|
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: 993.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 1 MRALLPYLALYKRHKWMLTLGIVLAIVTLLASIGLLTLSGWFLSASAAAGFAGLYSFNYMLPAAGVRGTAITRTAGRYFE 80
Cdd:PRK11160 1 MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFNYMLPAAGVRGAAIGRTAGRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 81 RLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDV 160
Cdd:PRK11160 81 RLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 161 PIALTLGGIMLMTLIILPPLFYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQ 240
Cdd:PRK11160 161 TLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 241 SELTAFSQALMMLIGGIAVIAMLWMASGGVGGNAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAEQ 320
Cdd:PRK11160 241 ANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 321 EPEVKFSAGQTAVPEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN 400
Cdd:PRK11160 321 KPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 401 DVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLEDD-GLNSWLGEGGRQLSGGE 479
Cdd:PRK11160 401 GQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDkGLNAWLGEGGRQLSGGE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 480 LRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
570
....*....|....
gi 489955000 560 LAKQGRYYQFKQRL 573
Cdd:PRK11160 561 LAQQGRYYQLKQRL 574
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-572 |
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: 759.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 2 RALLPYLALYKRHKWMLTLGIVLAIVTLLASIGLLTLSGWFLSASAAAGFaglySFNYMLPAAGVRGTAITRTAGRYFER 81
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPP----ILNLFVPIVGVRAFAIGRTVFRYLER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 82 LVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVP 161
Cdd:COG4987 77 LVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 162 IALTLGGIMLMTLIILPPLFYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQS 241
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 242 ELTAFSQALMMLIGGIAVIAMLWMASGGVGGNAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAEQE 321
Cdd:COG4987 237 RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 322 PEVKFSAGQTAVPEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFND 401
Cdd:COG4987 317 PAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 402 VPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGE 479
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAAlpDGLDTWLGEGGRRLSGGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 480 LRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
570
....*....|...
gi 489955000 560 LAKQGRYYQFKQR 572
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| 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: 554.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 4 LLPYLALYKRHKWMLTLGIVLAIVTLLASIGLLTLSGWFLSASAAAGFAGLYsfnyMLPAAGVRGTAITRTAGRYFERLV 83
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYL----SVAAVAVRAFGIGRAVFRYLERLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 84 SHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVPIA 163
Cdd:TIGR02868 77 GHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 164 LTLGGIMLMTLIILPPLFYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQSEL 243
Cdd:TIGR02868 157 LILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 244 TAFSQALMMLIGGIAVIAMLWMASGGVGGNAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAEQEPE 323
Cdd:TIGR02868 237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 324 VK---FSAGQTAVPEQVALTLSNVTFAYDkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN 400
Cdd:TIGR02868 317 VAegsAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 401 DVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGG 478
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 479 ELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRL 533
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-569 |
4.59e-133 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 399.92 E-value: 4.59e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 1 MRALLPYLalyKRHKWMLTLGIVLAIVTLLASIGLLTLSGWFLSASAAAGfaglySFNYMLPAAGVR-GTAITRTAGRYF 79
Cdd:COG1132 9 LRRLLRYL---RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-----DLSALLLLLLLLlGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 80 ERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLD 159
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 160 VPIALTLGGIMLMTLIILPpLFYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRR 239
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLR-LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 240 QSELTAFSQALMMLIGGIAVIAMLWMASGGV-GGNAQPGPLIAlFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIA 318
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVlSGSLTVGDLVA-FILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 319 EQEPEVKFSAGQTAVPE-QVALTLSNVTFAYDKqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEI 397
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPvRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 398 RFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQL 475
Cdd:COG1132 398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEAlpDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 476 SGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGS 555
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|....
gi 489955000 556 HAELLAKQGRYYQF 569
Cdd:COG1132 558 HEELLARGGLYARL 571
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-314 |
5.56e-129 |
|
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: 379.13 E-value: 5.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 25 AIVTLLASIGLLTLSGWFLSASAAAGFAGlYSFNYMLPAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLL 104
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAA-PTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 105 PLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVPIALTLGGIMLMTLIILPPLFYRA 184
Cdd:cd18585 80 PLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 185 GKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAMLW 264
Cdd:cd18585 160 GKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489955000 265 MASGGVGGNAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASALRI 314
Cdd:cd18585 240 LGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRL 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-564 |
1.88e-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: 1.88e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 1 MRALLPYL-ALYKRHKWMLTLGIVLAIVTLLASIGLLTLSGWFLSASAAAGFAGLYSFNYMLPAAGVrgtAITRTAGRYF 79
Cdd:COG4988 1 QKPLDKRLkRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAV---LLLRALLAWL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 80 ERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLD 159
Cdd:COG4988 78 RERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 160 VPIALtlggIMLMTLIILPpLF-----YRAGKTTGEN---LTRLRGeyrqQLTAWLQGQAELTLFGASKRYRARMentel 231
Cdd:COG4988 158 WLSGL----ILLVTAPLIP-LFmilvgKGAAKASRRQwraLARLSG----HFLDRLRGLTTLKLFGRAKAEAERI----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 232 nwheaqRRQSEltAFSQALMmliggiAV--IAML------WMASGGVGgnaqpgpLIALFV---------------FCAL 288
Cdd:COG4988 224 ------AEASE--DFRKRTM------KVlrVAFLssavleFFASLSIA-------LVAVYIgfrllggsltlfaalFVLL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 289 AAFEALAPV--TGAFQHLG-QVIASALRITDIAEQEPEVKFSAGQTA-VPEQVALTLSNVTFAYDkQAQNALEDITLSVD 364
Cdd:COG4988 283 LAPEFFLPLrdLGSFYHARaNGIAAAEKIFALLDAPEPAAPAGTAPLpAAGPPSIELEDVSFSYP-GGRPALDGLSLTIP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 365 AGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDD 444
Cdd:COG4988 362 PGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 445 TLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK 522
Cdd:COG4988 442 ELEAALEAAGLDEFVAAlpDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 489955000 523 GKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQG 564
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
100-572 |
8.26e-107 |
|
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: 336.42 E-value: 8.26e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 100 FSKLLPLSPAGLARFRQGELLNRVvADVDTLDHLylrVISPMVGAFVVIVVVTLGL---SFLDVPIAL-TLGGIMLMTLI 175
Cdd:COG2274 236 FRHLLRLPLSFFESRSVGDLASRF-RDVESIREF---LTGSLLTALLDLLFVLIFLivlFFYSPPLALvVLLLIPLYVLL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 176 ILppLFYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIG 255
Cdd:COG2274 312 GL--LFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 256 GIAVIAMLWMASGGV-GGNAQPGPLIAlFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAEQEPEVKFSAGQTAVP 334
Cdd:COG2274 390 QLATVALLWLGAYLViDGQLTLGQLIA-FNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLP 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 335 E-QVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALR 413
Cdd:COG2274 469 RlKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLH 491
Cdd:COG2274 549 RQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEAlpMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQFKQ 571
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
.
gi 489955000 572 R 572
Cdd:COG2274 709 Q 709
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
339-554 |
1.01e-79 |
|
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: 248.38 E-value: 1.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFsEAALRKTVSV 418
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLllaapdasddtlramleqvglhklleddglnswlgegGRQLSGGELRRLAIARALLHDAPLMLL 498
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 499 DEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQG 554
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
339-568 |
2.55e-76 |
|
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: 241.75 E-value: 2.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRfpDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQ 568
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-568 |
1.22e-75 |
|
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: 239.83 E-value: 1.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLE--DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQ 568
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
25-314 |
2.36e-74 |
|
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: 238.33 E-value: 2.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 25 AIVTLLASIGLLTLSGWFLSASAAAGFAGLYSFNYMLPAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLL 104
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 105 PLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVPIALtLGGIMLMTLIILPPLFYRA 184
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVAL-ILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 185 GKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAMLW 264
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489955000 265 MASGGVGGnAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASALRI 314
Cdd:cd18561 240 VGALRVLG-GQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADS 288
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
343-564 |
1.03e-73 |
|
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: 234.43 E-value: 1.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQR 422
Cdd:cd03254 7 NVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDE 500
Cdd:cd03254 86 TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKlpNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 501 PTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQG 564
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
339-549 |
3.45e-73 |
|
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: 231.12 E-value: 3.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLllaapdasddtlramleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLHDAPLMLL 498
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489955000 499 DEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGH 549
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-566 |
1.94e-70 |
|
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: 236.92 E-value: 1.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 2 RALLPYLALYKrhkWMLTLGIVLAIV-----TLLASIGLLTLSGWFLSASAAAGfaglysfnYMLPAaGVRGTAITRTAG 76
Cdd:TIGR02203 3 RRLWSYVRPYK---AGLVLAGVAMILvaateSTLAALLKPLLDDGFGGRDRSVL--------WWVPL-VVIGLAVLRGIC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 77 RYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDtldhlylRVISPMVGAFVVIVVVTLGLS 156
Cdd:TIGR02203 71 SFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSE-------QVASAATDAFIVLVRETLTVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 157 FLDVPIALTLGGIMLMTLIILPPL------FYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGA----SKRYrARM 226
Cdd:TIGR02203 144 GLFIVLLYYSWQLTLIVVVMLPVLsilmrrVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGqayeTRRF-DAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 227 ENTELNWheaQRRQSELTAFSQALMMLIGGIAVIAMLWMAS-GGVGGNAQPGPLIALFVfCALAAFEALAPVTGAFQHLG 305
Cdd:TIGR02203 223 SNRNRRL---AMKMTSAGSISSPITQLIASLALAVVLFIALfQAQAGSLTAGDFTAFIT-AMIALIRPLKSLTNVNAPMQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 306 QVIASALRITDIAEQEPEVkfSAGqTAVPEQVA--LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLL 383
Cdd:TIGR02203 299 RGLAAAESLFTLLDSPPEK--DTG-TRAIERARgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 384 QLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAP-DASDDTLRAMLEQVGLHKLLE-- 460
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDkl 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 461 DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFD 540
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
570 580
....*....|....*....|....*.
gi 489955000 541 QIIVMDNGHIIEQGSHAELLAKQGRY 566
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
216-568 |
7.48e-70 |
|
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: 236.26 E-value: 7.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 216 FGASKRYRARMENTELNWHEAQRR-QSELTA--FSQALMMligGIAVIAMLWMASGGV-GGNAQPG-------------- 277
Cdd:COG5265 234 FGNEAREARRYDEALARYERAAVKsQTSLALlnFGQALII---ALGLTAMMLMAAQGVvAGTMTVGdfvlvnayliqlyi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 278 PLIAL-FVF----CALAAFEALApvtgafqhlgqviasalritDIAEQEPEVKFSAG-QTAVPEQVALTLSNVTFAYDKQ 351
Cdd:COG5265 311 PLNFLgFVYreirQALADMERMF--------------------DLLDQPPEVADAPDaPPLVVGGGEVRFENVSFGYDPE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 352 AQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLR 431
Cdd:COG5265 371 RP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIA 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATT 509
Cdd:COG5265 450 YNIAYGRPDASEEEVEAAARAAQIHDFIESlpDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 510 ESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQ 568
Cdd:COG5265 530 ERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
62-545 |
1.36e-68 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 230.64 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 62 PAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPM 141
Cdd:TIGR02857 46 ALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 142 VGAfvviVVVTLGLSFLDVPIALTLGGIMLMTLIILPpLF-----YRAGKTTGEN---LTRLRGeyrqQLTAWLQGQAEL 213
Cdd:TIGR02857 126 VLA----VIVPLAILAAVFPQDWISGLILLLTAPLIP-IFmiligWAAQAAARKQwaaLSRLSG----HFLDRLRGLPTL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 214 TLFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIG--GIAVIAM---LWMASGGVggnaqpgPLIALFvFCAL 288
Cdd:TIGR02857 197 KLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFAtlSVALVAVyigFRLLAGDL-------DLATGL-FVLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 289 AAFEALAPV--TGAFQHLG-QVIASALRITDIAEQEPEVKFSAGQTAVPEQVALTLSNVTFAYdKQAQNALEDITLSVDA 365
Cdd:TIGR02857 269 LAPEFYLPLrqLGAQYHARaDGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 366 GQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDT 445
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 446 LRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKG 523
Cdd:TIGR02857 428 IREALERAGLDEFVAAlpQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG 507
|
490 500
....*....|....*....|..
gi 489955000 524 KTVLMVTHRLRGLVNFDQIIVM 545
Cdd:TIGR02857 508 RTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
340-569 |
1.37e-68 |
|
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: 221.64 E-value: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNVTFAYDKQAQN-ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03249 2 EFKNVSFRYPSRPDVpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQF 569
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
338-554 |
6.27e-67 |
|
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: 216.69 E-value: 6.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQG 554
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-569 |
2.97e-64 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 220.60 E-value: 2.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQR 422
Cdd:PRK13657 339 DVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLE--DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDE 500
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 501 PTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQF 569
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
160-562 |
1.19e-62 |
|
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: 218.58 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 160 VPIALtLGGIMLMTLIILPPLfyraGKTTGENLTRlrGEYRQQ-LTAWLQGQAELTLFGASKRYRARMENTELNWHEAQR 238
Cdd:TIGR03375 290 VPLVA-IPLILLPGLLLQRPL----SRLAEESMRE--SAQRNAvLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 239 RQSELTAFSQALMMLIGGIAVIAML----WMASGG---VGGnaqpgpLIAlfvfCALAAFEALAPVtGAFQHL---GQVI 308
Cdd:TIGR03375 363 KSRFLSNLATNFAQFIQQLVSVAIVvvgvYLISDGeltMGG------LIA----CVMLSGRALAPL-GQLAGLltrYQQA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 309 ASALRITDIAEQEPeVKFSAGQTAVPEQV---ALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQL 385
Cdd:TIGR03375 432 KTALQSLDELMQLP-VERPEGTRFLHRPRlqgEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 386 LTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DG 463
Cdd:TIGR03375 511 LLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRhpDG 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 464 LNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQII 543
Cdd:TIGR03375 591 LDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRII 670
|
410
....*....|....*....
