEMMR-EKTVLMVTHRLRGLSRFQQ--IIVMDNGQIIEQG--THAELLARQG 564
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTsENSIILITHYQRLLDYIKPdyVHVMQNGKIIKTGdaELAKELEKKG 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-561 |
4.51e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 335 DRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDP-----QQGEILLNDSPIASLNE 409
Cdd:PRK14271 16 DAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 410 A-ALRQTISVVPQRVHLFSATLRDNLLLAS------PGSSDEALSEI-LRRVGLEKLLEDAglnswLGEGGRQLSGGELR 481
Cdd:PRK14271 96 VlEFRRRVGMLFQRPNPFPMSIMDNVLAGVrahklvPRKEFRGVAQArLTEVGLWDAVKDR-----LSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQ-QIIVMDNGQIIEQGTHAELL 560
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISdRAALFFDGRLVEEGPTEQLF 250
|
.
gi 447124921 561 A 561
Cdd:PRK14271 251 S 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
356-560 |
8.89e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQ----QLTRAWDPQ----QGEILLNDSPIASLNEAALRQTISVVPQRVH-LF 426
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKalagDLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 427 SATLRDNLLLAS-PGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARAL--LHDAP-------LV 496
Cdd:PRK13547 97 AFSAREIVLLGRyPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWPPHdaaqpprYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREKT--VLMVTHRLRGLSRFQQIIVM-DNGQIIEQGTHAELL 560
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMlADGAIVAHGAPADVL 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
338-559 |
9.35e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 9.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIL-----LNDSPIASLNEAAL 412
Cdd:PRK11000 3 SVTLRNVTKAYGDV--VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 413 RQTISVVPqrvHLfsaTLRDN----LLLASPGSSD-----EALSEILRrvgLEKLLEdaglnswlgeggRQ---LSGGEL 480
Cdd:PRK11000 81 FQSYALYP---HL---SVAENmsfgLKLAGAKKEEinqrvNQVAEVLQ---LAHLLD------------RKpkaLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 481 RRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMR--EKTVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGTHA 557
Cdd:PRK11000 140 QRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPL 219
|
..
gi 447124921 558 EL 559
Cdd:PRK11000 220 EL 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
336-554 |
1.03e-15 |
|
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: 75.76 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 336 RVSLTLRDVQFTYPEQSQQA--LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ---QGEILLNDSPIASLNEA 410
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 411 ALRQTISVVPQRVHLFSATLRDNLllaspgssDEALS----EILRRVgleklledaglnswlgeggrqlSGGELRRLAIA 486
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETL--------DFALRckgnEFVRGI----------------------SGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 487 RALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVT---HRLRGLSRFQQIIVMDNGQIIEQG 554
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSlyqASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
356-542 |
1.04e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIaslneaalrqTISVVPQRVHLF--------S 427
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----------DDPDVAEACHYLghrnamkpA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 428 ATLRDNLLL--ASPGSSDEALSEILRRVGLEKLLEDAGlnswlgeggRQLSGGELRRLAIARALLHDAPLVLLDEPTEGL 505
Cdd:PRK13539 88 LTVAENLEFwaAFLGGEELDIAAALEAVGLAPLAHLPF---------GYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447124921 506 DATTEsqilELLAEMMREK-----TVLMVTHRLRGLSRFQQI 542
Cdd:PRK13539 159 DAAAV----ALFAELIRAHlaqggIVIAATHIPLGLPGAREL 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
358-531 |
1.06e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.00 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 358 GISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVpqrvHL------FSAT-- 429
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG----HQpgikteLTALen 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 430 LRDNLLLASPGSsDEALSEILRRVGLEKLlEDAGLnswlgeggRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:PRK13538 95 LRFYQRLHGPGD-DEALWEALAQVGLAGF-EDVPV--------RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|...
gi 447124921 510 ESQILELLAEMMREK-TVLMVTH 531
Cdd:PRK13538 165 VARLEALLAQHAEQGgMVILTTH 187
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
333-559 |
1.65e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.82 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 333 VAD-RVSLTLRD--VQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKST----------------------LLQQLT 387
Cdd:PRK15079 11 VADlKVHFDIKDgkQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTfaraiiglvkatdgevawlgkdLLGMKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 388 RAWDPQQGEI-LLNDSPIASLNEaalRQTI-SVVPQRVHLFSATLrdnlllaSPGSSDEALSEILRRVGLEKLLedagLN 465
Cdd:PRK15079 91 DEWRAVRSDIqMIFQDPLASLNP---RMTIgEIIAEPLRTYHPKL-------SRQEVKDRVKAMMLKVGLLPNL----IN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 466 SWLGEggrqLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRL---RGLSrfQ 540
Cdd:PRK15079 157 RYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLavvKHIS--D 230
|
250
....*....|....*....
gi 447124921 541 QIIVMDNGQIIEQGTHAEL 559
Cdd:PRK15079 231 RVLVMYLGHAVELGTYDEV 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
327-555 |
2.28e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.46 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 327 PDTQTRVADRVSLTLRD--VQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTL---LQQLTRAWDPQQGEILLND 401
Cdd:PRK09473 1 TVPLAQQQADALLDVKDlrVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 402 SPIASLNEAALR----QTISVVPQ----------RVhlfSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEdagLNSW 467
Cdd:PRK09473 81 REILNLPEKELNklraEQISMIFQdpmtslnpymRV---GEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE---ARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 468 LGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHRL---RGLSrfQQI 542
Cdd:PRK09473 155 MKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLgvvAGIC--DKV 232
|
250
....*....|...
gi 447124921 543 IVMDNGQIIEQGT 555
Cdd:PRK09473 233 LVMYAGRTMEYGN 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
359-532 |
2.50e-15 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 79.02 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWdPQQGEILLNDSPiaslneaalrQTISVVPQRVHLFSATLRDNLL--- 435
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAK----------GKLFYVPQRPYMTLGTLRDQIIypd 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 436 ----LASPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTES 511
Cdd:TIGR00954 540 ssedMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|.