gi 489955000 544 VMDNGHIIEQGSHAELLAK 562
Cdd:TIGR03375 671 VMDNGRIVADGPKDQVLEA 689
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
207-568 |
7.93e-60 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 208.72 E-value: 7.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 207 LQGQAELTLFGASKRYRARMENTELNwheaQRRQS----ELTAFSQALMMLIGGIAVIAMLWMAS-GGVGGNAQPGPLIA 281
Cdd:PRK11176 211 LKGHKEVLIFGGQEVETKRFDKVSNR----MRQQGmkmvSASSISDPIIQLIASLALAFVLYAASfPSVMDTLTAGTITV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 282 LF--VFCALAAFEALAPVTGAFQHlGQVIASAL-RITDIAEQEPEVKFSAGQTavpeQVALTLSNVTFAYDKQAQNALED 358
Cdd:PRK11176 287 VFssMIALMRPLKSLTNVNAQFQR-GMAACQTLfAILDLEQEKDEGKRVIERA----KGDIEFRNVTFTYPGKEVPALRN 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 359 ITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAA 438
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 439 pdaSDDTLRAMLEQVG--------LHKLleDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTE 510
Cdd:PRK11176 442 ---TEQYSREQIEEAArmayamdfINKM--DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 511 SQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQ 568
Cdd:PRK11176 517 RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
280-569 |
1.74e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.38 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 280 IALFV--FCALAAFEALAPV--TGAFQHL-GQVIASALRITDIAEQePEVKFSAGQTAVPEQVALTLSN---VTFAYDKQ 351
Cdd:PRK11174 285 VTLFAgfFVLILAPEFYQPLrdLGTFYHAkAQAVGAAESLVTFLET-PLAHPQQGEKELASNDPVTIEAedlEILSPDGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 352 AqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTrAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLR 431
Cdd:PRK11174 364 T--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATT 509
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLlpQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 510 ESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQF 569
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
343-555 |
5.06e-57 |
|
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: 190.78 E-value: 5.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQR 422
Cdd:cd03244 7 NVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFSATLRDNLllaAPD--ASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLL 498
Cdd:cd03244 87 PVLFSGTIRSNL---DPFgeYSDEELWQALERVGLKEFVESlpGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 499 DEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGS 555
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-571 |
1.74e-54 |
|
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: 184.61 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQFKQ 571
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
339-563 |
7.39e-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: 171.75 E-value: 7.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQ--RVHLFSATLRD-------NLLLAAPDAsDDTLRAMLEQVGLHKLLEddglnswlgeggR---QLSGGELRRLAIA 486
Cdd:COG1122 80 VFQnpDDQLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHLAD------------RpphELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLV-NFDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
339-568 |
3.66e-48 |
|
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: 178.78 E-value: 3.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:TIGR01193 474 IVINDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLAA-PDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:TIGR01193 553 LPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANvMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQ 568
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-549 |
4.55e-48 |
|
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: 166.49 E-value: 4.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVP 420
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 421 Q--RVHLFSATLRD-------NLLLAAPDAsDDTLRAMLEQVGLHKLLEDDglnswlgegGRQLSGGELRRLAIARALLH 491
Cdd:cd03225 82 QnpDDQFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGH 549
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
338-571 |
5.04e-48 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.45 E-value: 5.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQaQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:PRK10790 340 RIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSATLRDNLLLAApDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQFKQ 571
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
313-571 |
1.31e-46 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 172.20 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 313 RITDIAEQEPEVKfsAGQTAVPEQVALTLSNV-TFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD 391
Cdd:PRK10789 289 RIRAMLAEAPVVK--DGSEPVPEGRGELDVNIrQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 392 PQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASddtlRAMLEQVGLHKLLEDD------GLN 465
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAT----QQEIEHVARLASVHDDilrlpqGYD 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 466 SWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVM 545
Cdd:PRK10789 443 TEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVM 522
|
250 260
....*....|....*....|....*....
gi 489955000 546 DNGHIIEQGSHAELLAKQGRY---YQFKQ 571
Cdd:PRK10789 523 QHGHIAQRGNHDQLAQQSGWYrdmYRYQQ 551
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
336-553 |
2.17e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.52 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 336 QVALTLSNVTFAYD--KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQL---LTRawdPQQGEIRFNDVPLSGFSEA 410
Cdd:COG1136 2 SPLLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 AL----RKTVSVVPQRVHLF-SATLRDN----LLLAAPDASDDTLRA--MLEQVGLHKLLEDdglnswlgeggR--QLSG 477
Cdd:COG1136 79 ELarlrRRHIGFVFQFFNLLpELTALENvalpLLLAGVSRKERRERAreLLERVGLGDRLDH-----------RpsQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 478 GELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQ 553
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
338-560 |
4.08e-46 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 162.52 E-value: 4.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHL-FSATLRDNLLL---------AAPDASDDTL-RAMLEQVGLHKLLEddglnswlgeggR---QLSGGELRRL 483
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALgryphlglfGRPSAEDREAvEEALERTGLEHLAD------------RpvdELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 484 AIARALLHDAPLMLLDEPTEGLDATTESQILDLLA--NVMKGKTVLMVTHRLrglvNF-----DQIIVMDNGHIIEQGSH 556
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDL----NLaaryaDRLVLLKDGRIVAQGPP 222
|
....
gi 489955000 557 AELL 560
Cdd:COG1120 223 EEVL 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-561 |
8.62e-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: 8.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQN--ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKT 415
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQrvHLFSA-----TLRDnlLLAAP------DASDDTLRAMLEQVGLHKlleddglnSWLGEGGRQLSGGELRRLA 484
Cdd:COG1124 81 VQMVFQ--DPYASlhprhTVDR--ILAEPlrihglPDREERIAELLEQVGLPP--------SFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQGSHAELL 560
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDL-AVVAHlcDRVAVMQNGRIVEELTVADLL 227
|
.
gi 489955000 561 A 561
Cdd:COG1124 228 A 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-550 |
3.40e-45 |
|
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: 158.81 E-value: 3.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQN--ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL---- 412
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 RKTVSVVPQRVHL---FSAtlRDNLLLAA------PDASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRL 483
Cdd:cd03255 81 RRHIGFVFQSFNLlpdLTA--LENVELPLllagvpKKERRERAEELLERVGLGDRLN---------HYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 484 AIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRgLVN-FDQIIVMDNGHI 550
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPE-LAEyADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
327-561 |
7.76e-45 |
|
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: 166.23 E-value: 7.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 327 SAGQTAVPEQVALTLSNVTFAYD---KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVP 403
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 404 LSGFSEA---ALRKTVSVVPQRVhlFSA-----TLRD-------NLLLAAPDASDDTLRAMLEQVGLHKLLEDdglnswl 468
Cdd:COG1123 329 LTKLSRRslrELRRRVQMVFQDP--YSSlnprmTVGDiiaeplrLHGLLSRAERRERVAELLERVGLPPDLAD------- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 469 geggR---QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV--MKGKTVLMVTHRLrGLVNF--DQ 541
Cdd:COG1123 400 ----RyphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDL-AVVRYiaDR 474
|
250 260
....*....|....*....|
gi 489955000 542 IIVMDNGHIIEQGSHAELLA 561
Cdd:COG1123 475 VAVMYDGRIVEDGPTEEVFA 494
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
339-565 |
1.75e-44 |
|
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: 158.10 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKtVSV 418
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSA-TLRDNLLLAAP--DASDDTLRAMLEQVgLHKLLEDDGLNSWLGEggrqLSGGELRRLAIARALLHDAPL 495
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEEL-IELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVN-FDQIIVMDNGHIIEQGSHAELLAKQGR 565
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
343-554 |
3.11e-44 |
|
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: 156.90 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA---ALRKTVSVV 419
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQ----------RV-HLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKlleddglnSWLGEGGRQLSGGELRRLAIARA 488
Cdd:cd03257 88 FQdpmsslnprmTIgEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE--------EVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANV--MKGKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQG 554
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDL-GVVAKiaDRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-562 |
5.55e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.38 E-value: 5.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKtVSV 418
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSA-TLRDNLLLAA------PDASDDTLRAMLEQVGLhklleDDGLNSWLgeggRQLSGGELRRLAIARALLH 491
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFArlyglpRKEARERIDELLELFGL-----TDAADRKV----GTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTH------RLrglvnFDQIIVMDNGHIIEQGSHAELLAK 562
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHyleeaeRL-----CDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
338-560 |
7.80e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.02 E-value: 7.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLsgfseAALRKTVS 417
Cdd:COG1121 6 AIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHL---FSATLRD----------NLLLAAPDASDDTLRAMLEQVGLHKLLeddglNSWLGEggrqLSGGELRRLA 484
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDvvlmgrygrrGLFRRPSRADREAVDEALERVGLEDLA-----DRPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLAN-VMKGKTVLMVTHRLrGLV--NFDQIIVMdNGHIIEQGSHAELL 560
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDL-GAVreYFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
339-550 |
2.58e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:COG4619 1 LELEGLSFRVG--GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLL----LAAPDASDDTLRAMLEQVGL-HKLLEDDGlnswlgeggRQLSGGELRRLAIARALLHDA 493
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLpPDILDKPV---------ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVM--KGKTVLMVTH------RLrglvnFDQIIVMDNGHI 550
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
334-555 |
1.56e-42 |
|
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: 151.41 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALR 413
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFSATLRDNLllaapDA----SDDTLRAMLEqvglhklleddglnswLGEGGRQLSGGELRRLAIARAL 489
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNL-----DPfdeySDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGS 555
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
343-548 |
1.30e-41 |
|
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: 148.77 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNA---LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTrawdpqqGEIRfndvPLSGFSEaaLRKTVSVV 419
Cdd:cd03250 5 DASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELE----KLSGSVS--VPGSIAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQRVHLFSATLRDNLLLAAP-DAS--DDTLRAmleqVGLHKLLE--DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:cd03250 72 SQEPWIQNGTIRENILFGKPfDEEryEKVIKA----CALEPDLEilPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 495 LMLLDEPTEGLDATTESQILD--LLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNG 548
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-554 |
3.25e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 146.81 E-value: 3.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVV 419
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQrvhlfsatlrdnlllaapdasddtlraMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLAD---------RPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 500 EPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
343-550 |
1.96e-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: 146.46 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAY-DKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQ 421
Cdd:cd03248 16 NVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 422 RVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISElaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489955000 500 EPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHI 550
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-561 |
2.19e-40 |
|
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: 146.66 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA--- 410
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 ALRKTVSVVPQRVHLFSA-TLRDNL---LLAAPDASDDTLRAM----LEQVGL----HKLLeddglnswlgeggRQLSGG 478
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVafpLREHTDLSEAEIRELvlekLELVGLpgaaDKMP-------------SELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 479 ELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGS 555
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGT 225
|
....*.
gi 489955000 556 HAELLA 561
Cdd:COG1127 226 PEELLA 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-561 |
1.14e-39 |
|
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: 151.59 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 336 QVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ---QGEIRFNDVPLSGFSEAAL 412
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 RKTVSVVPQ--RVHLFSATLRDNLLLAaPDASDDTLRAMLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALL 490
Cdd:COG1123 82 GRRIGMVFQdpMTQLNPVTVGDQIAEA-LENLGLSRAEARARV--LELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 491 HDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-549 |
1.23e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 142.00 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVV 419
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQrvhlfsatlrdnlllaapdasddtlramleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489955000 500 EPTEGLDATTESQILDLL-ANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGH 549
Cdd:cd00267 106 EPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-552 |
1.36e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.23 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAY--DKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfseaa 411
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQRVHLFS-ATLRDNLLLA------APDASDDTLRAMLEQVGLhklleDDGLNSWlgegGRQLSGGELRRLA 484
Cdd:COG1116 78 PGPDRGVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGL-----AGFEDAY----PHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH------RLRglvnfDQIIVMDN--GHIIE 552
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFLA-----DRVVVLSArpGRIVE 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
87-570 |
1.76e-39 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 153.72 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 87 ATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDhlylRVISPMVGAFVVIVVVTLGLSFLDVPIALTL 166
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMS----RSLSLNVNVLLRNLVMLLGLLGFMLWLSPRL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 167 GgimLMTLIILPPLFYrAGKTTGEnLTRLRGEYRQQLTAWLQGQAELTL--------FGA----SKRYRARMENT-ELNW 233
Cdd:TIGR00958 304 T---MVTLINLPLVFL-AEKVFGK-RYQLLSEELQEAVAKANQVAEEALsgmrtvrsFAAeegeASRFKEALEETlQLNK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 234 HEAQRRQSEL--TAFSQALMMLIggiaviaMLWMASGGVGGNAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASA 311
Cdd:TIGR00958 379 RKALAYAGYLwtTSVLGMLIQVL-------VLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGAS 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 312 LRITDIAEQEPEVKFSAGQTAVPEQVALTLSNVTFAYDKQAQN-ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAW 390
Cdd:TIGR00958 452 EKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 391 DPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLEDD--GLNSWL 468
Cdd:TIGR00958 532 QPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEV 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 469 GEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLlaNVMKGKTVLMVTHRLRGLVNFDQIIVMDNG 548
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKG 689
|
490 500
....*....|....*....|..
gi 489955000 549 HIIEQGSHAELLAKQGRYYQFK 570
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQGCYKHLV 711
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
339-561 |
2.82e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 143.60 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPL--SGFSEAALRKTV 416
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHLFS-ATLRDNLLLA-------APDASDDTLRAMLEQVGLhklleDDGLNSWLGeggrQLSGGELRRLAIARA 488
Cdd:COG1126 80 GMVFQQFNLFPhLTVLENVTLApikvkkmSKAEAEERAMELLERVGL-----ADKADAYPA----QLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDllanVMK-----GKTVLMVTHRLRglvnF-----DQIIVMDNGHIIEQGSHAE 558
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLD----VMRdlakeGMTMVVVTHEMG----FarevaDRVVFMDGGRIVEEGPPEE 222
|
...
gi 489955000 559 LLA 561
Cdd:COG1126 223 FFE 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
339-553 |
3.62e-39 |
|
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: 142.61 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYD--KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAalrktV 416
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHLFS-ATLRDNLLLA------APDASDDTLRAMLEQVGLhklleDDGLNSWlgegGRQLSGGELRRLAIARAL 489
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGL-----SGFENAY----PHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVnF--DQIIVMDN--GHIIEQ 553
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDEAV-FlaDRVVVLSArpGRIVAE 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
236-562 |
6.19e-39 |
|
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: 150.28 E-value: 6.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 236 AQRRQSELTAFSQALMMLIGgiavIAMLwmasgGVG------GNAQPGPLIAlfvfCALAAFEALAPV---TGAFQHLGQ 306
Cdd:COG4618 234 ASDRAGGFSALSKFLRLLLQ----SAVL-----GLGaylviqGEITPGAMIA----ASILMGRALAPIeqaIGGWKQFVS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 307 VIASALRITDIAEQEPEvkfSAGQTAVPE-QVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQL 385
Cdd:COG4618 301 ARQAYRRLNELLAAVPA---EPERMPLPRpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 386 LTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLllaA--PDASDDTLRAMLEQVGLHKLLED-- 461
Cdd:COG4618 378 LVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI---ArfGDADPEKVVAAAKLAGVHEMILRlp 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 462 DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLVNFD 540
Cdd:COG4618 455 DGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVD 534
|
330 340
....*....|....*....|..
gi 489955000 541 QIIVMDNGHIIEQGSHAELLAK 562
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLAR 556
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
339-558 |
1.01e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE---AALRKT 415
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQRVHLFSA-TLRDNLLLA------APDASDDTLRAMLEQVGLhklleddglnswlgeGGR------QLSGGELRR 482
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGL---------------SDKakalphELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 483 LAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLrGLVN-FDQ-IIVMDNGHIIEQGSHAE 558
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDL-ELVDrMPKrVLELEDGRLVRDEARGV 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
339-550 |
1.01e-38 |
|
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: 140.04 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLllaapdasddtlramleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLHDAPLMLL 498
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489955000 499 DEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLVNFDQIIVMDNGHI 550
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-502 |
1.67e-38 |
|
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: 138.55 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSA-TLRDNL 434
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 435 LLAAP------DASDDTLRAMLEQVGLhklleDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPT 502
Cdd:pfam00005 81 RLGLLlkglskREKDARAEEALEKLGL-----GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-554 |
3.32e-38 |
|
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: 139.98 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFseaalRKTVSVVP 420
Cdd:cd03235 2 VEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 421 QRVHL---FSATLRD----------NLLLAAPDASDDTLRAMLEQVGLHKLLeddglNSWLGEggrqLSGGELRRLAIAR 487
Cdd:cd03235 75 QRRSIdrdFPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELA-----DRQIGE----LSGGQQQRVLLAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 488 ALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLrGLV--NFDQIIVMdNGHIIEQG 554
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDL-GLVleYFDRVLLL-NRTVVASG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
339-562 |
4.38e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 143.29 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNV--TFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL---R 413
Cdd:COG1135 2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFSA-TLRDN----LLLAAPDASDDTLRA--MLEQVGLhklleDDGLNSWLgeggRQLSGGELRRLAIA 486
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpLEIAGVPKAEIRKRVaeLLELVGL-----SDKADAYP----SQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH------RLrglvnFDQIIVMDNGHIIEQGSHAE 558
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHemdvvrRI-----CDRVAVLENGRIVEQGPVLD 227
|
....
gi 489955000 559 LLAK 562
Cdd:COG1135 228 VFAN 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
339-550 |
2.69e-37 |
|
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: 135.99 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKtVSV 418
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSA-TLRDNLllaapdasddtlramleqvglhklleddglnswlgeggrQLSGGELRRLAIARALLHDAPLML 497
Cdd:cd03230 78 LPEEPSLYENlTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 498 LDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVN-FDQIIVMDNGHI 550
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
341-563 |
1.14e-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: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA---ALRKTVS 417
Cdd:cd03261 3 LRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSA-TLRDNL---LLAAPDASDDTLRAM----LEQVGLHklledDGLNSWLGEggrqLSGGELRRLAIARAL 489
Cdd:cd03261 81 MLFQSGALFDSlTVFENVafpLREHTRLSEEEIREIvlekLEAVGLR-----GAEDLYPAE----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANV--MKGKTVLMVTH---RLRGLVnfDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHdldTAFAIA--DRIAVLYDGKIVAEGTPEELRASD 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
343-561 |
1.98e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 138.26 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ---QGEIRFNDVPLSGFSEAALR----KT 415
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQ----------RV-HLFSATLRDNLLLAAPDAsDDTLRAMLEQVGL-----------Hklleddglnswlgeggr 473
Cdd:COG0444 88 IQMIFQdpmtslnpvmTVgDQIAEPLRIHGGLSKAEA-RERAIELLERVGLpdperrldrypH----------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 474 QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrGLVNF--DQIIVMDNGH 549
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDL-GVVAEiaDRVAVMYAGR 228
|
250
....*....|..
gi 489955000 550 IIEQGSHAELLA 561
Cdd:COG0444 229 IVEEGPVEELFE 240
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
117-567 |
2.28e-36 |
|
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: 145.47 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 117 GELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVvTLGLSFLDVPIALtlggimlmtlIILPPL---------FYRAgkt 187
Cdd:TIGR00957 1062 GNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIG-ALIVILLATPIAA----------VIIPPLgllyffvqrFYVA--- 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 188 TGENLTRLRGEYRQQLTAWLQGqaelTLFGAS-----KRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAM 262
Cdd:TIGR00957 1128 SSRQLKRLESVSRSPVYSHFNE----TLLGVSvirafEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 263 LWMASGGVGGNAQPGP-LIALFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAEQEPEVKFSAGQTAVPE----QV 337
Cdd:TIGR00957 1204 LFAALFAVISRHSLSAgLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSgwppRG 1283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSATLRDNLllaAP--DASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSAlpDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYY 567
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
339-561 |
8.76e-36 |
|
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: 133.33 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKqAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGF-SEAALRKTVS 417
Cdd:cd03224 1 LEVENLNAGYGK-SQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLF-SATLRDNLLLAAPDASDDTLRAMLEQV-GLHKLLEDDglnswLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGAYARRRAKRKARLERVyELFPRLKER-----RKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-562 |
9.61e-36 |
|
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: 133.86 E-value: 9.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVT--FAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL---R 413
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFSA-TLRDN----LLLAAPDASDDTLRA--MLEQVGLhklleDDGLNSWLGeggrQLSGGELRRLAIA 486
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVleLLELVGL-----EDKADAYPA----QLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRL---RGLVnfDQIIVMDNGHIIEQGSHAELLA 561
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMevvKRIC--DRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 489955000 562 K 562
Cdd:cd03258 231 N 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-563 |
1.39e-35 |
|
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: 133.58 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFS-ATLRDNL-----LLAAPDASDDTlRA--MLEQVGLhklleddGLNSWLGEGGRQLSGGELRRLAIARALL 490
Cdd:cd03295 80 VIQQIGLFPhMTVEENIalvpkLLKWPKEKIRE-RAdeLLALVGL-------DPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 491 HDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRL-RGLVNFDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
338-559 |
3.07e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.87 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRK--- 414
Cdd:COG3638 2 MLELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQRVHLFS-ATLRDNLLLAA-PDAS-----------DDTLRAM--LEQVGL-HKLLEddglnswlgeggR--QLS 476
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRlGRTStwrsllglfppEDRERALeaLERVGLaDKAYQ------------RadQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 477 GGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLL--ANVMKGKTVLMVTHRLR-GLVNFDQIIVMDNGHIIEQ 553
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDlARRYADRIIGLRDGRVVFD 228
|
....*.
gi 489955000 554 GSHAEL 559
Cdd:COG3638 229 GPPAEL 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-551 |
8.33e-35 |
|
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: 130.45 E-value: 8.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNVTFAYDKQaQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPlsgFSEAALRKTVSVV 419
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQRV--HLFSATLRDNLLLAAPDASDDTLRA--MLEQVGLHKLLEDDGLNswlgeggrqLSGGELRRLAIARALLHDAPL 495
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGNEQAetVLKDLDLYALKERHPLS---------LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 496 MLLDEPTEGLDATTesqiLDLLANVMK-----GKTVLMVTHRLRGLVNF-DQIIVMDNGHII 551
Cdd:cd03226 148 LIFDEPTSGLDYKN----MERVGELIRelaaqGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-555 |
8.49e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 130.76 E-value: 8.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD-----PQQGEIRFN--DVPLSGFSEAA 411
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQRVHLFSATLRDNLLLAAP-------DASDDTLRAMLEQVGLHKLLEDDglnswlgEGGRQLSGGELRRLA 484
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDR-------LHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTH------RLRglvnfDQIIVMDNGHIIEQGS 555
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRVA-----DRTAFLLNGRLVEFGP 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
109-568 |
1.95e-34 |
|
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: 139.66 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 109 AGLARFRQGELLNRVVADVDTLDHL-------YLRVISPMVGAFVVIVVVTLGLSFLDVPIALTLggimlmtlIILPPLF 181
Cdd:TIGR01271 974 AVLNTMKAGRILNRFTKDMAIIDDMlpltlfdFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIF--------IMLRAYF 1045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 182 YRagktTGENLTRLRGEYRQ----QLTAWLQGQAELTLFGaSKRYRARMENTELNWHEAQ--RRQSELTAFsQALMMLIG 255
Cdd:TIGR01271 1046 LR----TSQQLKQLESEARSpifsHLITSLKGLWTIRAFG-RQSYFETLFHKALNLHTANwfLYLSTLRWF-QMRIDIIF 1119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 256 GIAVIAMLWMASGGVG-GNAQPGPLIALfVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAEQEPEVKFSAG----- 329
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQdGEGEVGIILTL-AMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGkyqls 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 330 ----------QTAVPEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDpQQGEIRF 399
Cdd:TIGR01271 1199 tvlvienphaQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI 1277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 400 NDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLllaAPDA--SDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQL 475
Cdd:TIGR01271 1278 DGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQfpDKLDFVLVDGGYVL 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 476 SGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGS 555
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
490
....*....|...
gi 489955000 556 HAELLAKQGRYYQ 568
Cdd:TIGR01271 1435 IQKLLNETSLFKQ 1447
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
339-561 |
1.98e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 130.26 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNAlediTLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfSEAALRKtVSV 418
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSA-TLRDNLLLA-----APDASD-DTLRAMLEQVGLHKLLEddglnswlgeggR---QLSGGELRRLAIARA 488
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLD------------RlpgQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
339-554 |
2.19e-34 |
|
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: 129.18 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfsEAALRKTVSV 418
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLF-SATLRDNLLLA------APDASDDTLRAMLEQVGLhklleDDGLNSWLgeggRQLSGGELRRLAIARALLH 491
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGlklrgvPKAEIRARVRELLELVGL-----EGLLNRYP----HELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
339-550 |
3.52e-34 |
|
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: 128.80 E-value: 3.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA--LRKTV 416
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHLFS-ATLRDNLLLA-------APDASDDTLRAMLEQVGLhklleDDGLNSWlgegGRQLSGGELRRLAIARA 488
Cdd:cd03262 79 GMVFQQFNLFPhLTVLENITLApikvkgmSKAEAEERALELLEKVGL-----ADKADAY----PAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRlrglVNF-----DQIIVMDNGHI 550
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
339-547 |
1.12e-33 |
|
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: 127.21 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgFSEAALRKTVSV 418
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSA-TLRDNLLLAA----PDASDDTLRAMLEQVGLHKLLEDDGlnswlgeggRQLSGGELRRLAIARALLHDA 493
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV---------RQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLAN-VMKGKTVLMVTHRLRGLvNFDQIIVMDN 547
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLEL-AAARVLDLGD 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-561 |
2.77e-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: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKTVS 417
Cdd:COG0410 4 LEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSA-TLRDNLLLAAPDASD-DTLRAMLEQV-GLHKLLEDDglnswLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDrAEVRADLERVyELFPRLKER-----RRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 495 LMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNReGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
232-548 |
1.39e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 131.85 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 232 NWHEAQRRQSELTAFSQALMMLIggiAVIAMLWMASGGVGGNAQPGPLIAlfvfcALAAF----EALAPVTGAFQHLGQV 307
Cdd:COG4178 257 NWRRLIRRQRNLTFFTTGYGQLA---VIFPILVAAPRYFAGEITLGGLMQ-----AASAFgqvqGALSWFVDNYQSLAEW 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 308 IASALRIT---DIAEQEPEVKFSAGQTAVPEQVALTLSNVTFA-YDKQAQnaLEDITLSVDAGQRIAILGRTGCGKSTLL 383
Cdd:COG4178 329 RATVDRLAgfeEALEAADALPEAASRIETSEDGALALEDLTLRtPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 384 QLLTRAWDPQQGEIRFNDvplsgfseaalRKTVSVVPQRVHLFSATLRDNLL--LAAPDASDDTLRAMLEQVGLHKLLE- 460
Cdd:COG4178 407 RAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAEr 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 461 -DDGLNsWlgegGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNF 539
Cdd:COG4178 476 lDEEAD-W----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFH 550
|
....*....
gi 489955000 540 DQIIVMDNG 548
Cdd:COG4178 551 DRVLELTGD 559
|
|
| 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 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLS--GFSEAALRKTV 416
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHLFS-ATLRDNLLLAapdasddtlramleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLHDAPL 495
Cdd:cd03229 79 GMVFQDFALFPhLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANV--MKGKTVLMVTHRLRGLVNF-DQIIVMDNGH 549
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
355-561 |
4.84e-32 |
|
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: 123.70 E-value: 4.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL-RKTVSVVPQRVHLFSA-TLRD 432
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAP----------------DASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:cd03219 95 NVMVAAQartgsglllararreeREARERAEELLERVGLADLAD---------RPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 497 LLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-568 |
8.26e-32 |
|
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: 124.20 E-value: 8.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDpQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLllaAPDA--SDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 495 LMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQ 568
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
336-560 |
2.57e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.41 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 336 QVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKT 415
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQRV--HLFSATLRDNLLLA------APDASDDTLRAMLEQVGLHKLLEDDGLNswlgeggrqLSGGELRRLAIAR 487
Cdd:PRK13632 85 IGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN---------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 488 ALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELL 560
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
338-569 |
3.09e-31 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 129.68 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIrfndvplsgfseaALRKTVS 417
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSATLRDNLLLAAPdASDDTLRAMLEQVGLHKLLE--DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKA-LNEKYYQQVLEACALLPDLEilPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADI 781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 496 MLLDEPTEGLDATTESQILDLL---ANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQGRYYQF 569
Cdd:TIGR00957 782 YLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
77-568 |
4.54e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 129.33 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 77 RYFERLVShdATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVvvTLGLS 156
Cdd:PLN03232 360 QYFQNVGR--VGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIV--SMVLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 157 FLDVPIALTLGGIMLMTLIILPPLFY-RAGKTTGENLTRLrgEYRQQLT-AWLQGQAELTLFGASKRYRARME---NTEL 231
Cdd:PLN03232 436 YQQLGVASLFGSLILFLLIPLQTLIVrKMRKLTKEGLQWT--DKRVGIInEILASMDTVKCYAWEKSFESRIQgirNEEL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 232 NWHeaqRRQSELTAFSQalmMLIGGIAVIAMLwmASGGV----GGNAQPGPlialfVFCALAAFEAL-APVTGAFQHLGQ 306
Cdd:PLN03232 514 SWF---RKAQLLSAFNS---FILNSIPVVVTL--VSFGVfvllGGDLTPAR-----AFTSLSLFAVLrSPLNMLPNLLSQ 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 307 VIASALRITDIAEQ--EPEVKFSAGQTAVPEQVALTLSNVTFAYDKQAQN-ALEDITLSVDAGQRIAILGRTGCGKSTLL 383
Cdd:PLN03232 581 VVNANVSLQRIEELllSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLI 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 384 QLLtrawdpqqgeirFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLEDDG 463
Cdd:PLN03232 661 SAM------------LGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPG 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 464 LN-SWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILD-LLANVMKGKTVLMVTHRLRGLVNFDQ 541
Cdd:PLN03232 729 RDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTNQLHFLPLMDR 808
|
490 500
....*....|....*....|....*..
gi 489955000 542 IIVMDNGHIIEQGSHAElLAKQGRYYQ 568
Cdd:PLN03232 809 IILVSEGMIKEEGTFAE-LSKSGSLFK 834
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
337-554 |
4.78e-31 |
|
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: 119.58 E-value: 4.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVTFAYDKQAQNA----LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT--RAWDPQQGEIRFNDVPLSgfsEA 410
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 ALRKTVSVVPQRVHLFSA-TLRDNLLLAApdasddtlramleqvglhKLleddglnswlgeggRQLSGGELRRLAIARAL 489
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTlTVRETLMFAA------------------KL--------------RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLV--NFDQIIVMDNGHIIEQG 554
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
336-560 |
6.29e-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: 120.96 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 336 QVALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTrAWDPQ--QGEIRFNDVPLSGFSEAALR 413
Cdd:COG1119 1 DPLLELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT-GDLPPtyGNDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLF---SATLRDNLLLAA---------PDASDDTL-RAMLEQVGLHKLLEDdglnSWlgeggRQLSGGEL 480
Cdd:COG1119 78 KRIGLVSPALQLRfprDETVLDVVLSGFfdsiglyrePTDEQRERaRELLELLGLAHLADR----PF-----GTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLR-GLVNFDQIIVMDNGHIIEQGSHA 557
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKE 228
|
...
gi 489955000 558 ELL 560
Cdd:COG1119 229 EVL 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-559 |
9.90e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.90 E-value: 9.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 335 EQVALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLtrA--WDPQQGEIRFNDVPLSGfSEAAL 412
Cdd:COG3842 2 AMPALELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI--AgfETPDSGRILLDGRDVTG-LPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 RKtVSVVPQRV----HLfsaTLRDN------LLLAAPDASDDTLRAMLEQVGLhklledDGLnswlgeGGR---QLSGGE 479
Cdd:COG3842 77 RN-VGMVFQDYalfpHL---TVAENvafglrMRGVPKAEIRARVAELLELVGL------EGL------ADRyphQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 480 LRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHrlrglvnfDQ---------IIVMDNG 548
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTH--------DQeealaladrIAVMNDG 212
|
250
....*....|.