gi 447124921 512 QILELLAEMmrEKTVLMVTHR 532
Cdd:TIGR00954 620 YMYRLCREF--GITLFSVSHR 638
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
309-562 |
3.53e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 309 ASAVRISDLTdqkpeVTFpdtqtRVADRVSLTLRDVQFTYPEQSQQ---ALKGISLQVNAGEHIAILGRTGCGKSTLLQQ 385
Cdd:COG1134 2 SSMIEVENVS-----KSY-----RLYHEPSRSLKELLLRRRRTRREefwALKDVSFEVERGESVGIIGRNGAGKSTLLKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 386 LTRAWDPQQGEILLNDSpIASLNEAALrqtiSVVPQrvhlfsATLRDNLLL------ASPGSSDEALSEIlrrvgleklL 459
Cdd:COG1134 72 IAGILEPTSGRVEVNGR-VSALLELGA----GFHPE------LTGRENIYLngrllgLSRKEIDEKFDEI---------V 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 460 EDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSR 538
Cdd:COG1134 132 EFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....*
gi 447124921 539 F-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG1134 212 LcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
359-560 |
1.08e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.81 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTrAWDPQQGEILLNDSPIA--SLNEAALR-----QTISVVPQrVHLFSATLR 431
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMA-GLLPGSGSIQFAGQPLEawSAAELARHraylsQQQTPPFA-MPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASPGSSDEALSEILRRVGLEKLLedaglnswlgegGR---QLSGGELRRLAIARALLHDAP-------LVLLDEP 501
Cdd:PRK03695 93 HQPDKTRTEAVASALNEVAEALGLDDKL------------GRsvnQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 502 TEGLDATTESQILELLAEMMRE-KTVLMVTHRL-RGLSRFQQIIVMDNGQIIEQGTHAELL 560
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
354-562 |
1.71e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.94 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ----------QGEILLNDSPiaSLNEAALRQTISVV---P 420
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKLSP--RERRKIIGREIAMIfqeP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 421 QRVHLFSATLRDNLLLASPGSS------------DEALSEILRRVGLEKllEDAGLNSWlgegGRQLSGGELRRLAIARA 488
Cdd:COG4170 99 SSCLDPSAKIGDQLIEAIPSWTfkgkwwqrfkwrKKRAIELLHRVGIKD--HKDIMNSY----PHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 489 LLHDAPLVLLDEPTEGLDATTESQILELLAEM--MREKTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQWaDTITVLYCGQTVESGPTEQILKS 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-564 |
2.15e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlneAALRQT----I 416
Cdd:NF033858 4 LEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAvcprI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 SVVPQRV--HLFsATL--RDNL-----LLAspgssdeaLSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIAR 487
Cdd:NF033858 79 AYMPQGLgkNLY-PTLsvFENLdffgrLFG--------QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 488 ALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK---TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQG 564
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
322-554 |
2.27e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 322 PEVTFPDTQ--TRVADRVSLTLRDVQFTYPEQSQ---------QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAW 390
Cdd:PRK10261 295 PAKQEPPIEqdTVVDGEPILQVRNLVTRFPLRSGllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 391 DPQQGEILLNDSPIASLNEAAL--------------------RQTIS---VVPQRVHlfsatlrdNLLLASpgSSDEALS 447
Cdd:PRK10261 375 ESQGGEIIFNGQRIDTLSPGKLqalrrdiqfifqdpyasldpRQTVGdsiMEPLRVH--------GLLPGK--AAAARVA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 448 EILRRVGLekLLEDAglnsWlgEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTV- 526
Cdd:PRK10261 445 WLLERVGL--LPEHA----W--RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIa 516
|
250 260 270
....*....|....*....|....*....|
gi 447124921 527 -LMVTHRLRGLSRF-QQIIVMDNGQIIEQG 554
Cdd:PRK10261 517 yLFISHDMAVVERIsHRVAVMYLGQIVEIG 546
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-551 |
2.74e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 323 EVTFP-DTQTRVADRVSLTLRDVQFTyPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLND 401
Cdd:COG3845 241 EVLLRvEKAPAEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 402 SPIASLNEAALRQT-ISVVP---QRVHLF-SATLRDNLLLASPGSSDEALSEILRRVGL----EKLLED-----AGLNSW 467
Cdd:COG3845 320 EDITGLSPRERRRLgVAYIPedrLGRGLVpDMSVAENLILGRYRRPPFSRGGFLDRKAIrafaEELIEEfdvrtPGPDTP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 468 LgeggRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRL---RGLS-RfqqI 542
Cdd:COG3845 400 A----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLdeiLALSdR---I 472
|
....*....
gi 447124921 543 IVMDNGQII 551
Cdd:COG3845 473 AVMYEGRIV 481
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
22-314 |
4.10e-14 |
|
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: 73.19 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 22 IVLAIVTLLASIGLlTLSGWFLSASAV--AGVAGLYSFNYMLPAAGVR-GAAITRTAGRYFERLVSHDATFRVLQHLRIY 98
Cdd:cd18544 1 FILALLLLLLATAL-ELLGPLLIKRAIddYIVPGQGDLQGLLLLALLYlGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 99 TFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftlggimLLTLFLMP 178
Cdd:cd18544 80 LFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLA-------LISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 179 PLFYragkstgqnLTHL-----RGQYRQ------QLTAWLQ----GQAELTIFGASDRYRTQLENTEIQWLEAQRRQSEL 243
Cdd:cd18544 153 LLLL---------ATYLfrkksRKAYREvreklsRLNAFLQesisGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 244 TALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd18544 224 FALFRPLVELLSSLALALVLWYGGGQVlSGAVTLGVLYA-FIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
356-559 |
4.68e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQT-ISVVPQRVHLF-SATLRDN 433
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFpNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 434 LLLASPGSSD--EALSEILRRVGLE-KLLEDAGLnswLGEGGRQLsggelrrLAIARALLHDAPLVLLDEPTEGLD-ATT 509
Cdd:PRK15439 107 ILFGLPKRQAsmQKMKQLLAALGCQlDLDSSAGS---LEVADRQI-------VEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447124921 510 E---SQILELLAEMMrekTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK15439 177 ErlfSRIRELLAQGV---GIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-314 |
5.04e-14 |
|
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: 72.97 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYsfnyMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRI 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLL----LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 98 YTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftlggimLLTLFLM 177
Cdd:cd07346 77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLT-------LVALLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 178 PPLFYRAGKSTGQnlthLRGQYR--QQLTAWLQGQAELTI--------FGA----SDRYRTQLEnteiQWLEAQRRQSEL 243
Cdd:cd07346 150 PLYVLILRYFRRR----IRKASRevRESLAELSAFLQESLsgirvvkaFAAeereIERFREANR----DLRDANLRAARL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 244 TALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd07346 222 SALFSPLIGLLTALGTALVLLYGGYLVlQGSLTIGELVA-FLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-561 |
5.52e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ--QGEILLNDSPIAslnEAALRQTISVVPQRVHLFSA 428
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT---KQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLASPGSSDEALSEILRRVGLEKLLEDAGL----NSWLGEGG-RQLSGGELRRLAIARALLHDAPLVLLDEPTE 503
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLtkceNTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 504 GLDATTESQILELLAEMMRE-KTVLMVTHR--LRGLSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKgKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
305-559 |
8.06e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 305 GQVIASAvRISDLTDQ---------KPEVTFPDtQTRVADRVSLTLRDVQftypeqSQQALKGISLQVNAGEHIAILGRT 375
Cdd:COG1129 216 GRLVGTG-PVAELTEDelvrlmvgrELEDLFPK-RAAAPGEVVLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 376 GCGKSTLLQQLTRAWDPQQGEILLNDSPIASLN-EAALRQTISVVP---QRVHLF-SATLRDNLLLASpgssdeaLSEIL 450
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPedrKGEGLVlDLSIRENITLAS-------LDRLS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 451 RRVGLEKLLEDAGLNSWLGEGG----------RQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEM 520
Cdd:COG1129 361 RGGLLDRRRERALAEEYIKRLRiktpspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL 440
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447124921 521 MRE-KTVLMVT---HRLRGLS-RfqqIIVMDNGQIIEQGTHAEL 559
Cdd:COG1129 441 AAEgKAVIVISselPELLGLSdR---ILVMREGRIVGELDREEA 481
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-314 |
1.12e-13 |
|
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: 71.68 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYsfnYMLPAAGVrGAAITRTAGRYFERLVSHDATFRVLQHLRI 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEAL---LLVPLAII-GLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 98 YTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftlggimLLTLFLM 177
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLT-------LIALVVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 178 PPLFY---RAGKStgqnlthLRGQYRQQLTAW----------LQGQAELTIFGA----SDRYRTQLENTEIQWLEAQRRQ 240
Cdd:cd18552 150 PLAALpirRIGKR-------LRKISRRSQESMgdltsvlqetLSGIRVVKAFGAedyeIKRFRKANERLRRLSMKIARAR 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 241 seltALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd18552 223 ----ALSSPLMELLGAIAIALVLWYGGYQViSGELTPGEFIS-FITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
354-555 |
3.03e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.27 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNeAALRQtISVVPQRVHLFS-ATLRD 432
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDRK-VGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 NL---LLASPGSSDEALSEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:PRK10851 94 NIafgLTVLPRRERPNAAAIKAKV--TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447124921 510 ESQILELLAEMMREK--TVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGT 555
Cdd:PRK10851 172 RKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-533 |
3.13e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 366 GEHIAILGRTGCGKSTLLQQLTrawdpqqGEILLN----DSP------------------IASLNEAALRqtISVVPQRV 423
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILS-------GELIPNlgdyEEEpswdevlkrfrgtelqnyFKKLYNGEIK--VVHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 424 HL----FSATLRDnlLLASpgsSDE--ALSEILRRVGLEKLLE-DAglnswlgeggRQLSGGELRRLAIARALLHDAPLV 496
Cdd:PRK13409 170 DLipkvFKGKVRE--LLKK---VDErgKLDEVVERLGLENILDrDI----------SELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*..