gi 489955000 549 HIIEQGSHAEL 559
Cdd:COG3842 213 RIEQVGTPEEI 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
332-552 |
1.10e-30 |
|
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: 119.85 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 332 AVPEQVALTLSNVTFAYDKQAQ--NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE 409
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 410 ---AALR-KTVSVVPQRVHLFSA-TLRDNLLLAAPDASDDTLR----AMLEQVGLHKLLeddglnswlGEGGRQLSGGEL 480
Cdd:COG4181 82 darARLRaRHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARararALLERVGLGHRL---------DHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLL--ANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIE 552
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
311-552 |
3.26e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.41 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 311 ALRITDIAEQEPEVKFSAGQTAVPEQVALTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAW 390
Cdd:COG0488 288 KLEREEPPRRDKTVEIRFPPPERLGKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 391 DPQQGEIRFNdvplsgfseaalrKTVSV--VPQRVHLF--SATLRDNLLLAAPDASDDTLRAMLEQVGLHklleddglns 466
Cdd:COG0488 366 EPDSGTVKLG-------------ETVKIgyFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGRFLFS---------- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 467 wlgeGGRQ------LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANvMKGkTVLMVTH-R--LRGLV 537
Cdd:COG0488 423 ----GDDAfkpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRVA 496
|
250
....*....|....*
gi 489955000 538 nfDQIIVMDNGHIIE 552
Cdd:COG0488 497 --TRILEFEDGGVRE 509
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
351-561 |
4.00e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.02 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 351 QAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA---ALRKTVSVVPQRV---- 423
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 424 ---HLFSATLRD---NLLLAAPDASDDTLRAMLEQVGLhklleDDGLNSWLGEggrQLSGGELRRLAIARALLHDAPLML 497
Cdd:PRK10419 103 nprKTVREIIREplrHLLSLDKAERLARASEMLRAVDL-----DDSVLDKRPP---QLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 498 LDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNFDQ-IIVMDNGHIIEQGSHAELLA 561
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQrVMVMDNGQIVETQPVGDKLT 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
334-564 |
4.41e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 126.24 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALR 413
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFSATLRDNLllaAP--DASDDTLRAMLEQVGLHKLLEDD--GLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PLN03232 1310 RVLSIIPQSPVLFSGTVRFNI---DPfsEHNDADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQG 564
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
339-562 |
6.26e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 119.35 E-value: 6.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQ---AQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA----A 411
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQ--RVHLFSAT-LRD------NLLLAAPDAsDDTLRAMLEQVGL-HKLLEDDGLnswlgeggrQLSGGELR 481
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETvEKDicfgpmNFGVSEEDA-KQKAREMIELVGLpEELLARSPF---------ELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 482 RLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVM--KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAE 558
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPRE 232
|
....
gi 489955000 559 LLAK 562
Cdd:PRK13634 233 IFAD 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
355-561 |
2.55e-29 |
|
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: 116.68 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL-RKTVSVVPQRVHLFSA-TLRD 432
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAA--------------PDASDDTLRAMLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLL 498
Cdd:COG0411 99 NVLVAAharlgrgllaallrLPRARREEREARERA--EELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 499 DEPTEGLDAtTESQ-ILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG0411 177 DEPAAGLNP-EETEeLAELIRRLRDerGITILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-559 |
3.51e-29 |
|
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: 115.74 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL---RKT 415
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQRVHLFS-ATLRDNLLLAAPdASDDTLRAMLEQVGLH------KLLEDDGLNSWLGEGGRQLSGGELRRLAIARA 488
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRL-GRRSTWRSLFGLFPKEekqralAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLL--ANVMKGKTVLMVTHRLR-GLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
339-561 |
6.34e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.68 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNaledITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAalRKTVSV 418
Cdd:PRK10771 2 LKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFS-ATLRDNLLLA-AP-----DASDDTLRAMLEQVGLHKLLEDdgLNSwlgeggrQLSGGELRRLAIARALLH 491
Cdd:PRK10771 76 LFQENNLFShLTVAQNIGLGlNPglklnAAQREKLHAIARQMGIEDLLAR--LPG-------QLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVMKGK--TVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
339-554 |
6.47e-29 |
|
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: 114.21 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQaqNALEDITLSVDAGQrIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfSEAALRKTVSV 418
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSA-TLRDNL--LLAAPDASDDTLRAMLEQVglhklLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:cd03264 77 LPQEFGVYPNfTVREFLdyIAWLKGIPSKEVKARVDEV-----LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
355-550 |
7.55e-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: 114.04 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA---LRKTVSVVPQRVHLFSA-TL 430
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLPDrNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 RDNLLLA------APDASDDTLRAMLEQVGL-HKllEDDGLNswlgeggrQLSGGELRRLAIARALLHDAPLMLLDEPTE 503
Cdd:cd03292 96 YENVAFAlevtgvPPREIRKRVPAALELVGLsHK--HRALPA--------ELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489955000 504 GLDATTESQILDLLANVMK-GKTVLMVTHRlRGLVNFDQ--IIVMDNGHI 550
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKaGTTVVVATHA-KELVDTTRhrVIALERGKL 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
350-560 |
1.17e-28 |
|
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: 114.90 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 350 KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLS---GFSEAALRKTVSVVPQ-RVHL 425
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRKQRRAFRRDVQLVFQdSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 426 FSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLEDDGLNS-WLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEG 504
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 505 LDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL 560
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLL 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-564 |
1.30e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.77 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALR 413
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFSATLRDNLllaAP--DASDDTLRAMLEQVGLHKLLEDD--GLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNL---DPfnEHNDADLWESLERAHLKDVIRRNslGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQG 564
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
339-560 |
1.87e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.96 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:PRK11231 3 LRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQrVHLfsatlrdnlllaAPdasddtlramlEQVGLHKLLEdDGLNSWLGEGGR------------------------- 473
Cdd:PRK11231 81 LPQ-HHL------------TP-----------EGITVRELVA-YGRSPWLSLWGRlsaednarvnqameqtrinhladrr 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 474 --QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLVNF-DQIIVMDNGH 549
Cdd:PRK11231 136 ltDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYcDHLVVLANGH 215
|
250
....*....|.
gi 489955000 550 IIEQGSHAELL 560
Cdd:PRK11231 216 VMAQGTPEEVM 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-561 |
1.38e-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: 116.71 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTL----LQLLtrawdPQQGEIRFNDVPLSGFSEAA---LRKTVSVVPQ------ 421
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 422 ----RVhlfSATLRDNLLLAAPDASDDTLRA----MLEQVGlhklLEDDGLNSWLGEggrqLSGGELRRLAIARALLHDA 493
Cdd:COG4172 376 sprmTV---GQIIAEGLRVHGPGLSAAERRArvaeALEEVG----LDPAARHRYPHE----FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRgLVNF--DQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
330-554 |
1.79e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 330 QTAVPEQVALTLSNVTFAY-DKQAqnaLEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD--PQQ---GEIRFNDVP 403
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYgDKQA---LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 404 LSGFSE--AALRKTVSVVPQRVHLFSATLRDNLLLAAPDAS-------DDTLRAMLEQVGLHKLLEDDglnswLGEGGRQ 474
Cdd:COG1117 80 IYDPDVdvVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGikskselDEIVEESLRKAALWDEVKDR-----LKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 475 LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANvMKGK-TVLMVTHRL----RglVNfDQIIVMDNGH 549
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDyTIVIVTHNMqqaaR--VS-DYTAFFYLGE 230
|
....*
gi 489955000 550 IIEQG 554
Cdd:COG1117 231 LVEFG 235
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
338-559 |
2.53e-27 |
|
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: 110.46 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD-----PQQGEIRFN--DVPLSGFSEA 410
Cdd:TIGR00972 1 AIEIENLNLFYGEK--EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDgqDIYDKKIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 ALRKTVSVVPQRVHLFSATLRDNLLLAaPDAS--------DDTLRAMLEQVGLHKLLEDDglnswLGEGGRQLSGGELRR 482
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFPMSIYDNIAYG-PRLHgikdkkelDEIVEESLKKAALWDEVKDR-----LHDSALGLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 483 LAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAEL 559
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFYDGELVEYGPTEQI 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-554 |
3.11e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 109.50 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQnaleDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLsGFSEAAlRKTVSV 418
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPA-DRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFS-ATLRDNLLLAApdasDDTLRAMLEQVG-LHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:cd03298 75 LFQENNLFAhLTVEQNVGLGL----SPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 497 LLDEPTEGLDATTESQILDLLANV--MKGKTVLMVTHRLRGLVN-FDQIIVMDNGHIIEQG 554
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
356-559 |
4.35e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.80 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLl 435
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 436 laAP--DASDDTLRAMLEQVGL--HKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALL-HDAPLMLLDEPTEGLDATTE 510
Cdd:PTZ00243 1405 --DPflEASSAEVWAALELVGLreRVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALD 1482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489955000 511 SQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:PTZ00243 1483 RQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-559 |
7.82e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 108.36 E-value: 7.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNdvplsGFS----EAALRK 414
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-----GYSirtdRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQRVHLFSA-TLRDNLLLAAPdasddtLRAMLE---QVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALL 490
Cdd:cd03263 76 SLGYCPQFDALFDElTVREHLRFYAR------LKGLPKseiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 491 HDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRgLVNF--DQIIVMDNGHIIEQGSHAEL 559
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMD-EAEAlcDRIAIMSDGKLRCIGSPQEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
337-560 |
1.05e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.09 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTV 416
Cdd:PRK13548 1 AMLEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHL-FSATLRDNLLL------AAPDASDDTLRAMLEQVGLHKLleddglnswlgeGGR---QLSGGELRRLAIA 486
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHL------------AGRdypQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 487 RALL------HDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrglvNF-----DQIIVMDNGHIIEQ 553
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDL----NLaaryaDRIVLLHQGRLVAD 222
|
....*..
gi 489955000 554 GSHAELL 560
Cdd:PRK13548 223 GTPAEVL 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
339-565 |
1.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQA---QNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE----AA 411
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQ--RVHLFSATLRDNLLLAAPDASDDtlramLEQVG--LHKLLEDDGLN-SWLGEGGRQLSGGELRRLAIA 486
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-----LDEVKnyAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANVM--KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKDK 237
|
..
gi 489955000 564 GR 565
Cdd:PRK13646 238 KK 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
343-561 |
1.55e-26 |
|
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: 113.63 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKS----TLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRK---- 414
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQR-------VHL----FSATLRDNLLLAAPDASDDTLrAMLEQVGL-----------Hklleddglnswlgegg 472
Cdd:COG4172 93 RIAMIFQEpmtslnpLHTigkqIAEVLRLHRGLSGAAARARAL-ELLERVGIpdperrldaypH---------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 473 rQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrGLV-NF-DQIIVMDNG 548
Cdd:COG4172 156 -QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDL-GVVrRFaDRVAVMRQG 233
|
250
....*....|...
gi 489955000 549 HIIEQGSHAELLA 561
Cdd:COG4172 234 EIVEQGPTAELFA 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-561 |
1.78e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 115.22 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQA-QNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTrawdpqqGEIrfndVPLSGfSEAAL 412
Cdd:PLN03130 610 PGLPAISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GEL----PPRSD-ASVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 RKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAmLEQVGLHKLLE--DDGLNSWLGEGGRQLSGGELRRLAIARALL 490
Cdd:PLN03130 678 RGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERA-IDVTALQHDLDllPGGDLTEIGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 491 HDAPLMLLDEPTEGLDATTESQILD-LLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVFDkCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
343-558 |
1.88e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQ---AQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLS--GFSEAALRKTVS 417
Cdd:PRK13637 7 NLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQ--RVHLFSATL-RD------NLLLAAPDASDDTLRAMlEQVGLHKlleddglNSWLGEGGRQLSGGELRRLAIARA 488
Cdd:PRK13637 87 LVFQypEYQLFEETIeKDiafgpiNLGLSEEEIENRVKRAM-NIVGLDY-------EDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGK--TVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAE 558
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
356-562 |
1.98e-26 |
|
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: 107.81 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAalRKTVSVVPQRVHLF-SATLRDNL 434
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 435 -----LLAAPDASDDtlramlEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATT 509
Cdd:cd03299 93 ayglkKRKVDKKEIE------RKV--LEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 510 ESQILDLLANVMK--GKTVLMVTHRL-RGLVNFDQIIVMDNGHIIEQGSHAELLAK 562
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
338-559 |
2.02e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.55 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQL---LTrawDPQQGEIRFNDVPLSGFsEAALRK 414
Cdd:COG3839 3 SLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagLE---DPTSGEILIGGRDVTDL-PPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 tVSVVPQRVHLF-SATLRDNLLLA------APDASDDTLRAMLEQVGLHKLLEddglnswlgeggR---QLSGGELRRLA 484
Cdd:COG3839 77 -IAMVFQSYALYpHMTVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLD------------RkpkQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDA----TTESQILDLLANVmkGKTVLMVTHrlrglvnfDQ---------IIVMDNGHII 551
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTH--------DQveamtladrIAVMNDGRIQ 213
|
....*...
gi 489955000 552 EQGSHAEL 559
Cdd:COG3839 214 QVGTPEEL 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
357-561 |
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 489955000 357 EDITLSVDAGQRIAILGRTGCGKS----TLLQLLTRAWDPQQGEIRFNDVPLSGfseAALR-KTVSVVPQR-------VH 424
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRgRKIATIMQNprsafnpLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 425 LFSATLRDNLLLAAPDASDDTLRAMLEQVGLhkllEDDGlnSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEG 504
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAALEAVGL----ENAA--RVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 505 LDATTESQILDLLANVM--KGKTVLMVTHRLrGLVN--FDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK10418 171 LDVVAQARILDLLESIVqkRALGMLLVTHDM-GVVArlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-560 |
4.04e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.28 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQ---AQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE----AA 411
Cdd:PRK13643 2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQ--RVHLFSATLRDNLLLA------APDASDDTLRAMLEQVGLHKlleddglnSWLGEGGRQLSGGELRRL 483
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqnfgiPKEKAEKIAAEKLEMVGLAD--------EFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 484 AIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL 560
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDVF 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
338-531 |
6.50e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDK--QAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSeaALRkt 415
Cdd:COG4525 3 MLTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 vSVVPQRVHLFS-ATLRDN----LLLAAPDASDDTLRA--MLEQVGLHKLLEDdglNSWlgeggrQLSGGELRRLAIARA 488
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNvafgLRLRGVPKAERRARAeeLLALVGLADFARR---RIW------QLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH 531
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
340-562 |
9.47e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 9.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNV--TFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKT-- 415
Cdd:PRK11153 3 ELKNIskVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 -VSVVPQRVHLFSA-TLRDN----LLLAAPDASDDTLR--AMLEQVGLhklleDDGLNSWLGeggrQLSGGELRRLAIAR 487
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNvalpLELAGTPKAEIKARvtELLELVGL-----SDKADRYPA----QLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 488 ALLHDAPLMLLDEPTEGLD-ATTESqILDLLANVMK--GKTVLMVTHRL---RGLVnfDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDpATTRS-ILELLKDINRelGLTIVLITHEMdvvKRIC--DRVAVIDAGRLVEQGTVSEVFS 230
|
.
gi 489955000 562 K 562
Cdd:PRK11153 231 H 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
338-573 |
1.19e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEI-----RFNdvplsgFSEA-- 410
Cdd:PRK11124 2 SIQLNGINCFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFD------FSKTps 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 -----ALRKTVSVVPQRVHLFS-ATLRDNLLlAAP------DASDDTLRAMleqvglhKLLEDDGLNSWLGEGGRQLSGG 478
Cdd:PRK11124 74 dkairELRRNVGMVFQQYNLWPhLTVQQNLI-EAPcrvlglSKDQALARAE-------KLLERLRLKPYADRFPLHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 479 ELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRlrglVNF-----DQIIVMDNGHIIE 552
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHE----VEVarktaSRVVYMENGHIVE 221
|
250 260
....*....|....*....|.
gi 489955000 553 QGSHAELLAKQGRyyQFKQRL 573
Cdd:PRK11124 222 QGDASCFTQPQTE--AFKNYL 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-563 |
1.24e-25 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 112.31 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFndvplSGfseaalrkTVSVVPQRVHLFSATLRDNLL 435
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH-----SG--------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 436 LAApdaSDDTLR-------AMLEQvGLHKLLEDDglNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDAT 508
Cdd:TIGR01271 509 FGL---SYDEYRytsvikaCQLEE-DIALFPEKD--KTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 509 TESQILD-LLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:TIGR01271 583 TEKEIFEsCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
339-563 |
1.43e-25 |
|
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: 105.76 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLllaAPD--ASDDTLRAMLEQVGLHKLLED--DGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:cd03288 100 ILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 495 LMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
339-559 |
2.18e-25 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 104.63 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFseAALRKTVSV 418
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFS-ATLRDN----LLLAAPDASDDTLRA--MLEQVGLhklleddglnswLGEGGR---QLSGGELRRLAIARA 488
Cdd:cd03300 77 VFQNYALFPhLTVFENiafgLRLKKLPKAEIKERVaeALDLVQL------------EGYANRkpsQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-552 |
2.25e-25 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 110.27 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 10 LYKRHKWMLTLGIVLAIVTLLASIGLLtlsgWFLSASAAAGFAGLYSFNYMLPAAGVRGTAITRTAGRYFERLvSHDATF 89
Cdd:COG4615 7 LLRESRWLLLLALLLGLLSGLANAGLI----ALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRL-GQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 90 RvlqhLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRvISPMVGAFVVIVVVTLGLSFLDVPIALtlggI 169
Cdd:COG4615 82 R----LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFL----L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 170 MLMTLIILPPLFYRAGKTTGENLTRLR---GEYRQQLTAWLQGQAELTLfgaSKRYRARMENTELNWHEAQRRQSELTAF 246
Cdd:COG4615 153 TLVLLGLGVAGYRLLVRRARRHLRRAReaeDRLFKHFRALLEGFKELKL---NRRRRRAFFDEDLQPTAERYRDLRIRAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 247 SQAL-------MMLIGGIAVIamLWMAsggVGGNAQPGPLIALFVFCALAAFEALAPVTGAFQHLGQVIASALRITDIAE 319
Cdd:COG4615 230 TIFAlannwgnLLFFALIGLI--LFLL---PALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 320 QEPEVKFSAGQTAVPEQVA----LTLSNVTFAYDKQAQN---ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDP 392
Cdd:COG4615 305 ALAAAEPAAADAAAPPAPAdfqtLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 393 QQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFsatlrDNLLLAAPDASDDTLRAMLEQVGL-HKL-LEDDGLNSwlge 470
Cdd:COG4615 385 ESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLERLELdHKVsVEDGRFST---- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 471 ggRQLSGGELRRLAIARALLHDAPLMLLDE------P-------TEgldattesqIL-DLLAnvmKGKTVLMVTH--RLR 534
Cdd:COG4615 456 --TDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPefrrvfyTE---------LLpELKA---RGKTVIAISHddRYF 521
|
570
....*....|....*...
gi 489955000 535 GLVnfDQIIVMDNGHIIE 552
Cdd:COG4615 522 DLA--DRVLKMDYGKLVE 537
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
356-554 |
2.55e-25 |
|
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: 104.28 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT---RAWDPQQGEIRFNDVPLSgfsEAALRKTVSVVPQRVHLFSA-TLR 431
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAA----PDASDDTLRAMLEQVGLHKLLEDDGLNSWLGEGgrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA 507
Cdd:cd03234 100 ETLTYTAilrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489955000 508 TTESQILDLLANVMK-GKTVLMVTHRLR-GLVN-FDQIIVMDNGHIIEQG 554
Cdd:cd03234 177 FTALNLVSTLSQLARrNRIVILTIHQPRsDLFRlFDRILLLSSGEIVYSG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-551 |
2.82e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.38 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDvplsgfseaalRKTVSVVP 420
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 421 QRVHLFS-ATLRDNL----------------LLAAPDASDDTLRAM------LEQVG-----------LHKL-LEDDGLN 465
Cdd:COG0488 68 QEPPLDDdLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLaelqeeFEALGgweaearaeeiLSGLgFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 466 SWLGEggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTesqiLDLLANVMKG--KTVLMVTH-R--LRGLVNfd 540
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNypGTVLVVSHdRyfLDRVAT-- 217
|
250
....*....|.
gi 489955000 541 QIIVMDNGHII 551
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
355-564 |
2.96e-25 |
|
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: 105.94 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN--DVplsgFSEAA-LRKTVSVVPQRVHLFSA-TL 430
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgyDV----VREPRkVRRSIGIVPQYASVDEDlTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 RDNLLLAAP--DASDDTLRAMLEQvglhkLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDAT 508
Cdd:TIGR01188 84 RENLEMMGRlyGLPKDEAEERAEE-----LLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 509 TESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQG 564
Cdd:TIGR01188 159 TRRAIWDYIRALKEeGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
355-562 |
3.39e-25 |
|
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: 105.03 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL----RKTVSVVPQRVHLF-SAT 429
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDN----LLLAAPDASDDTLRAM--LEQVGLHKlleddglnsWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTE 503
Cdd:cd03294 119 VLENvafgLEVQGVPRAEREERAAeaLELVGLEG---------WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 504 GLDAT----TESQILDLLANVmkGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:cd03294 190 ALDPLirreMQDELLRLQAEL--QKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
356-559 |
6.35e-25 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 104.55 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFndvplSGfseaalrkTVSVVPQRVHLFSATLRDNLL 435
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH-----SG--------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 436 LAApdaSDDTLR-------AMLEQvGLHKLLEDDglNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDAT 508
Cdd:cd03291 120 FGV---SYDEYRyksvvkaCQLEE-DITKFPEKD--NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489955000 509 TESQILD-LLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:cd03291 194 TEKEIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-561 |
1.12e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.94 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRV--HLFSATLRDNLLLAAPDAS---DDtlraMLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGLENIGvprEE----MVERV--DQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLA--NVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
339-550 |
1.34e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.22 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSG--------FSEA 410
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEaredtrlmFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 ALRKTVSVVpqrvhlfsatlrDNLLLA-APDASDDTLRAmLEQVGLhklleDDGLNSWLGeggrQLSGGELRRLAIARAL 489
Cdd:PRK11247 91 RLLPWKKVI------------DNVGLGlKGQWRDAALQA-LAAVGL-----ADRANEWPA----ALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHI 550
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
341-573 |
2.05e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgFSEA-------ALR 413
Cdd:COG4161 5 LKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD-FSQKpsekairLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFS-ATLRDNLLlAAP------DASDDTLRAM--LEQVGLhklleDDGLNSWlgegGRQLSGGELRRLA 484
Cdd:COG4161 82 QKVGMVFQQYNLWPhLTVMENLI-EAPckvlglSKEQAREKAMklLARLRL-----TDKADRF----PLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRlrglVNF-----DQIIVMDNGHIIEQGSHAE 558
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHE----VEFarkvaSQVVYMEKGRIIEQGDASH 227
|
250
....*....|....*
gi 489955000 559 LLAKQGRyyQFKQRL 573
Cdd:COG4161 228 FTQPQTE--AFAHYL 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
339-561 |
2.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQ---AQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF---NDVPLSGFSEA-- 410
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 -------------------ALRKTVSVVPQ--RVHLFSATLRDNLLLAA------PDASDDTLRAMLEQVGLHKlleddg 463
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPvsmgvsKEEAKKRAAKYIELVGLDE------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 464 lnSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQ 541
Cdd:PRK13651 157 --SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEWtKR 234
|
250 260
....*....|....*....|
gi 489955000 542 IIVMDNGHIIEQGSHAELLA 561
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-551 |
3.71e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKTVS 417
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQrvhlfsatlrdnlllaapdasddtlramleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLHDAPLML 497
Cdd:cd03216 79 MVYQ-----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 498 LDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHII 551
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
338-555 |
5.38e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.13 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYdkQAQN-----ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE--- 409
Cdd:PRK13649 2 GINLQNVSYTY--QAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 410 -AALRKTVSVVPQ--RVHLFSATLRDNLLLA------APDASDDTLRAMLEQVGLHKLLEDdglnswlgEGGRQLSGGEL 480
Cdd:PRK13649 80 iKQIRKKVGLVFQfpESQLFEETVLKDVAFGpqnfgvSQEEAEALAREKLALVGISESLFE--------KNPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGS 555
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
356-554 |
5.96e-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: 100.06 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVD---AGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfSEAAL-----RKTVSVVPQRVHLFS 427
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 428 -ATLRDNLLLAAPDASDDTLRAMLEQvglhkLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLD 506
Cdd:cd03297 89 hLNVRENLAFGLKRKRNREDRISVDE-----LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489955000 507 ATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
339-559 |
6.05e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 100.29 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKTVS 417
Cdd:TIGR03410 1 LEVSNLNVYYG-QSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSA-TLRDNLLLAApDASDDTLRAMLEQV-GLHKLLEDdglnsWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTGL-AALPRRSRKIPDEIyELFPVLKE-----MLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 496 MLLDEPTEGLDATTESQI---LDLLANvMKGKTVLMVTHRLrglvNF-----DQIIVMDNGHIIEQGSHAEL 559
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIgrvIRRLRA-EGGMAILLVEQYL----DFarelaDRYYVMERGRVVASGAGDEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
339-553 |
8.32e-24 |
|
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: 99.64 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF-----NDVPlsgfseaALR 413
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdvTDLP-------PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLF-SATLRDNLL--LAAPDASDDTLRAMLEQVGlhKLLEDDGLnswLGEGGRQLSGGELRRLAIARALL 490
Cdd:cd03301 72 RDIAMVFQNYALYpHMTVYDNIAfgLKLRKVPKDEIDERVREVA--ELLQIEHL---LDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 491 HDAPLMLLDEPTEGLDA----TTESQILDLLANVmkGKTVLMVTH-RLRGLVNFDQIIVMDNGhIIEQ 553
Cdd:cd03301 147 REPKVFLMDEPLSNLDAklrvQMRAELKRLQQRL--GTTTIYVTHdQVEAMTMADRIAVMNDG-QIQQ 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
339-549 |
1.80e-23 |
|
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: 96.36 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDvplsgfseaalRKTVSV 418
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQrvhlfsatlrdnlllaapdasddtlramleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLHDAPLMLL 498
Cdd:cd03221 68 FEQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 499 DEPTEGLDATTesqiLDLLANVMKG--KTVLMVTHRlRGLVN--FDQIIVMDNGH 549
Cdd:cd03221 95 DEPTNHLDLES----IEALEEALKEypGTVILVSHD-RYFLDqvATKIIELEDGK 144
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-559 |
2.06e-23 |
|
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: 98.60 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRfndvpLSGFS---EAA-LRKTVSVVPQRVHLFSA-T 429
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDvvrEPReVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDNLLLAAP------DASDDTLRAMLEQVGL----HKLLeddglnswlgeggRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:cd03265 90 GWENLYIHARlygvpgAERRERIDELLDFVGLleaaDRLV-------------KTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 500 EPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAEL 559
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
356-560 |
3.21e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSG--FSEAALRKTVSVVPQRVHLF-SATLRD 432
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLL-------AAPDASDDTLRAMLEQVGLhklleDDGLNSWLGEggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGL 505
Cdd:PRK09493 97 NVMFgplrvrgASKEEAEKQARELLAKVGL-----AERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 506 DATTESQILdllaNVMK-----GKTVLMVTHRlrglVNFDQ-----IIVMDNGHIIEQGSHAELL 560
Cdd:PRK09493 168 DPELRHEVL----KVMQdlaeeGMTMVIVTHE----IGFAEkvasrLIFIDKGRIAEDGDPQVLI 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
358-561 |
3.53e-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: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 358 DITLSVDAGQRIAILGRTGCGKSTLLQL---LTRawdPQQGEIRFNDVPLsgFSEAAL------RKTVSVVPQRVHLFS- 427
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVL--QDSARGiflpphRRRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 428 ATLRDNLLLAAPDASDDTLRAMLEQVglHKLLeddGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA 507
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEV--VELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 508 TTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG4148 167 ARKAEILPYLERLRDelDIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
355-531 |
3.86e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTrawdpqqGEIRfndvPLSGFSEAALRKTVSVVPQRVHL---FSATLR 431
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLA-------GVLR----PTSGTVRRAGGARVAYVPQRSEVpdsLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNL---------LLAAPDASD-DTLRAMLEQVGLHKLLeddglnswlgegGRQ---LSGGELRRLAIARALLHDAPLMLL 498
Cdd:NF040873 76 DLVamgrwarrgLWRRLTRDDrAAVDDALERVGLADLA------------GRQlgeLSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....
gi 489955000 499 DEPTEGLDATTESQILDLLAN-VMKGKTVLMVTH 531
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEeHARGATVVVVTH 177
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
338-531 |
3.88e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.00 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfsEAALRKTV- 416
Cdd:PRK11248 1 MLQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERGVVf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 ---SVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHklleddglnswlGEGGR---QLSGGELRRLAIARALL 490
Cdd:PRK11248 77 qneGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE------------GAEKRyiwQLSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489955000 491 HDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH 531
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
337-563 |
4.35e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.52 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVTFAYDK----QAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPL----SGFS 408
Cdd:PRK13641 1 MSIKFENVDYIYSPgtpmEKK-GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 409 EAALRKTVSVVPQ--RVHLFSATLRDNLLLAAPD--ASDDTLRAM----LEQVGLHKLLEDdglnswlgEGGRQLSGGEL 480
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKalkwLKKVGLSEDLIS--------KSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAE 558
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEYaDDVLVLEHGKLIKHASPKE 231
|
....*
gi 489955000 559 LLAKQ 563
Cdd:PRK13641 232 IFSDK 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
355-559 |
4.77e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 100.19 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL---RKTVSVVPQ---------- 421
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQdpyaslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 422 RVhlfSATLRDNLL---LAAPDASDDTLRAMLEQVGL---------HklleddglnswlgeggrQLSGGELRRLAIARAL 489
Cdd:COG4608 113 TV---GDIIAEPLRihgLASKAERRERVAELLELVGLrpehadrypH-----------------EFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQGSHAEL 559
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDL-SVVRHisDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
355-563 |
5.41e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPL--SGFSEAALRKTVSVVPQRV--HLFSATL 430
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPdnQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 RDnlllaapDASDDTLRAMLEQVGLHK----LLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLD 506
Cdd:PRK13636 101 YQ-------DVSFGAVNLKLPEDEVRKrvdnALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 507 ATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
357-568 |
9.24e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 103.57 E-value: 9.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 357 EDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD--------------------------------------------- 391
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 392 ---------PQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED- 461
Cdd:PTZ00265 1265 gsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESl 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 462 -DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVN 538
Cdd:PTZ00265 1345 pNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR 1424
|
250 260 270
....*....|....*....|....*....|....*
gi 489955000 539 FDQIIVMDN----GHIIE-QGSHAELLAKQGRYYQ 568
Cdd:PTZ00265 1425 SDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYK 1459
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
323-560 |
9.35e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 102.43 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 323 EVKFSAGQTAVPEQVALTLSNVtFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLT--RAWDPQ-QGEIRF 399
Cdd:TIGR00955 9 DVFGRVAQDGSWKQLVSRLRGC-FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrSPKGVKgSGSVLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 400 NDVPLsgfsEAALRKTVSVVPQRVHLF--SATLRDNLLLAA-----PDASDDTLRAMLEQVglhklLEDDGL----NSWL 468
Cdd:TIGR00955 88 NGMPI----DAKEMRAISAYVQQDDLFipTLTVREHLMFQAhlrmpRRVTKKEKRERVDEV-----LQALGLrkcaNTRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 469 GEGGRQ--LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTH----RLRGLvnFDQ 541
Cdd:TIGR00955 159 GVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHqpssELFEL--FDK 236
|
250
....*....|....*....