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRL 533
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
359-559 |
3.86e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIAslnEAALRQ-TISVVPQRVHLFS-ATLRDNLL- 435
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQrDICMVFQSYALFPhMSLGENVGy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 436 -LASPGSSDEalsEILRRV--GLEkLLEDAGLnswlgeGGR---QLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATt 509
Cdd:PRK11432 102 gLKMLGVPKE---ERKQRVkeALE-LVDLAGF------EDRyvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447124921 510 esqilelLAEMMREK----------TVLMVTH-RLRGLSRFQQIIVMDNGQIIEQGTHAEL 559
Cdd:PRK11432 171 -------LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
360-562 |
5.20e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 360 SLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRvhlfsatlrDNLLLASP 439
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQR---------NNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 440 GSSDEAL--SEILR-----RVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQ 512
Cdd:PRK10938 94 GEDDTGRttAEIIQdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 513 ILELLAEMMREKTVLMVThrlrgLSRF-------QQIIVMDNGQIIEQGTHAELLAR 562
Cdd:PRK10938 174 LAELLASLHQSGITLVLV-----LNRFdeipdfvQFAGVLADCTLAETGEREEILQQ 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
356-564 |
5.60e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 68.83 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLtrAWDPQ----QGEILLNDSPIASL--NEAAlRQTISVVPQR-VHLFSA 428
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPSyevtSGTILFKGQDLLELepDERA-RAGLFLAFQYpEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRDNLLLASPGSSDEALSEILRRVGLEKLLED---------AGLNSWLGEGgrqLSGGELRRLAIARALLHDAPLVLLD 499
Cdd:TIGR01978 93 SNLEFLRSALNARRSARGEEPLDLLDFEKLLKEklalldmdeEFLNRSVNEG---FSGGEKKRNEILQMALLEPKLAILD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 500 EPTEGLDATTESQILELLAEMMREKT-VLMVTHRLRGLSRFQ--QIIVMDNGQIIEQG--THAELLARQG 564
Cdd:TIGR01978 170 EIDSGLDIDALKIVAEGINRLREPDRsFLIITHYQRLLNYIKpdYVHVLLDGRIVKSGdvELAKELEAKG 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
354-548 |
1.69e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA-ALRQTISVVPQRVHLFSA-TLR 431
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASPGSSD-------------EALSEILRRVGLEKLLEDAGLNswlgeggrqLSGGELRRLAIARALLHDAPLVLL 498
Cdd:PRK09700 99 ENLYIGRHLTKKvcgvniidwremrVRAAMMLLRVGLKVDLDEKVAN---------LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 499 DEPTEGLdatTESQILELLAEMMR----EKTVLMVTHRLRGLSRF-QQIIVMDNG 548
Cdd:PRK09700 170 DEPTSSL---TNKEVDYLFLIMNQlrkeGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-531 |
2.32e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 341 LRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQG--------EILLNDSPIASL----- 407
Cdd:PRK11147 322 MENVNYQIDGK--QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklEVAYFDQHRAELdpekt 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 408 ---NEAALRQTISVVPQRVHLFSaTLRDnlLLASPgssDEALSEIlrrvgleklledaglnswlgeggRQLSGGELRRLA 484
Cdd:PRK11147 400 vmdNLAEGKQEVMVNGRPRHVLG-YLQD--FLFHP---KRAMTPV-----------------------KALSGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447124921 485 IARALLHDAPLVLLDEPTEGLDATTesqiLELLAEMMRE--KTVLMVTH 531
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSyqGTVLLVSH 495
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
351-555 |
4.60e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 351 QSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQL----TRAWDPQQ-----GEILLNDSPIASLNEAALRQTISVVPQ 421
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsgliTGDKSAGShiellGRTVQREGRLARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 RVHLFSATLRDNLLLASPGSSD------EALSEILRRVGLEKLLEdAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK09984 95 FNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447124921 496 VLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGT 555
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYcERIVALRQGHVFYDGS 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
474-559 |
5.54e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 474 QLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQI 550
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAaHKIIVMYAGQV 232
|
....*....
gi 447124921 551 IEQGTHAEL 559
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
366-533 |
7.44e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 366 GEHIAILGRTGCGKSTLLQQLTrawdpqqGEILLN----DSPiASLNE--------------AALRQ-TISVV--PQRVH 424
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILS-------GELKPNlgdyDEE-PSWDEvlkrfrgtelqdyfKKLANgEIKVAhkPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 425 L----FSATLRDnlLLASpgsSDE--ALSEILRRVGLEKLLE-DAglnswlgeggRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:COG1245 171 LipkvFKGTVRE--LLEK---VDErgKLDELAEKLGLENILDrDI----------SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*....
gi 447124921 498 LDEPTEGLDAT---TESQILELLAEMmrEKTVLMVTHRL 533
Cdd:COG1245 236 FDEPSSYLDIYqrlNVARLIRELAEE--GKYVLVVEHDL 272
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
339-533 |
3.58e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQrvhlFSATlrDNLLlasPGSSDEALSEILRRVGLEKL-------LEDAGLNSWLGEGGRQLSGGELRRLAIARALLH 491
Cdd:TIGR01257 2017 CPQ----FDAI--DDLL---TGREHLYLYARLRGVPAEEIekvanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447124921 492 DAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRL 533
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
344-561 |
3.99e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 344 VQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQL----TRAWDPQQGEILLNDSPIASLNEAALRQTI--- 416
Cdd:PRK15093 11 IEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVghn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 -SVV---PQRVHLFSATLRDNLLLASPGSSDEA------------LSEILRRVGLeKLLEDAglnswLGEGGRQLSGGEL 480
Cdd:PRK15093 91 vSMIfqePQSCLDPSERVGRQLMQNIPGWTYKGrwwqrfgwrkrrAIELLHRVGI-KDHKDA-----MRSFPYELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 481 RRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHA 557
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWaDKINVLYCGQTVETAPSK 244
|
....
gi 447124921 558 ELLA 561
Cdd:PRK15093 245 ELVT 248
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
338-548 |
4.00e-11 |
|
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: 62.26 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 338 SLTLRDVQFTY--PEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ--QGEILLNDSPIaslnEAALR 413
Cdd:cd03232 3 VLTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QTISVVPQR-VHLFSATLRDNLLlaspgssdeaLSEILRRVGLEklledaglnswlgeggrqlsggELRRLAIARALLHD 492
Cdd:cd03232 79 RSTGYVEQQdVHSPNLTVREALR----------FSALLRGLSVE----------------------QRKRLTIGVELAAK 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHR--LRGLSRFQQIIVMDNG 548
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-531 |
4.15e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQqltrawdpqqgeILLN-DSPIasLNEAALRQTISV 418
Cdd:TIGR03719 6 TMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLR------------IMAGvDKDF--NGEARPQPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 --VPQRVHL-FSATLRDNLLlaspgssdEALSEILR------RVGLEKLLEDAGLNSWLGEGGR---------------- 473
Cdd:TIGR03719 71 gyLPQEPQLdPTKTVRENVE--------EGVAEIKDaldrfnEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsq 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447124921 474 ------------------QLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMmrEKTVLMVTH 531
Cdd:TIGR03719 143 leiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
343-555 |
6.00e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 343 DVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEI-----LLN--DSPIASLNEAALRQT 415
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRrrSRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 416 -------ISVVPQR-------VHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEDAGLnswLGEGGRQLSGGELR 481
Cdd:PRK10261 99 rhvrgadMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI---LSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 482 RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKT--VLMVTHRLRGLSRF-QQIIVMDNGQIIEQGT 555
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQGEAVETGS 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
320-564 |
6.95e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 320 QKPEVTFpdTQTRVADRVSLTLRDVQFTYPEQsqQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIll 399
Cdd:PRK15064 303 QNPFIRF--EQDKKLHRNALEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 400 ndspiaSLNEAAlrqTISVVPQ-RVHLFSATLrdNLL-----LASPGSSDEALSEILRRvglekLL---EDAglnswlGE 470
Cdd:PRK15064 377 ------KWSENA---NIGYYAQdHAYDFENDL--TLFdwmsqWRQEGDDEQAVRGTLGR-----LLfsqDDI------KK 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 471 GGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDatTESqILEL-LAEMMREKTVLMVTHRLRGLSRF-QQIIVMDNG 548
Cdd:PRK15064 435 SVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD--MES-IESLnMALEKYEGTLIFVSHDREFVSSLaTRIIEITPD 511
|
250
....*....|....*..