gi 489955000 542 IIVMDNGHIIEQGSHAELL 560
Cdd:TIGR00955 237 IILMAEGRVAYLGSPDQAV 255
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
353-569 |
1.31e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 353 QNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDV------PLSGFSEA--ALRKTVSVVPQRVH 424
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidtarSLSQQKGLirQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 425 LFS-ATLRDNLLlAAPDASDDTLRAMLEQVGlHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTE 503
Cdd:PRK11264 96 LFPhRTVLENII-EGPVIVKGEPKEEATARA-RELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 504 GLDATTESQILDLLANVMKGK-TVLMVTHRL---RGLVnfDQIIVMDNGHIIEQGSHAELLA--KQGRYYQF 569
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKrTMVIVTHEMsfaRDVA--DRAIFMDQGRIVEQGPAKALFAdpQQPRTRQF 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
356-553 |
1.69e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA---LR-KTVSVVPQRVHL---FSA 428
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLlpdFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 TlrDN----LLL--AAPDASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPLMLLDEPT 502
Cdd:PRK11629 105 L--ENvampLLIgkKKPAEINSRALEMLAAVGLEHRAN---------HRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489955000 503 EGLDATTESQILDLLA--NVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQ 553
Cdd:PRK11629 174 GNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
338-563 |
1.69e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAlRKTVS 417
Cdd:PRK13537 7 PIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHL---FsaTLRDNLLLAAP--DASDDTLRAMLEqvglhKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHD 492
Cdd:PRK13537 84 VVPQFDNLdpdF--TVRENLLVFGRyfGLSAAAARALVP-----PLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 493 APLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
337-563 |
3.08e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.98 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAlRKTV 416
Cdd:PRK13536 40 VAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHL-FSATLRDNLLLAAPDASDDTLRamLEQVgLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLVFGRYFGMSTRE--IEAV-IPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
339-531 |
6.00e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.78 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:PRK10247 8 LQLQNVGYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLA------APDasDDTLRAMLEQVGLHKLLEDDGLNswlgeggrQLSGGELRRLAIARALLHD 492
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPwqirnqQPD--PAIFLDDLERFALPDTILTKNIA--------ELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489955000 493 APLMLLDEPTEGLDATTESQILDLLANVM--KGKTVLMVTH 531
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTH 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
355-562 |
6.97e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.96 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA---LRKTVSVVPQ--------Rv 423
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQnpygslnpR- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 424 HLFSATLRDNLL----LAAPDASDDTLrAMLEQVGL---HKlleddglnswlgegGR---QLSGGELRRLAIARALLHDA 493
Cdd:PRK11308 109 KKVGQILEEPLLintsLSAAERREKAL-AMMAKVGLrpeHY--------------DRyphMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDL-SVVEHiaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
358-570 |
7.80e-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: 7.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 358 DITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPL----SGFSEAALRKTVSVVPQRVHLFS-ATLRD 432
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAPDAsddtlRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQ 512
Cdd:TIGR02142 95 NLRYGMKRA-----RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 513 ILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQGRYYQFK 570
Cdd:TIGR02142 170 ILPYLERLHAefGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-565 |
8.29e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLS-------GF--S 408
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrriGYlpE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 409 EAALRKTVSVVPQRVHLfsATLRDnllLAAPDAsddtLRAMLEqvglhkLLEDDGLNSWLGEGGRQLSGGELRRLAIARA 488
Cdd:COG4152 79 ERGLYPKMKVGEQLVYL--ARLKG---LSKAEA----KRRADE------WLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 489 LLHDAPLMLLDEPTEGLDA----TTESQILDLLAnvmKGKTVLMVTHRLRG---LVnfDQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPvnveLLKDVIRELAA---KGTTVIFSSHQMELveeLC--DRIVIINKGRKVLSGSVDEIRR 218
|
....
gi 489955000 562 KQGR 565
Cdd:COG4152 219 QFGR 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
339-560 |
9.61e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 96.75 E-value: 9.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQ----LLTrawdPQQGEIRFNDVPLSGFSEAALRK 414
Cdd:COG1118 3 IEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRiiagLET----PDSGRIVLNGRDLFTNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 tVSVVPQ-----RvHLfsaTLRDNL------LLAAPDASDDTLRAMLEQVGLhklleddglnSWLGEggR---QLSGGEL 480
Cdd:COG1118 77 -VGFVFQhyalfP-HM---TVAENIafglrvRPPSKAEIRARVEELLELVQL----------EGLAD--RypsQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATT----ESQILDLLANVmkGKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGS 555
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
....*
gi 489955000 556 HAELL 560
Cdd:COG1118 218 PDEVY 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
339-560 |
1.26e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAydkqaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQ----LLtrawdPQQGEIRFNDVPLSGFSEAALRK 414
Cdd:COG4138 1 LQLNDVAVA------GRLGPISAQVNAGELIHLIGPNGAGKSTLLArmagLL-----PGQGEILLNGRPLSDWSAAELAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQR-VHLFSATLRDNLLLAAPDASDDtlrAMLEQVgLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLH-- 491
Cdd:COG4138 70 HRAYLSQQqSPPFAMPVFQYLALHQPAGASS---EAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvw 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 492 -----DAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRL-RGLVNFDQIIVMDNGHIIEQGSHAELL 560
Cdd:COG4138 146 ptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELcQQGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
162-562 |
1.31e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 98.51 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 162 IALT-LGGIMLMTLIilpplfYRAGKTTGENLTRLRGEYRqqltAWLQGQAELTLfgasKRYRARM--ENTELNWHEAQR 238
Cdd:PRK10522 157 MAVTiWGGFVLVARV------YKHMATLRETEDKLYNDYQ----TVLEGRKELTL----NRERAEYvfENEYEPDAQEYR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 239 RQS------ELTAFSQALMMLIGGIAVIamLWMASGGVGGNAQPGPLIALFVF-------CALAAFEALAPVTGAFQHLG 305
Cdd:PRK10522 223 HHIiradtfHLSAVNWSNIMMLGAIGLV--FYMANSLGWADTNVAATYSLTLLflrtpllSAVGALPTLLSAQVAFNKLN 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 306 QViasalritDIAEQEPEvkFSAGQtAVPEQVALTLSNVTFAYDKQAqNALEDITLSVDAGQRIAILGRTGCGKSTLLQL 385
Cdd:PRK10522 301 KL--------ALAPYKAE--FPRPQ-AFPDWQTLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAML 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 386 LTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFsatlrDNLLLAAPDASDDTL-RAMLEQVGL-HKLLEDDG 463
Cdd:PRK10522 369 LTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-----DQLLGPEGKPANPALvEKWLERLKMaHKLELEDG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 464 LNSWLgeggrQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNFDQ 541
Cdd:PRK10522 444 RISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADR 518
|
410 420
....*....|....*....|..
gi 489955000 542 IIVMDNGHIIE-QGSHAELLAK 562
Cdd:PRK10522 519 LLEMRNGQLSElTGEERDAASR 540
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-563 |
1.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQ---NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFND--VP--LSGFSEAA 411
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaIPanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 -LRKTVSVVPQ--RVHLFSATLRDNLLLAAPDASDD---TLRAMLEQVGLHKLLEDdglnsWLGEGGRQLSGGELRRLAI 485
Cdd:PRK13645 87 rLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENkqeAYKKVPELLKLVQLPED-----YVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 486 ARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSPFEIFSN 241
|
.
gi 489955000 563 Q 563
Cdd:PRK13645 242 Q 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
355-559 |
1.46e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.17 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKTVSVVPQRVHLFSA-TLRD 432
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAPDASDDTL---------RAMLEQVGLH----KLLEDdglnswLGEGGRQLsggelrrLAIARALLHDAPLMLLD 499
Cdd:COG1129 99 NIFLGREPRRGGLIdwramrrraRELLARLGLDidpdTPVGD------LSVAQQQL-------VEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 500 EPTEGLDAtTESQIL-----DLLAnvmKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAEL 559
Cdd:COG1129 166 EPTASLTE-REVERLfriirRLKA---QGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
355-554 |
2.05e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 93.17 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFND-VPLSGfSEAALRKTVSVVPQRVHL-FSATLRD 432
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKR-RKKFLRRIGVVFGQKTQLwWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAP--DASDDTLRAMLEqvGLHKLLEddgLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTE 510
Cdd:cd03267 115 SFYLLAAiyDLPPARFKKRLD--ELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489955000 511 SQILDLL--ANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03267 190 ENIRNFLkeYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-554 |
2.13e-21 |
|
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: 92.67 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 -----VPQRvhlfsaTLRDNLLLAA--PDASDDTLRAMLEQVGLHklleddglnswlGEGGR---QLSGGELRRLAIARA 488
Cdd:cd03268 79 eapgfYPNL------TARENLRLLArlLGIRKKRIDEVLDVVGLK------------DSAKKkvkGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
339-554 |
2.42e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.34 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLS-------GF--SE 409
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnriGYlpEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 410 AALRKTVSVVPQRVHLfsATLRDnllLAAPDASDDTLRamleqvglhkLLEDDGLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:cd03269 79 RGLYPKMKVIDQLVYL--AQLKG---LKKEEARRRIDE----------WLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 490 LHDAPLMLLDEPTEGLDA----TTESQILDLLANvmkGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03269 144 IHDPELLILDEPFSGLDPvnveLLKDVIRELARA---GKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
356-548 |
3.04e-21 |
|
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: 92.53 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLS--GFSEAALRKTVSVVPQRvhlfsaTLRDN 433
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDRMVVFQNYSLLPWL------TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 434 LLLAA----PDASDDTLRAMLEQvglHklLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATT 509
Cdd:TIGR01184 75 IALAVdrvlPDLSKSERRAIVEE---H--IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489955000 510 ESQILDLLANVMK--GKTVLMVTHRL-RGLVNFDQIIVMDNG 548
Cdd:TIGR01184 150 RGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
329-561 |
3.32e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.31 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 329 GQTAVPEQVALTLSNVTFA-YDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIrfndvplsgF 407
Cdd:PTZ00243 648 EATPTSERSAKTPKMKTDDfFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------W 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 408 SEaalrKTVSVVPQRVHLFSATLRDNLLLAAP-DASD--DTLR-----AMLEQVGlhklledDGLNSWLGEGGRQLSGGE 479
Cdd:PTZ00243 719 AE----RSIAYVPQQAWIMNATVRGNILFFDEeDAARlaDAVRvsqleADLAQLG-------GGLETEIGEKGVNLSGGQ 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 480 LRRLAIARALLHDAPLMLLDEPTEGLDATTESQIL-DLLANVMKGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAE 558
Cdd:PTZ00243 788 KARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD 867
|
...
gi 489955000 559 LLA 561
Cdd:PTZ00243 868 FMR 870
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
355-531 |
3.56e-21 |
|
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: 91.33 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLsGFSEAAL---RKTVSVVPQRV--HLFSAT 429
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLlerRQRVGLVFQDPddQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRD-------NLLLAaPDASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPLMLLDEPT 502
Cdd:TIGR01166 86 VDQdvafgplNLGLS-EAEVERRVREALTAVGASGLRE---------RPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 489955000 503 EGLDATTESQILDLLAN-VMKGKTVLMVTH 531
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRlRAEGMTVVISTH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-566 |
4.23e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 354 NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNdvplsGFS----EAALRKTVSVV-PQRVHLF-S 427
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVpfkrRKEFARRIGVVfGQRSQLWwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 428 ATLRDNL-LLAA----PDAS-DDTLRAMLEQVGLHKLLEDDGlnswlgeggRQLSGGELRRLAIARALLHDAPLMLLDEP 501
Cdd:COG4586 111 LPAIDSFrLLKAiyriPDAEyKKRLDELVELLDLGELLDTPV---------RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 502 TEGLDATTESQILDLLA--NVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQGRY 566
Cdd:COG4586 182 TIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-560 |
4.28e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.84 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVV 419
Cdd:COG4604 3 EIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQRVHLFSA-TLRDnlLLA---------APDASDDTL-RAMLEQVGLHKlLEDDGLNswlgeggrQLSGGELRRLAIARA 488
Cdd:COG4604 81 RQENHINSRlTVRE--LVAfgrfpyskgRLTAEDREIiDEAIAYLDLED-LADRYLD--------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVM--KGKTVLMVTHRLrglvNF-----DQIIVMDNGHIIEQGSHAELL 560
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDI----NFascyaDHIVAMKDGRVVAQGTPEEII 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
356-548 |
4.62e-21 |
|
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: 92.01 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN----DVPLSGFSEAALRKTVSVVPQRVHLFSATLR 431
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnkneSEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAAPdASDDTLRAMLEQVGLHKLLE--DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA-- 507
Cdd:cd03290 97 ENITFGSP-FNKQRYKAVTDACSLQPDIDllPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489955000 508 ---TTESQILDLLANvmKGKTVLMVTHRLRGLVNFDQIIVMDNG 548
Cdd:cd03290 176 sdhLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-563 |
5.24e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQN---ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDV---PLSGFSEAA- 411
Cdd:PRK13631 22 LRVKNLYCVFDEKQENelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigDKKNNHELIt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 ------------LRKTVSVVPQ--RVHLFSATLRDNLLLAaPDAsddtlramleqVGLHKL---------LEDDGLN-SW 467
Cdd:PRK13631 102 npyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVA-----------LGVKKSeakklakfyLNKMGLDdSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 468 LGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVM 545
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEVaDEVIVM 249
|
250
....*....|....*...