gi 447124921 549 QIIE-QGTHAELLARQG 564
Cdd:PRK15064 512 GVVDfSGTYEEYLRSQG 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-538 |
7.81e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYpeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:PRK13540 2 LDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLF-SATLRDNLLLASPGSSDE-ALSEILRRVGLEKLLE-DAGLnswlgeggrqLSGGELRRLAIARALLHDAPL 495
Cdd:PRK13540 79 VGHRSGINpYLTLRENCLYDIHFSPGAvGITELCRLFSLEHLIDyPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447124921 496 VLLDEPTEGLDA-TTESQILELLAEMMREKTVLMVTHRLRGLSR 538
Cdd:PRK13540 149 WLLDEPLVALDElSLLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
408-564 |
9.46e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.60 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 408 NEAALRQTIS----VVPQRVHLFSAtlRDNLLLASPGSSdeaLSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRL 483
Cdd:NF000106 79 NRRALRRTIG*hrpVR*GRRESFSG--RENLYMIGR*LD---LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRLRGLSRF-QQIIVMDNGQIIEQGTHAELLA 561
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKT 233
|
...
gi 447124921 562 RQG 564
Cdd:NF000106 234 KVG 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-561 |
1.47e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGE--ILLNDSPI-----ASLNEAALRQTISVVPQRVHLF 426
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVdmtkpGPDGRGRAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 427 S-ATLRDNLLLASpgsSDEALSEILRRVGLEKL----LEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEP 501
Cdd:TIGR03269 378 PhRTVLDNLTEAI---GLELPDELARMKAVITLkmvgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 502 TEGLDATTESQ----ILELLAEMmrEKTVLMVTHRLRG-LSRFQQIIVMDNGQIIEQGTHAELLA 561
Cdd:TIGR03269 455 TGTMDPITKVDvthsILKAREEM--EQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
315-533 |
2.08e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 315 SDLTDQKPevTFPDTQTRVadrvslTLRDVQFTYPEQSqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTrawdpqq 394
Cdd:PRK10938 245 PDEPSARH--ALPANEPRI------VLNNGVVSYNDRP--ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 395 geillNDSPIASLNEAAL--------------RQTISVVPQRVHL---FSATLRDNLLlasPGSSD-----EALSEILRR 452
Cdd:PRK10938 308 -----GDHPQGYSNDLTLfgrrrgsgetiwdiKKHIGYVSSSLHLdyrVSTSVRNVIL---SGFFDsigiyQAVSDRQQK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 453 VGLEkLLEDAGLNSWLGEGG-RQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLM-- 528
Cdd:PRK10938 380 LAQQ-WLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfv 458
|
250
....*....|....*
gi 447124921 529 ----------VTHRL 533
Cdd:PRK10938 459 shhaedapacITHRL 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
332-532 |
3.58e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 332 RVADRVSLTLRDVQFTypeqsqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRA--WDPQQGEILLNDSPIASlne 409
Cdd:COG2401 29 IVLEAFGVELRVVERY-------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQFGR--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 410 aalrqtisvvpqrvhlfSATLRDNLllASPGSSDEALsEILRRVGLEklleDAGLnsWLGEGgRQLSGGELRRLAIARAL 489
Cdd:COG2401 99 -----------------EASLIDAI--GRKGDFKDAV-ELLNAVGLS----DAVL--WLRRF-KELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447124921 490 LHDAPLVLLDEPTEGLDATTESQILELLAEMMRE--KTVLMVTHR 532
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRagITLVVATHH 196
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-314 |
4.46e-10 |
|
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: 61.01 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFLSASAVAG--VAGLYSFnymlpAAGVRGAAITRTAGRYFERLVSHDATFRVLQHL 95
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSksLGLLLGL-----ALLLLGAYLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 96 RIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftlggimLLTLF 175
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLA-------LLTLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 176 LMPPLFYRAGKSTGqnltHLRGQYRQQ------LTAWLQ----GQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTA 245
Cdd:cd18778 149 PIPFLALGAWLYSK----KVRPRYRKVrealgeLNALLQdnlsGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 246 LSQAIMLLIGALAVILMLWMasGG---VGGNAQPGALIALFVFCALaAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd18778 225 IFHPLMEFLTSLGTVLVLGF--GGrlvLAGELTIGDLVAFLLYLGL-FYEPITSLHGLNEMLQRALAGAERV 293
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
354-556 |
5.88e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTR-----AWDpqqGEILLNDSPI-ASLNEAALRQTISVVPQRVHLF- 426
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgTWD---GEIYWSGSPLkASNIRDTERAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 427 SATLRDNLLLAS----PGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGgrQLSGGELRRLAIARALLHDAPLVLLDEPT 502
Cdd:TIGR02633 92 ELSVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG--DYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 503 EGLDATTESQILELLAEMMREKTV-LMVTHRLRGLSrfqqiIVMDNGQIIEQGTH 556
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVK-----AVCDTICVIRDGQH 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
315-517 |
1.04e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 315 SDLTDQKPEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQ--QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDP 392
Cdd:TIGR00956 736 TDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVKIKKEkrVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTT 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 393 ---QQGEILLNDSPiasLNEAALRQTISVVPQRVHLFSATLRDNL----LLASPGS-----SDEALSEILRRVGLEKLLE 460
Cdd:TIGR00956 816 gviTGGDRLVNGRP---LDSSFQRSIGYVQQQDLHLPTSTVRESLrfsaYLRQPKSvskseKMEYVEEVIKLLEMESYAD 892
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 461 daglnSWLGEGGRQLSGGELRRLAIARALL-HDAPLVLLDEPTEGLDATTESQILELL 517
Cdd:TIGR00956 893 -----AVVGVPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQTAWSICKLM 945
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
354-559 |
1.14e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLN------DSPIASlNEAAlrqtISVVPQRVHLFS 427
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLgkevtfNGPKSS-QEAG----IGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 428 A-TLRDNLLLAspgssdealSEILRRVGL----------EKLLedAGLNswLGEGGRQLSG----GELRRLAIARALLHD 492
Cdd:PRK10762 93 QlTIAENIFLG---------REFVNRFGRidwkkmyaeaDKLL--ARLN--LRFSSDKLVGelsiGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 493 APLVLLDEPTEGL-DATTESQ---ILELLAEmmrEKTVLMVTHRLRGLsrFQ---QIIVMDNGQIIEQGTHAEL 559
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETESLfrvIRELKSQ---GRGIVYISHRLKEI--FEicdDVTVFRDGQFIAEREVADL 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
366-533 |
1.44e-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: 58.92 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 366 GEHIAILGRTGCGKSTLLQQLTRAWDPQQG---------EILLN--DSPIASLNEAALRQTISVV--PQRVHLFSATLRd 432
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDEfrGSELQNYFTKLLEGDVKVIvkPQYVDLIPKAVK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 433 nlllaspGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQ 512
Cdd:cd03236 105 -------GKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|..