gi 489955000 546 DNGHIIEQGSHAELLAKQ 563
Cdd:PRK13631 250 DKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
343-561 |
9.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.45 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgFSEAAL---RKTVSVV 419
Cdd:PRK13639 6 DLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQRV--HLFSATLRD-------NLLLAApDASDDTLRAMLEQVGLhklledDGLNSwlgEGGRQLSGGELRRLAIARALL 490
Cdd:PRK13639 84 FQNPddQLFAPTVEEdvafgplNLGLSK-EEVEKRVKEALKAVGM------EGFEN---KPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 491 HDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDV-DLVPVyaDKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-563 |
1.05e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.12 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSV 418
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRvhlfsatlRDNLLLAAPDASDDTL---------RAMLEQVGlhKLLEDDGLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PRK13648 88 VFQN--------PDNQFVGSIVKYDVAFglenhavpyDEMHRRVS--EALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMKGK--TVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
339-560 |
1.11e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.52 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSN--VTFAydkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTV 416
Cdd:PRK09536 4 IDVSDlsVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHL-FSATLRDNLLLA-AP-----DASDDTLRAMLEQVglhklLEDDGLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PRK09536 80 ASVPQDTSLsFEFDVRQVVEMGrTPhrsrfDTWTETDRAAVERA-----MERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLAN-VMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL 560
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRlVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
355-559 |
1.23e-20 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 91.25 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSeaALRKTVSVVPQRVHLFS-ATLRDN 433
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERNVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 434 L---LLAAPDASDDTLRAMLEQVglHKLLEDDGLnSWLGEggR---QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA 507
Cdd:cd03296 95 VafgLRVKPRSERPPEAEIRAKV--HELLKLVQL-DWLAD--RypaQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 508 TTESQILDLLANVMK--GKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:cd03296 170 KVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-551 |
1.91e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.30 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQN---ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKT 415
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVV---PQRVHLFSATLRDNLLLAA------------PDASDDTLRAMLEQVGLHklLEDDgLNSWLGeggrQLSGGEL 480
Cdd:COG1101 82 IGRVfqdPMMGTAPSMTIEENLALAYrrgkrrglrrglTKKRRELFRELLATLGLG--LENR-LDTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGK--TVLMVTHRLRGLVNF-DQIIVMDNGHII 551
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
338-562 |
2.15e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ---QGEIRFNDVPLSGFSEAALRK 414
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQRvhlfsatlRDNLLLAApDASDDTL-----RA-----MLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLA 484
Cdd:PRK13640 85 KVGIVFQN--------PDNQFVGA-TVGDDVAfglenRAvprpeMIKIV--RDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGK--TVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
339-547 |
3.56e-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: 87.59 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNaLEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIrfnDVPLsgfseaalRKTVSV 418
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE--------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFSATLRDNLLLAapdasddtlramleqvglhklleddglnsWlgegGRQLSGGELRRLAIARALLHDAPLMLL 498
Cdd:cd03223 69 LPQRPYLPLGTLREQLIYP-----------------------------W----DDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489955000 499 DEPTEGLDATTESQILDLLANvmKGKTVLMVTHRLRGLVNFDQIIVMDN 547
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
337-550 |
3.98e-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: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVTFAydkqaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKT 415
Cdd:cd03215 3 PVLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVP---QRVHLF-SATLRDNLLLaapdasddtlramleqvglhklleddglnswlgegGRQLSGGELRRLAIARALLH 491
Cdd:cd03215 77 IAYVPedrKREGLVlDLSVAENIAL-----------------------------------SSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 492 DAPLMLLDEPTEGLD-ATTES--QILDLLANvmKGKTVLMVTHRLRGLVNF-DQIIVMDNGHI 550
Cdd:cd03215 122 DPRVLILDEPTRGVDvGAKAEiyRLIRELAD--AGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
355-531 |
4.65e-20 |
|
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: 89.03 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFND----VPLSGFSE---AALRKT----VS----VV 419
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASPreiLALRRRtigyVSqflrVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PqRVhlfSAtlRD---NLLLA---APDASDDTLRAMLEQVGLHKLLeddglnsWlgeggrQL-----SGGELRRLAIARA 488
Cdd:COG4778 106 P-RV---SA--LDvvaEPLLErgvDREEARARARELLARLNLPERL-------W------DLppatfSGGEQQRVNIARG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTH 531
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFH 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
338-563 |
5.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRV--HLFSATLRD-------NLLLaAPDASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARA 488
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDdvafgpvNMGL-DKDEVERRVEEALKAVRMWDFRD---------KPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 489 LLHDAPLMLLDEPTEGLDAT---TESQILDLLANvmKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRgqeTLMEILDRLHN--QGKTVIVATHDVDLAAEWaDQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
341-554 |
9.35e-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: 93.92 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfSEAALRKTVSVVP 420
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 421 QRVHLFS-ATLRDNLLLAAPDASDDTLRAMLEqvgLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:TIGR01257 1010 QHNILFHhLTVAEHILFYAQLKGRSWEEAQLE---MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 500 EPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRglvnfDQIIVMDNGHIIEQG 554
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD-----EADLLGDRIAIISQG 1136
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
339-555 |
1.26e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.78 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSeaALRKTVSV 418
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--AENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFS-ATLRDNLLLA-----APDAS-----DDTLRAM-LEQVGLHKLleddglnswlgeggRQLSGGELRRLAIA 486
Cdd:PRK09452 91 VFQSYALFPhMTVFENVAFGlrmqkTPAAEitprvMEALRMVqLEEFAQRKP--------------HQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGS 555
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
339-559 |
1.37e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.66 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgfSEAALRKTVSV 418
Cdd:PRK11607 20 LEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHLFS-ATLRDNLllaAPDASDDTLRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLML 497
Cdd:PRK11607 96 MFQSYALFPhMTVEQNI---AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 498 LDEPTEGLDAT----TESQILDLLANVmkGKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-568 |
1.60e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQ--NALEDITLSVDAGQRIAILGRTGCGKS-TLLQLLTRAWDPQ----QGEIRFNDVPLSGFSEAA 411
Cdd:PRK15134 6 LAIENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKT-------------VSVVPqrVHLFSATLRDNLLL---AAPDASDDTLRAMLEQVGLHKlleddgLNSWLGEGGRQL 475
Cdd:PRK15134 86 LRGVrgnkiamifqepmVSLNP--LHTLEKQLYEVLSLhrgMRREAARGEILNCLDRVGIRQ------AAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 476 SGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIE 552
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLaDRVAVMQNGRCVE 237
|
250
....*....|....*..
gi 489955000 553 QGSHAELL-AKQGRYYQ 568
Cdd:PRK15134 238 QNRAATLFsAPTHPYTQ 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
356-561 |
1.75e-19 |
|
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: 87.60 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGF--SEAAlRKTVSVVPQRVHLF-SATLRD 432
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRA-RLGIGYLPQEASIFrKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAPDA--SDDTLRAMLEQvglhkLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTE 510
Cdd:cd03218 95 NILAVLEIRglSKKEREEKLEE-----LLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489955000 511 SQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:cd03218 170 QDIQKIIKILKdRGIGVLITDHNVRETLSItDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
339-531 |
1.87e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.15 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQnaLEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ---QGEIRFNDVPLSGFseAALRKT 415
Cdd:COG4136 2 LSLENLTITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQRVHLFS-ATLRDNLLLAAPD-----ASDDTLRAMLEQVGLHKLLEDDGlnswlgeggRQLSGGELRRLAIARAL 489
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFALPPtigraQRRARVEQALEEAGLAGFADRDP---------ATLSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH 531
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRqrGIPALLVTH 192
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
339-554 |
2.29e-19 |
|
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: 87.04 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQN--ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKtV 416
Cdd:cd03266 2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHLFS-ATLRDNLLLAA------PDASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARAL 489
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYFAglyglkGDELTARLEELADRLGMEELLD---------RRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-561 |
2.39e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE-AALRKTVSVV 419
Cdd:PRK13644 4 LENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQ--RVHLFSATLRDNLLLAAPDASddtlramLEQVGLHKL----LEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:PRK13644 83 FQnpETQFVGRTVEEDLAFGPENLC-------LPPIEIRKRvdraLAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
345-561 |
3.01e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.92 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 345 TFAY-----DKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgFSEAALRK----- 414
Cdd:PRK15112 13 TFRYrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqrirm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 -----TVSVVP-QRV-HLFSATLRDNLLLAAPdASDDTLRAMLEQVGLhklleddgLNSWLGEGGRQLSGGELRRLAIAR 487
Cdd:PRK15112 92 ifqdpSTSLNPrQRIsQILDFPLRLNTDLEPE-QREKQIIETLRQVGL--------LPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 488 ALLHDAPLMLLDEPTEGLDATTESQILDLLANVM--KGKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQekQGISYIYVTQHL-GMMKHisDQVLVMHQGEVVERGSTADVLA 239
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
354-561 |
5.60e-19 |
|
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: 86.17 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 354 NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS--EAAlRKTVSVVPQRVHLFSA-TL 430
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERA-RLGIGYLPQEASIFRKlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 RDNLLlAAPDASDDTLRAMLEQVgLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTE 510
Cdd:TIGR04406 94 EENIM-AVLEIRKDLDRAEREER-LEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 511 S---QILDLLANvmKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:TIGR04406 172 GdikKIIKHLKE--RGIGVLITDHNVRETLDIcDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-531 |
8.22e-19 |
|
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: 84.85 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFSATLRDNLL 435
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 436 LAAPDASDDTLRAMLEQVGLHKLlEDDGLNswlgeggrQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILD 515
Cdd:cd03231 96 FWHADHSDEQVEEALARVGLNGF-EDRPVA--------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*..
gi 489955000 516 LLA-NVMKGKTVLMVTH 531
Cdd:cd03231 167 AMAgHCARGGMVVLTTH 183
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
333-554 |
8.24e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.13 E-value: 8.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 333 VPEQVALTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF-----NDVPLSGF 407
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYG--PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 408 SEAALRKTV----SVVPQRVhlfsatlRDNL-------------LLAAPDASDDTLRAM----LEQVGLHKLLEDDGlns 466
Cdd:PRK11701 79 SEAERRRLLrtewGFVHQHP-------RDGLrmqvsaggnigerLMAVGARHYGDIRATagdwLERVEIDAARIDDL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 467 wlgegGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRL---RGLVnfDQ 541
Cdd:PRK11701 149 -----PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLavaRLLA--HR 221
|
250
....*....|...
gi 489955000 542 IIVMDNGHIIEQG 554
Cdd:PRK11701 222 LLVMKQGRVVESG 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
339-561 |
1.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQ-NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRV--HLFSATLRDNLLLAAPDASDDTlRAMLEQVGlHKLLEDDGLNSWLGEGGRqLSGGELRRLAIARALLHDAPL 495
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPR-EEMIKRVD-EALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVmKGK---TVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
343-562 |
1.28e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQR 422
Cdd:PRK13652 8 DLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 V--HLFSATLRDNLLLAAPDASDD--TLRAMLEQVgLHKLleddGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLL 498
Cdd:PRK13652 87 PddQIFSPTVEQDIAFGPINLGLDeeTVAHRVSSA-LHML----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 499 DEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-533 |
1.90e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.47 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAwDPQQGEIRFNDvPLSGFSEAA------ 411
Cdd:PRK14258 7 AIKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEG-RVEFFNQNIyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 ---LRKTVSVVPQRVHLFSATLRDNLLLAapdasddtlramLEQVGLHKLLEDDGL--------NSW------LGEGGRQ 474
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYG------------VKIVGWRPKLEIDDIvesalkdaDLWdeikhkIHKSALD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 475 LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGK-TVLMVTHRL 533
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSElTMVIVSHNL 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
329-534 |
3.17e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.83 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 329 GQTAVPEQVALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD-----PQQGEIRFNDVP 403
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 404 L--SGFSEAALRKTVSVVPQRVHLFSATLRDNLLLAA-----PDASDDTLRAMLEQVGLHKLLEDDglnswLGEGGRQLS 476
Cdd:PRK14243 79 LyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGAringyKGDMDELVERSLRQAALWDEVKDK-----LKQSGLSLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 477 GGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLR 534
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
339-551 |
4.22e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYD--KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF---NDVPLSGFSEAALR 413
Cdd:PRK10535 5 LELKDIRRSYPsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KT-VSVVPQRVHLFS-ATLRDNLLLAAPDASDDTlRAMLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLH 491
Cdd:PRK10535 85 REhFGFIFQRYHLLShLTAAQNVEVPAVYAGLER-KQRLLRA--QELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNFDQIIVMDNGHII 551
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
335-563 |
4.78e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 335 EQVALTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA-LR 413
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKI--QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQRVHLFS-ATLRDNLLLAAPDASDDTLRAMLEQVGlhklleddGLNSWLGEGGRQ----LSGGELRRLAIARA 488
Cdd:PRK11614 80 EAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWVY--------ELFPRLHERRIQragtMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRL-RGLVNFDQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
336-554 |
4.89e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 336 QVALTLSNVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPlsgfSEAALRKT 415
Cdd:PRK15056 4 QAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 -VSVVPQRVHL---FSATLRDNLL---------LAAPDASD-DTLRAMLEQVGLHKLLEDDglnswLGEggrqLSGGELR 481
Cdd:PRK15056 79 lVAYVPQSEEVdwsFPVLVEDVVMmgryghmgwLRRAKKRDrQIVTAALARVDMVEFRHRQ-----IGE----LSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 482 RLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQG 554
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-566 |
7.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS------EAA 411
Cdd:PRK14271 21 AMAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSifnyrdVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQRVHLFSATLRDNLL-------LAAPDASDDTLRAMLEQVGLHklledDGLNSWLGEGGRQLSGGELRRLA 484
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMSIMDNVLagvrahkLVPRKEFRGVAQARLTEVGLW-----DAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL--- 560
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFssp 253
|
....*...
gi 489955000 561 --AKQGRY 566
Cdd:PRK14271 254 khAETARY 261
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
354-531 |
8.61e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.52 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 354 NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSE---AALR-KTVSVVPQRVHLF-SA 428
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFMLIpTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 TLRDNLLLAA------PDASDDTLRAMLEQVGLHKLLedDGLNSwlgeggrQLSGGELRRLAIARALLHDAPLMLLDEPT 502
Cdd:PRK10584 104 NALENVELPAllrgesSRQSRNGAKALLEQLGLGKRL--DHLPA-------QLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|.
gi 489955000 503 EGLDATTESQILDLL--ANVMKGKTVLMVTH 531
Cdd:PRK10584 175 GNLDRQTGDKIADLLfsLNREHGTTLILVTH 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-562 |
1.04e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.39 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLL--TRAWDPQQGEIRFN---------------- 400
Cdd:TIGR03269 1 IEVKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 401 --------------DVPLSGFSEA---ALRKTVSVVPQRVHLF--SATLRDNLLLAAPDASDDTLRAMLEQVglhKLLED 461
Cdd:TIGR03269 79 gepcpvcggtlepeEVDFWNLSDKlrrRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAV---DLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 462 DGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMV-----THRLRGL 536
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltshwPEVIEDL 235
|
250 260
....*....|....*....|....*.