gi 447124921 513 ILELLAEMMRE-KTVLMVTHRL 533
Cdd:cd03236 178 AARLIRELAEDdNYVLVVEHDL 199
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
23-281 |
1.45e-09 |
|
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: 59.37 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 23 VLAIVTLLASIGLLTLSGWFLSaSAVAGVAGLYSFNYMLP-AAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFS 101
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIR-RIIDSVIGGGLRELLWLlALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 102 KLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftlggimLLTLFLMPPLF 181
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLT-------LISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 182 YRAGKsTGQNLTHLRGQYRQQLtawlqgqAELTI--------------FGAsdryrtqlENTEIQ--------WLEAQRR 239
Cdd:cd18542 154 LFSYV-FFKKVRPAFEEIREQE-------GELNTvlqenltgvrvvkaFAR--------EDYEIEkfdkeneeYRDLNIK 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447124921 240 QSELTALSQAIMLLIGALAVILMLWMasGG---VGGNAQPGALIA 281
Cdd:cd18542 218 LAKLLAKYWPLMDFLSGLQIVLVLWV--GGylvINGEITLGELVA 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
359-550 |
2.18e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ-QGEILLNDSPIASLNEA-ALRQTISVVPQRVHlfsatlRDNLLL 436
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAGIAMVPEDRK------RHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 437 ASPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGR-------------QLSGGELRRLAIARALLHDAPLVLLDEPTE 503
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRlkvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447124921 504 GLDATTESQILELLAEMMREK-TVLMVTHRLR---GLSrfQQIIVMDNGQI 550
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGvAIIVVSSELAevlGLS--DRVLVIGEGKL 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
339-564 |
2.59e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTypeqsqqALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASlNEAALRQTISV 418
Cdd:NF033858 272 LTMRFGDFT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 419 VPQRVHLFSA-TLRDNLLL------ASPGSSDEALSEILRRVGLEKLLEDagLNSWLGEGGRQlsggelrRLAIARALLH 491
Cdd:NF033858 344 MSQAFSLYGElTVRQNLELharlfhLPAAEIAARVAEMLERFDLADVADA--LPDSLPLGIRQ-------RLSLAVAVIH 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 492 DAPLVLLDEPTEGLDATTESQILELLAEMMREK--TVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQG 564
Cdd:NF033858 415 KPELLILDEPTSGVDPVARDMFWRLLIELSREDgvTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
355-517 |
2.94e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 355 ALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTR-----AWDpqqGEILLNDSPIASLN----EAA----LRQTISVVPQ 421
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgTYE---GEIIFEGEELQASNirdtERAgiaiIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 422 rvhlfsATLRDNLLLASP----GSSDEAlsEILRRVglEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVL 497
Cdd:PRK13549 97 ------LSVLENIFLGNEitpgGIMDYD--AMYLRA--QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180
....*....|....*....|
gi 447124921 498 LDEPTEGLdatTESQILELL 517
Cdd:PRK13549 167 LDEPTASL---TESETAVLL 183
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
70-314 |
5.01e-09 |
|
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: 57.81 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 70 AITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVD-TLDHLYLRVISPLVGAFVVI 148
Cdd:cd18554 56 LILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEqTKDFITTGLMNIWLDMITII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 149 MVVTIGLsFLDFTLAFTlgGIMLLTL-FLMPPLFYRAGKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLE 227
Cdd:cd18554 136 IAICIML-VLNPKLTFV--SLVIFPFyILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 228 NTEIQWLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIALFVFCALaAFEALAPVTGAFQHLGQ 306
Cdd:cd18554 213 KRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLViEGNLTVGTLVAFVGYMER-MYSPLRRLVNSFTTLTQ 291
|
....*...
gi 447124921 307 VIASAVRI 314
Cdd:cd18554 292 SFASMDRV 299
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
354-554 |
6.03e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEIllnDSPIA----SLNEAALRQTISVV---PQRVHLF 426
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGV---EGVITydgiTPEEIKKHYRGDVVynaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 427 SATLRDNLLLA----SPGSSDEALSEILRRVGLEKL-LEDAGL----NSWLG-EGGRQLSGGELRRLAIARALLHDAPLV 496
Cdd:TIGR00956 152 HLTVGETLDFAarckTPQNRPDGVSREEYAKHIADVyMATYGLshtrNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMMRE--KTVLMV-------THRLrglsrFQQIIVMDNGQIIEQG 554
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANIldTTPLVAiyqcsqdAYEL-----FDKVIVLYEGYQIYFG 293
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-531 |
9.26e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 340 TLRDVQFTYPEQsQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLndSPIAslneaalrqTISVV 419
Cdd:PRK11819 8 TMNRVSKVVPPK-KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--APGI---------KVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 420 PQRVHL-FSATLRDNLllaspgssDEALSEI---LRR---VGLEKLLEDAGLNSWLGEGGR------------------- 473
Cdd:PRK11819 76 PQEPQLdPEKTVRENV--------EEGVAEVkaaLDRfneIYAAYAEPDADFDALAAEQGElqeiidaadawdldsqlei 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 474 ---------------QLSGGELRRLAIARALLHDAPLVLLDEPTEGLDAttES-QILE-LLAEMmrEKTVLMVTH 531
Cdd:PRK11819 148 amdalrcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--ESvAWLEqFLHDY--PGTVVAVTH 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
352-554 |
1.54e-08 |
|
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: 54.25 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 352 SQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAwdpqQGEILLNDSPiaslnEAALRQTISVVPQrvhlfsatlr 431
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFL-----PKFSRNKLIFIDQ---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 dnlllaspgssdeaLSEILRrVGLEKLLEDAGLNSwlgeggrqLSGGELRRLAIARALLHDAP--LVLLDEPTEGLDATT 509
Cdd:cd03238 68 --------------LQFLID-VGLGYLTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447124921 510 ESQILELLAEMMREK-TVLMVTHRLRGLSRFQQIIVM------DNGQIIEQG 554
Cdd:cd03238 125 INQLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
366-548 |
3.06e-08 |
|
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: 53.15 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 366 GEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVvpqrvhlfsatlrdnlllaspgssdea 445
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 446 lseilrrvgleklledaglnswlGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREK- 524
Cdd:smart00382 55 -----------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLl 111
|
170 180 190
....*....|....*....|....*....|....*.
gi 447124921 525 ------TVLMVTHRLRGL------SRFQQIIVMDNG 548
Cdd:smart00382 112 kseknlTVILTTNDEKDLgpallrRRFDRRIVLLLI 147
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-285 |
3.34e-08 |
|
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: 54.96 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFeRLVSHdATFRVLQHLRI 97
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQS-YLLNH-TGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 98 YTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAFtlggIMLLTLFLM 177
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTL----VLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 178 PPLFYRAGKstgqnltHLRGQYRQQLTAW----------LQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALS 247
Cdd:pfam00664 155 ILVSAVFAK-------ILRKLSRKEQKAVakassvaeesLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 447124921 248 QAIMLLIGALAVILMLWMASGGVG-GNAQPGALIALFVF 285
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVIsGELSVGDLVAFLSL 266
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
357-552 |
3.96e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 357 KGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLN------DSPIASLNEA-----------------ALR 413
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkdispRSPLDAVKKGmayitesrrdngffpnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 414 QTISVVPQrvhlfsatLRDNLLLASPGSSDEALSEILRRVGLEKL-LEDAGLNSWLGEggrqLSGGELRRLAIARALLHD 492
Cdd:PRK09700 360 QNMAISRS--------LKDGGYKGAMGLFHEVDEQRTAENQRELLaLKCHSVNQNITE----LSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 493 APLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRL-RGLSRFQQIIVMDNGQIIE 552
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
347-530 |
4.20e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 347 TYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLF 426
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 427 SATLRDNLLLASPGSSDEAL-SEILRRVGLeklledAGLNSWLGeggRQLSGGELRRLAIARALLHDAPLVLLDEPTEGL 505
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQMpGSALAIVGL------AGYEDTLV---RQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180
....*....|....*....|....*
gi 447124921 506 DATTESQILELLAEMMREKTVLMVT 530
Cdd:PRK13543 169 DLEGITLVNRMISAHLRGGGAALVT 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
339-552 |
6.64e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 339 LTLRDVQFTYPeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTrAWDPQ---QGEILLNDSPIA----SLNEAA 411
Cdd:NF040905 2 LEMRGITKTFP--GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-GVYPHgsyEGEILFDGEVCRfkdiRDSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 412 ----LRQTISVVPQrvhlfsATLRDNLLLASPGSS------DEALS---EILRRVGLEkllEDAG-LNSWLGEGGRQLsg 477
Cdd:NF040905 79 giviIHQELALIPY------LSIAENIFLGNERAKrgvidwNETNRrarELLAKVGLD---ESPDtLVTDIGVGKQQL-- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 478 gelrrLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEmMREK--TVLMVTHRLRGLSRF-QQIIVMDNGQIIE 552
Cdd:NF040905 148 -----VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQgiTSIIISHKLNEIRRVaDSITVLRDGRTIE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
306-550 |
7.36e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 306 QVIASAVRISDLTD-QKPEVTFPDTQ-TRVADRVSLTLRDVqftypeqSQQALKGISLQVNAGEHIAILGRTGCGKSTLL 383
Cdd:PRK15439 234 QAITPAAREKSLSAsQKLWLELPGNRrQQAAGAPVLTVEDL-------TGEGFRNISLEVRAGEILGLAGVVGAGRTELA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 384 QQLTRAWDPQQGEILLNDSPIASLNEAA-LRQTISVVP---QRVHLF-SATLRDN---LLLASPG-----SSDEALSEIL 450
Cdd:PRK15439 307 ETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYlDAPLAWNvcaLTHNRRGfwikpARENAVLERY 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 451 RRVGLEKLledaglnSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKT-VLMV 529
Cdd:PRK15439 387 RRALNIKF-------NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFI 459
|
250 260
....*....|....*....|....
gi 447124921 530 T---HRLRGLSrfQQIIVMDNGQI 550
Cdd:PRK15439 460 SsdlEEIEQMA--DRVLVMHQGEI 481
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-314 |
8.12e-08 |
|
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: 53.98 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYsfnYMLPAAGVRGAAITRTAGRYFERLVSHdatfRVLQHLRI 97
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGL---LALLVALFLLQAVLSALSSYLLGRTGE----RVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 98 YTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAFTLGGIMLLTLFLM 177
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 178 PPLFYRAGKSTGQNLTHLrGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIMLLIGAL 257
Cdd:cd18551 154 LPLGRRIRKASKRAQDAL-GELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 258 AVILMLWMasGGV---GGNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd18551 233 ALLVVLGV--GGArvaSGALTVGTLVA-FLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
363-549 |
1.05e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.19 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 363 VNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNdspiaslneaalRQTISVVPQRVhlfsatlrdnlllaspgss 442
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQYI------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 443 dealseilrrvgleklledaglnswlgeggrQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTE---SQILELLAE 519
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|
gi 447124921 520 mMREKTVLMVTHRLRGLSRFQQIIVMDNGQ 549
Cdd:cd03222 120 -EGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
361-509 |
1.33e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 361 LQVNAGEHIAILGRTGCGKSTLLQQLTrawdpqqGEILLNDSPI---ASLNEAALRQ---------TISVVPQRVHLFSA 428
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIiyeQDLIVARLQQdpprnvegtVYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 429 TLRD-----NLLLASPgsSDEALSEILRrvgLEKLLEDAGL-------NSWLGEGG-------RQLSGGELRRLAIARAL 489
Cdd:PRK11147 97 YLKRyhdisHLVETDP--SEKNLNELAK---LQEQLDHHNLwqlenriNEVLAQLGldpdaalSSLSGGWLRKAALGRAL 171
|
170 180
....*....|....*....|
gi 447124921 490 LHDAPLVLLDEPTEGLDATT 509
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
25-314 |
2.73e-07 |
|
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: 52.49 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 25 AIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLL 104
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 105 PLSPAGLARYRQGELLNRVVADVDTLDHLylrVISPLVGAFVVIMVVTIGLSFLdFTLAFTLGGIMLLTLflmpPLFYRA 184
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDT---LTTTLAEFLRQILTLIGGVVLL-FFISWKLTLLMLATV----PVVVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 185 GKSTGQNLTHLRGQYRQQLTAW-------LQGQAELTIFGA----SDRYRTQLENTeiqwLEAQRRQSELTALSQAIMLL 253
Cdd:cd18576 153 AVLFGRRIRKLSKKVQDELAEAntiveetLQGIRVVKAFTRedyeIERYRKALERV----VKLALKRARIRALFSSFIIF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 254 IGALAVILMLWMASGGV-GGNAQPGALIALFVFCAL--AAFEALAPVTGAFQhlgQVIASAVRI 314
Cdd:cd18576 229 LLFGAIVAVLWYGGRLVlAGELTAGDLVAFLLYTLFiaGSIGSLADLYGQLQ---KALGASERV 289
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
356-561 |
3.59e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ---QGEILLNDSpiaSLNEAALRQTISVVPQR-VHLFSATLR 431
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY---RLNEFVPRKTSAYISQNdVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASP----GSSDEALSEILRRVGLEKLLEDA------------GLNSWL--------------------GEGGRQL 475
Cdd:PLN03140 258 ETLDFSARcqgvGTRYDLLSELARREKDAGIFPEAevdlfmkatameGVKSSLitdytlkilgldickdtivgDEMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 476 SGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMR--EKTVLMV-------THRLrglsrFQQIIVMD 546
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMSllqpapeTFDL-----FDDIILLS 412
|
250
....*....|....*
gi 447124921 547 NGQIIEQGTHAELLA 561
Cdd:PLN03140 413 EGQIVYQGPRDHILE 427
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
359-550 |
4.94e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQ-QGEILLNDSPIASLNEA-ALRQTISVVPQR------VHLFSatL 430
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgiVPVMG--V 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 431 RDNLLLAS------PGSSDEALSEILRRVGLEKL-LEDAGLNSWLGeggrQLSGGELRRLAIARALLHDAPLVLLDEPTE 503
Cdd:PRK13549 359 GKNITLAAldrftgGSRIDDAAELKTILESIQRLkVKTASPELAIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447124921 504 GLDATTESQILELLAEMMREK-TVLMVTHRLR---GLSrfQQIIVMDNGQI 550
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGvAIIVISSELPevlGLS--DRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
354-551 |
6.08e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 354 QALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIA-SLNEAALRQTISVVPQRVHLF-SATLR 431
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNLLLASPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLdatTES 511
Cdd:PRK10982 92 DNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447124921 512 QILEL--LAEMMREK--TVLMVTHRLRGLsrFQ---QIIVMDNGQII 551
Cdd:PRK10982 169 EVNHLftIIRKLKERgcGIVYISHKMEEI--FQlcdEITILRDGQWI 213
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-281 |
8.08e-07 |
|
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: 50.97 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 22 IVLAIVTLLASIGLLTLSGWFL-----------SASAVAGVAGLYSFNYM----LPAAGVRGAAITRTAGRYFERLVSHD 86
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLkvviddvlgdkPLPGLLGLAPLLGPDPLalllLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 87 ATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftl 166
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLA--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 167 ggimLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQQ--LTAWLQG--------QAeltiFGASDRYRTQLENTEIQWLEA 236
Cdd:cd18564 158 ----LIALAVAPLLLLAARRFSRRIKEASREQRRREgaLASVAQEslsairvvQA----FGREEHEERRFARENRKSLRA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447124921 237 QRRQSELTALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIA 281
Cdd:cd18564 230 GLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVlAGRLTPGDLLV 275
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
359-558 |
1.69e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 359 ISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEA-ALRQTISVVPQR------VHLfsATLR 431
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdAIRAGIMLCPEDrkaegiIPV--HSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 432 DNL------------LLASPGSSDEALSEILRRV-----GLEKLLedaglnswlgeggRQLSGGELRRLAIARALLHDAP 494
Cdd:PRK11288 350 DNInisarrhhlragCLINNRWEAENADRFIRSLniktpSREQLI-------------MNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447124921 495 LVLLDEPTEGLDATTESQILELLAEMM-REKTVLMVTHRLR---GLSrfQQIIVMDNGQIIEQGTHAE 558
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLPevlGVA--DRIVVMREGRIAGELAREQ 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-531 |
2.06e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILL-------------------NDSPIASLNEAALRQTi 416
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgiklgyfaqhqleflraDESPLQHLARLAPQEL- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 417 svvpqrvhlfSATLRDnlLLASPGSSDEALSEILRRvgleklledaglnswlgeggrqLSGGELRRLAIARALLHDAPLV 496
Cdd:PRK10636 407 ----------EQKLRD--YLGGFGFQGDKVTEETRR----------------------FSGGEKARLVLALIVWQRPNLL 452
|
170 180 190
....*....|....*....|....*....|....*
gi 447124921 497 LLDEPTEGLDATTESQILELLAEMmrEKTVLMVTH 531
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDF--EGALVVVSH 485
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
25-227 |
4.05e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 48.94 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 25 AIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPA-AGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKL 103
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLlLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 104 LPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAFtlggIMLLTLFLMPPLFYR 183
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSAL----ILLVTAPLIPLFMIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447124921 184 AGKSTgQNLThlrgqyRQQLTA----------WLQGQAELTIFGASDRYRTQLE 227
Cdd:cd18584 157 IGKAA-QAAS------RRQWAAlsrlsghfldRLRGLPTLKLFGRARAQAARIA 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
475-566 |
4.29e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 475 LSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTH---RLRGLSrfQQIIVMDNGQ- 549
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSempELLGIT--DRILVMSNGLv 469
|
90 100
....*....|....*....|.
gi 447124921 550 --IIE--QGTHAELLARQGRY 566
Cdd:PRK10982 470 agIVDtkTTTQNEILRLASLH 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-561 |
6.19e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 475 LSGGELRRLAIARALLhDAPLVL-LDEPTEGLDATTESQILELLAEMMREK-TVLMVTH---RLRGLSrfQQIIVMDNGQ 549
Cdd:PRK10762 396 LSGGNQQKVAIARGLM-TRPKVLiLDEPTRGVDVGAKKEIYQLINQFKAEGlSIILVSSempEVLGMS--DRILVMHEGR 472
|
90
....*....|....*..
gi 447124921 550 I-----IEQGTHAELLA 561
Cdd:PRK10762 473 IsgeftREQATQEKLMA 489
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-314 |
1.31e-05 |
|
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: 47.17 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 21 GIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFN--YML-------PAAGVRGAAITrTAGryfERLVSHdatfrv 91
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELalILLaiyllqsVFTFVRYYLFN-IAG---ERIVAR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 92 lqhLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVvimVVTIGLSFLdFTLAFTLGGIML 171
Cdd:cd18557 71 ---LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNIL---QVIGGLIIL-FILSWKLTLVLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 172 LTlflMPPLFYrAGKSTGQNLTHLRGQYRQQLTA-------WLQGQAELTIFGA----SDRYRTQLENTeiqwLEAQRRQ 240
Cdd:cd18557 144 LV---IPLLLI-ASKIYGRYIRKLSKEVQDALAKagqvaeeSLSNIRTVRSFSAeekeIRRYSEALDRS----YRLARKK 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 241 SELTALSQAIMLLIGALAVILMLWMASGGVG-GNAQPGALIAlFVFCALAAFEALAPVTGAFQHLGQVIASAVRI 314
Cdd:cd18557 216 ALANALFQGITSLLIYLSLLLVLWYGGYLVLsGQLTVGELTS-FILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
360-531 |
3.16e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 360 SLQVNAGEHIAILGRTGCGKSTLLQQLT-RAWD--PQQGEILLNDSPIASLNEAALR--------------QTISVVPQR 422
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILHVEQEVVGDDTTALQcvlntdiertqlleEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 423 VHLFSATLRDNLLLASPGSSD-----EALSEILRRvgLEKLLED----------AGLnSWLGE----GGRQLSGGELRRL 483
Cdd:PLN03073 277 RELEFETETGKGKGANKDGVDkdavsQRLEEIYKR--LELIDAYtaearaasilAGL-SFTPEmqvkATKTFSGGWRMRI 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447124921 484 AIARALLHDAPLVLLDEPTEGLDAtteSQILELLAEMMR-EKTVLMVTH 531
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKwPKTFIVVSH 399
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
356-515 |
3.86e-05 |
|
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: 46.47 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 356 LKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSpiaslneaalrQTISVVPQRvhlfsatlRDNLl 435
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----------VKLAYVDQS--------RDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 436 laSPGSSD-EALSEilrrvGLEKL-LEDAGLNS--WLG----EGGRQ------LSGGELRRLAIARALLHDAPLVLLDEP 501
Cdd:TIGR03719 398 --DPNKTVwEEISG-----GLDIIkLGKREIPSraYVGrfnfKGSDQqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170
....*....|....*...
gi 447124921 502 TEGLDATT----ESQILE 515
Cdd:TIGR03719 471 TNDLDVETlralEEALLN 488
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
90-302 |
4.18e-05 |
|
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: 45.55 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 90 RVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDtldhlylrVISPLVGAFVVI----MVVTIGLSFLDFTLAFT 165
Cdd:cd18575 66 RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTT--------LIQTVVGSSLSIalrnLLLLIGGLVMLFITSPK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 166 LGGIMLLTLFLM--PPLFYragkstGQNLTHLRGQYrQQLTAWLQGQAELTI--------FG----ASDRYRTQLENTei 231
Cdd:cd18575 138 LTLLVLLVIPLVvlPIILF------GRRVRRLSRAS-QDRLADLSAFAEETLsaiktvqaFTredaERQRFATAVEAA-- 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 232 qwLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIAlFVFCAL---AAFEALAPVTGAFQ 302
Cdd:cd18575 209 --FAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVlAGRMSAGELSQ-FVFYAVlaaGSVGALSEVWGDLQ 280
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
444-533 |
4.87e-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: 45.30 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 444 EALSEILRRVgleKLLEDAGLNSW-LGEGGRQLSGGELRRLAIARALLHDAP---LVLLDEPTEGLDATTESQILELLAE 519
Cdd:cd03271 141 ENIPKIARKL---QTLCDVGLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQR 217
|
90
....*....|....*
gi 447124921 520 MM-REKTVLMVTHRL 533
Cdd:cd03271 218 LVdKGNTVVVIEHNL 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-533 |
5.38e-05 |
|
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: 43.89 E-value: 5.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447124921 474 QLSGGELRRLAIARAL----LHDAPLVLLDEPTEGLDATTESQILELLAEMMREK-TVLMVTHRL 533
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLP 141
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
474-568 |
7.07e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 474 QLSGGE------LRRLAIARALLHDAPLVLLDEPTEGLDattESQILELLAEMMREktvlmvthrLRGLSRFQQIIVmdn 547
Cdd:cd03240 115 RCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEE---------RKSQKNFQLIVI--- 179
|
90 100
....*....|....*....|..
gi 447124921 548 gqiieqgTHAE-LLARQGRYYQ 568
Cdd:cd03240 180 -------THDEeLVDAADHIYR 194
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
319-531 |
8.86e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 319 DQKPEVTFPDtqtrvaDRVS---LTLRDVQFTYPeQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQG 395
Cdd:PLN03073 492 DYKFEFPTPD------DRPGppiISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 396 EIllndspiasLNEAALRqtISVVPQRvHLFSATLRDNLLL----ASPGSSDEALSEILRRVGLEKLLEDAGLNSwlgeg 471
Cdd:PLN03073 565 TV---------FRSAKVR--MAVFSQH-HVDGLDLSSNPLLymmrCFPGVPEQKLRAHLGSFGVTGNLALQPMYT----- 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 472 grqLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAemMREKTVLMVTH 531
Cdd:PLN03073 628 ---LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV--LFQGGVLMVSH 682
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
474-531 |
1.08e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447124921 474 QLSGGElR-------RLAIARALLH----DAPL--VLLDEPTEGLDATTESQILELLaEMMREKTV---LMVTH 531
Cdd:PRK02224 781 QLSGGE-RalfnlslRCAIYRLLAEgiegDAPLppLILDEPTVFLDSGHVSQLVDLV-ESMRRLGVeqiVVVSH 852
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
410-531 |
4.30e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 410 AALRQTISVVPQRVHLFSATLRDnlllASPGSSD-EALSEILRRVGLEklLEDAGLNSWLGEggRQLSGGELRRLAIArA 488
Cdd:COG4637 201 AVLATLRETHPERFERILEALRD----AFPGFEDiEVEPDEDGRVLLE--FREKGLDRPFPA--RELSDGTLRFLALL-A 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 447124921 489 LLHDA---PLVLLDEPTEGLDatteSQILELLAEMMRE----KTVLMVTH 531
Cdd:COG4637 272 ALLSPrppPLLCIEEPENGLH----PDLLPALAELLREaserTQVIVTTH 317
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-177 |
4.41e-04 |
|
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: 42.39 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 22 IVLAIVTLLASIGLLTLSGWFL-----SASAVAGVAGLYSFNYMLPAAGVRGAA-ITRTAGRYFERLVSHDATFRVLQHL 95
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLgkaidLIIEGLGGGGGVDFSGLLRILLLLLGLyLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 96 RIYTFSKL--LPLSpaglarY----RQGELLNRVVADVDTLDHLYLRVISPLVGAFVVImvvtIGLSFLDFTLAFTLGGI 169
Cdd:cd18547 81 RKDLFEKLqrLPLS------YfdthSHGDIMSRVTNDVDNISQALSQSLTQLISSILTI----VGTLIMMLYISPLLTLI 150
|
....*...
gi 447124921 170 MLLTLFLM 177
Cdd:cd18547 151 VLVTVPLS 158
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
457-559 |
9.62e-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: 42.31 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 457 KLLEDAGLNSW-LGEGGRQLSGGELRRLAIARALLHDA---PLVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTH 531
Cdd:TIGR00630 811 QTLCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEH 890
|
90 100 110
....*....|....*....|....*....|....
gi 447124921 532 RLRGLSRFQQIIVM------DNGQIIEQGTHAEL 559
Cdd:TIGR00630 891 NLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
22-284 |
1.13e-03 |
|
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: 41.24 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 22 IVLAIVTLLASIGLLTLSGWFLSAsAVAGVA--GLYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYT 99
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGR-AIDALTagTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 100 FSKLLPLSPAGLARYRQGELLNRVVADVDTLDhlylRVISP----LVGAFVVIMVVTIGLSFLDFTLAFtlggIMLLTLF 175
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVR----MALGPgilyLVDALFLGVLVLVMMFTISPKLTL----IALLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 176 LMPPLFYRAGKSTGQNLTHLRGQYrQQLTAWLQ----GQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIM 251
Cdd:cd18541 152 LLALLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLI 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 447124921 252 LLIGALAVILMLWMasGG---VGGNAQPGALIALFV 284
Cdd:cd18541 231 GLLIGLSFLIVLWY--GGrlvIRGTITLGDLVAFNS 264
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
18-283 |
1.77e-03 |
|
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: 40.55 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYsfnyMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRI 97
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVL----LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 98 YTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAftlggimLLTLFLM 177
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLA-------LVALAAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 178 PPLF-----YRAGKSTGQNLT-----HLRGQYRQQLT------AWLQGQAELTIFGA-SDRYRtqlenteiqwlEAQRRQ 240
Cdd:cd18546 150 PPLAlatrwFRRRSSRAYRRAreriaAVNADLQETLAgirvvqAFRRERRNAERFAElSDDYR-----------DARLRA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447124921 241 SELTALSQAIMLLIGALAVILMLWMASGGV-GGNAQPGALIALF 283
Cdd:cd18546 219 QRLVAIYFPGVELLGNLATAAVLLVGAWRVaAGTLTVGVLVAFL 262
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
18-260 |
1.79e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 40.54 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 18 LSLGIVLAIVTLLASIGLLTLSGWFL-SASAVAGVAGLYsfnymLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLR 96
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 97 IYTFSKLLPLSPAGLARYRQGELLNRVVADvdtldhlyLRVISPLV--GAFVVIMVVTIGLSF-LDFTLAFTLGGIMLLT 173
Cdd:cd18543 76 TDLFAHLQRLDGAFHDRWQSGQLLSRATSD--------LSLVQRFLafGPFLLGNLLTLVVGLvVMLVLSPPLALVALAS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 174 lflMPPLFYRAgkstgqnlTHLRGQYR------QQLTAWLQGQAELTI--------FGASDR------------YRTQLE 227
Cdd:cd18543 148 ---LPPLVLVA--------RRFRRRYFpasrraQDQAGDLATVVEESVtgirvvkaFGRERReldrfeaaarrlRATRLR 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 447124921 228 NTEIQ-----WLEAqrrqseLTALSQAIMLLIGALAVI 260
Cdd:cd18543 217 AARLRarfwpLLEA------LPELGLAAVLALGGWLVA 248
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
470-531 |
2.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447124921 470 EGGRQLSGGELR------RLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKT----VLMVTH 531
Cdd:PRK01156 797 EGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISH 868
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
474-509 |
2.46e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*.
gi 447124921 474 QLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATT 509
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
468-533 |
2.56e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 468 LGEGGRQLSGGELRRLAIARALLHDAP---LVLLDEPTEGLDATTESQILELLAEMMRE-KTVLMVTHRL 533
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQgHTVVIIEHNM 872
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
368-404 |
4.18e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.21 E-value: 4.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 447124921 368 HIAILGRTGCGKSTLLQQLTRAW-----------DPQQGEILLNDSPI 404
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKaivsdypgttrDPNEGRLELKGKQI 48
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
442-561 |
4.89e-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: 40.00 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447124921 442 SDEALSEILRRVGLeklLEDAGLNSW-LGEGGRQLSGGELRRLAIARALlhDAPLV----LLDEPTEGLDATTESQILEL 516
Cdd:TIGR00630 458 AEEVLKEIRERLGF---LIDVGLDYLsLSRAAGTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINT 532
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 447124921 517 LAEmMREK--TVLMVTHRLRGLSRFQQIIVM------DNGQIIEQGTHAELLA 561
Cdd:TIGR00630 533 LKR-LRDLgnTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| |