gi 489955000 537 VnfDQIIVMDNGHIIEQGSHAELLAK 562
Cdd:TIGR03269 236 S--DKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-547 |
1.20e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.01 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 316 DIAEQEPEVKFSAGQTAVPEQVALTLSNVTFAYDKQAQNAL-EDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQ 394
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 395 GEIRFNDV-PLSGFSEAALRKTVSVVPQRVHLFSATLRDNL---------LLAAPDASDD-------------------- 444
Cdd:PTZ00265 440 GDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdLEALSNYYNEdgndsqenknkrnscrakca 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 445 -TLRAMLEQVGLHKLLE-----------------------------DDGLNSWLGEGGRQLSGGELRRLAIARALLHDAP 494
Cdd:PTZ00265 520 gDLNDMSNTTDSNELIEmrknyqtikdsevvdvskkvlihdfvsalPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 495 LMLLDEPTEGLDATTESQILDLLANvMKG---KTVLMVTHRLRGLVNFDQIIVMDN 547
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINN-LKGnenRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
337-554 |
1.42e-17 |
|
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: 81.15 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVTFAYDKQAQNA--LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ---QGEIRFNDVPLSGFSEAA 411
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQRVHLFSATLRDNLLLAAPDASDDTLRAmleqvglhklleddglnswlgeggrqLSGGELRRLAIARALLH 491
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVRG--------------------------ISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILD---LLANVMKGKTVLMVTHRLRGLVN-FDQIIVMDNGHIIEQG 554
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKcirTMADVLKTTTFVSLYQASDEIYDlFDKVLVLYEGRQIYYG 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
341-538 |
1.57e-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: 81.25 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgfseaalrkTVSVVP 420
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 421 QRVHLFSA---------TLRDNLLLAAPDASDdtlramlEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLH 491
Cdd:TIGR01189 72 HENILYLGhlpglkpelSALENLHFWAAIHGG-------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLL-ANVMKGKTVLMVTHRLRGLVN 538
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLrAHLARGGIVLLTTHQDLGLVE 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
355-555 |
1.90e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKST----LLQLLtrawdPQQGEIRFNDVPLSGFSEAAL---RKTVSVVPQ------ 421
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 422 --------------RVH--LFSATLRDNLLLAApdasddtlramLEQVGlhklLEDDGLNSWLGEggrqLSGGELRRLAI 485
Cdd:PRK15134 376 nprlnvlqiieeglRVHqpTLSAAQREQQVIAV-----------MEEVG----LDPETRHRYPAE----FSGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 486 ARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTV--LMVTHRL---RGLVNfdQIIVMDNGHIIEQGS 555
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLhvvRALCH--QVIVLRQGEVVEQGD 509
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-559 |
3.28e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.36 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQaqNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD--PQ---QGEIRFN--DVPLSGFSEAA 411
Cdd:PRK14239 6 LQVSDLSVYYNKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNghNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKTVSVVPQRVHLFSATLRDNL-----LLAAPDAS--DDTLRAMLEQVGLHKLLEDDGLNSWLGeggrqLSGGELRRLA 484
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVvyglrLKGIKDKQvlDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
339-563 |
4.43e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKTVS 417
Cdd:PRK10895 4 LTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRVHLFSATLRDNLLLAAPDASDDtLRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLML 497
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 498 LDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQ 563
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
343-562 |
4.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.67 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQN----ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA-ALRKTVS 417
Cdd:PRK13633 9 NVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRvhlfsatlRDNLLLAAPDASD------------DTLRAMLEQVglhklLEDDGLNSWLGEGGRQLSGGELRRLAI 485
Cdd:PRK13633 89 MVFQN--------PDNQIVATIVEEDvafgpenlgippEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 486 ARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
343-560 |
8.02e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPQR 422
Cdd:PRK10253 12 QLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFSATLRDNLLLAA--PDASDDTLRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDE 500
Cdd:PRK10253 90 ATTPGDITVQELVARGryPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 501 PTEGLDATTESQILDLLA--NVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL 560
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSelNREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-569 |
8.12e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.40 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEI----------RFNDVPLSGFSEAAL---RKTVSVVPQR 422
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvRDKDGQLKVADKNQLrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFS-ATLRDNLL--------LAAPDASDDTLRaMLEQVGLHKLLEddglnswlGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:PRK10619 101 FNLWShMTVLENVMeapiqvlgLSKQEARERAVK-YLAKVGIDERAQ--------GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA--KQGRYYQF 569
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGnpQSPRLQQF 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
339-565 |
9.34e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRfndvplsgfSEAALRktVSV 418
Cdd:PRK09544 5 VSLENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHL---FSATLRDNLLLAAPDASDDTLRAmLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK09544 72 VPQKLYLdttLPLTVNRFLRLRPGTKKEDILPA-LKRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 496 MLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRgLV--NFDQIIVMdNGHIIEQGS------HAELLAKQGR 565
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLH-LVmaKTDEVLCL-NHHICCSGTpevvslHPEFISMFGP 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
336-560 |
1.27e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 336 QVALTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKT 415
Cdd:PRK10575 9 DTTFALRNVSFRV--PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 416 VSVVPQRVhlfsatlrdnlllaaPDASDDTLRamlEQVGLhklleddGLNSWLGEGGR---------------------- 473
Cdd:PRK10575 87 VAYLPQQL---------------PAAEGMTVR---ELVAI-------GRYPWHGALGRfgaadrekveeaislvglkpla 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 474 -----QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV--MKGKTVLMVTHRLRGLVNF-DQIIVM 545
Cdd:PRK10575 142 hrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINMAARYcDYLVAL 221
|
250
....*....|....*
gi 489955000 546 DNGHIIEQGSHAELL 560
Cdd:PRK10575 222 RGGEMIAQGTPAELM 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
356-559 |
1.43e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA-ALRKTVSVVPQRVHLF-SATLRDN 433
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkAHQLGIYLVPQEPLLFpNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 434 LL--LAAPDASDDTLRAMLEQVGLHklLEDDGLNSWLGEGGRQLsggelrrLAIARALLHDAPLMLLDEPTEGLD-ATTE 510
Cdd:PRK15439 107 ILfgLPKRQASMQKMKQLLAALGCQ--LDLDSSAGSLEVADRQI-------VEILRGLMRDSRILILDEPTASLTpAETE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489955000 511 ---SQILDLLAnvmKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK15439 178 rlfSRIRELLA---QGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-560 |
1.83e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.32 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTR---AWDPQ---QGEIRFNDVPLSGFSEAALRKTVSVVPQRVHLFS-A 428
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieIYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPhL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 TLRDNLllAAPDAS---------DDTLRAMLEQVGLHKLLEDDgLNSwlgeGGRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:PRK14246 106 SIYDNI--AYPLKShgikekreiKKIVEECLRKVGLWKEVYDR-LNS----PASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 500 EPTEGLDATTESQILDLLANVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL 560
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-531 |
2.15e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.55 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQR-----IAILGRTGCGKSTLLQLLTrawdpqqGEIRfndvPLSGFSEAALRktVSVVPQRV-HLFSAT 429
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLA-------GVLK----PDEGEVDPELK--ISYKPQYIkPDYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDNLLLAAPDASDDTLRA-MLEQVGLHKLLEddglnSWLGEggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDAT 508
Cdd:PRK13409 417 VEDLLRSITDDLGSSYYKSeIIKPLQLERLLD-----KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*
gi 489955000 509 TESQILDLLANVM--KGKTVLMVTH 531
Cdd:PRK13409 488 QRLAVAKAIRRIAeeREATALVVDH 512
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
355-567 |
2.95e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL----RKTVSVVPQRVHLFS-AT 429
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPhMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDN----LLLAAPDASDDTLRAM--LEQVGLHklleddglnSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTE 503
Cdd:PRK10070 123 VLDNtafgMELAGINAEERREKALdaLRQVGLE---------NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 504 GLDATTESQILDLLANVMKG--KTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQGRYY 567
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
356-560 |
4.26e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT--RAWDPQQGEIRFNDVPLSGFSeaalrktvsvVPQRVH--LFSA--- 428
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELS----------PDERARagIFLAfqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 -------TLRdNLLLAA--------PDASD--DTLRAMLEQVGLhkllEDDGLNSWLGEGgrqLSGGELRRLAIARALLH 491
Cdd:COG0396 86 pveipgvSVS-NFLRTAlnarrgeeLSAREflKLLKEKMKELGL----DEDFLDRYVNEG---FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 492 DAPLMLLDEPTEGLDATTesqiLDLLANVM-----KGKTVLMVTH--RLRGLVNFDQIIVMDNGHIIEQGShAELL 560
Cdd:COG0396 158 EPKLAILDETDSGLDIDA----LRIVAEGVnklrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELA 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-562 |
4.28e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYdkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPL--SGFSEAALRKTV 416
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQ--RVHLFSATLRDNLLLAAPD---ASDDTLRAMleqvglhklleDDGLNSWLGEGGRQ-----LSGGELRRLAIA 486
Cdd:PRK13638 80 ATVFQdpEQQIFYTDIDSDIAFSLRNlgvPEAEITRRV-----------DEALTLVDAQHFRHqpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
340-559 |
4.35e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 340 TLSNVTFAYDKQAQNalEDITLSVDAGQRIAILGRTGCGKSTLLQLLT-----RAWDPQQGEIRFNDVPLSgfseaalRK 414
Cdd:PRK11000 5 TLRNVTKAYGDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAglediTSGDLFIGEKRMNDVPPA-------ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQRVHLFS-ATLRDN----LLLAAPDASDDTLRamLEQVG----LHKLLEddglnswlgeggRQ---LSGGELRR 482
Cdd:PRK11000 76 GVGMVFQSYALYPhLSVAENmsfgLKLAGAKKEEINQR--VNQVAevlqLAHLLD------------RKpkaLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 483 LAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
338-564 |
5.61e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFndvpLSG-FSEAALRKTV 416
Cdd:NF033858 1 VARLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV----LGGdMADARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 S----VVPQRV--HLFsATL--RDNLL----LAAPDASDDTLRamleqvgLHKLLEDDGLNSWLGEGGRQLSGGELRRLA 484
Cdd:NF033858 75 CpriaYMPQGLgkNLY-PTLsvFENLDffgrLFGQDAAERRRR-------IDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK---GKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAerpGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLA 226
|
...
gi 489955000 562 KQG 564
Cdd:NF033858 227 RTG 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
353-558 |
6.15e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 353 QNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA---LRKTVSVVPQRVHLF-SA 428
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 TLRDNL---LLAAPDASDDTLR---AMLEQVGLHklleDDGLNSWLgeggrQLSGGELRRLAIARALLHDAPLMLLDEPT 502
Cdd:PRK10908 95 TVYDNVaipLIIAGASGDDIRRrvsAALDKVGLL----DKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 503 EGLDATTESQILDLLANVMK-GKTVLMVTHRLrGLV---NFdQIIVMDNGHIIEqGSHAE 558
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRvGVTVLMATHDI-GLIsrrSY-RMLTLSDGHLHG-GVGGE 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
357-569 |
7.22e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 357 EDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAAL---RKTVSVVPQRVHLFS-ATLRD 432
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTdMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NllLAAPDASDDTLRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQ 512
Cdd:PRK11831 104 N--VAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 513 ILDLLA--NVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAKQG-RYYQF 569
Cdd:PRK11831 182 LVKLISelNSALGVTCVVVSHDVPEVLSIaDHAYIVADKKIVAHGSAQALQANPDpRVRQF 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-531 |
8.55e-16 |
|
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: 80.60 E-value: 8.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQ-----RIAILGRTGCGKSTLLQLLTrawdpqqGEIRfndvPLSGFSEAALRktVSVVPQRV-HLFSAT 429
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILA-------GVLK----PDEGEVDEDLK--ISYKPQYIsPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDNLLLAAPDASDDT-LRA-MLEQVGLHKLLEDDgLNSwlgeggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA 507
Cdd:COG1245 418 VEEFLRSANTDDFGSSyYKTeIIKPLGLEKLLDKN-VKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180
....*....|....*....|....*.
gi 489955000 508 TTESQILDLLANVM--KGKTVLMVTH 531
Cdd:COG1245 489 EQRLAVAKAIRRFAenRGKTAMVVDH 514
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
355-534 |
1.73e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS-EAALRKTVSVVPQRVHLFSA-TLRD 432
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAPDA-----SDDTLRAMLEQV----GL----HKLLEDdglnswlgeggrqLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:COG3845 100 NIVLGLEPTkggrlDRKAARARIRELseryGLdvdpDAKVED-------------LSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489955000 500 EPTEGLdatTESQILDLLAnVMK-----GKTVLMVTHRLR 534
Cdd:COG3845 167 EPTAVL---TPQEADELFE-ILRrlaaeGKSIIFITHKLR 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
356-553 |
2.15e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSeaALRKTVSVVPQRVHLFS-ATLRDNL 434
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH--ARDRKVGFVFQHYALFRhMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 435 ---LLAAPDASDDTLRAMLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTES 511
Cdd:PRK10851 96 afgLTVLPRRERPNAAAIKAKV--TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489955000 512 QI---LDLLANVMKGKTVLmVTH-RLRGLVNFDQIIVMDNGHiIEQ 553
Cdd:PRK10851 174 ELrrwLRQLHEELKFTSVF-VTHdQEEAMEVADRVVVMSQGN-IEQ 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
339-560 |
3.56e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVtfaydkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQ----LLtrawdPQQGEIRFNDVPLSGFSEAALRK 414
Cdd:PRK03695 1 MQLNDV------AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQRV---------HLFSATLRDNlllAAPDASDDTLRAMLEQVGLhklleDDGLNSWLGeggrQLSGGELRRLAI 485
Cdd:PRK03695 70 HRAYLSQQQtppfampvfQYLTLHQPDK---TRTEAVASALNEVAEALGL-----DDKLGRSVN----QLSGGEWQRVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 486 ARALLHDAP-------LMLLDEPTEGLDATTESqILDLLANVM--KGKTVLMVTHRL-RGLVNFDQIIVMDNGHIIEQGS 555
Cdd:PRK03695 138 AAVVLQVWPdinpagqLLLLDEPMNSLDVAQQA-ALDRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGR 216
|
....*
gi 489955000 556 HAELL 560
Cdd:PRK03695 217 RDEVL 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
356-532 |
4.78e-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: 78.25 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWdPQQGEIRFNDVPLSGFseaalrktvsVVPQRVHLFSATLRDNLL 435
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGKLF----------YVPQRPYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 436 LaaPDASDD---------TLRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLD 506
Cdd:TIGR00954 537 Y--PDSSEDmkrrglsdkDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*.
gi 489955000 507 ATTESQILDLLANVmkGKTVLMVTHR 532
Cdd:TIGR00954 615 VDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
357-531 |
4.92e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 357 EDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfseaalrktvsvvpQRVHLFSATL------ 430
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR--------------QRDEYHQDLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 --------RDNLLLAAP---DASDDTLRAMLEQVGLHKLlEDDGLnswlgeggRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:PRK13538 84 gikteltaLENLRFYQRlhgPGDDEALWEALAQVGLAGF-EDVPV--------RQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|...
gi 489955000 500 EPTEGLDATTESQILDLLA-NVMKGKTVLMVTH 531
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAqHAEQGGMVILTTH 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
355-554 |
6.09e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.11 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEI--RFNDVPLSGFseaalrkTVSVVPqrvhlfSATLRD 432
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvRGRVSSLLGL-------GGGFNP------ELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 N--LLLAAPDASDDTLRAMLEQVglhklLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTE 510
Cdd:cd03220 104 NiyLNGRLLGLSRKEIDEKIDEI-----IEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489955000 511 SQILDLLAN-VMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQG 554
Cdd:cd03220 179 EKCQRRLRElLKQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
339-559 |
7.14e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.30 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN--DVPLSGFSEaalrKTV 416
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgeDVTHRSIQQ----RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPQRVHLFS-ATLRDNL-----LLAAPDAS-DDTLRAMLEQVGLHKLlEDDGLNswlgeggrQLSGGELRRLAIARAL 489
Cdd:PRK11432 81 CMVFQSYALFPhMSLGENVgyglkMLGVPKEErKQRVKEALELVDLAGF-EDRYVD--------QISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTH-RLRGLVNFDQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
355-533 |
8.85e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 8.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgFSE--AALRKTVSVVPQRVHLF-SATLR 431
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASttAALAAGVAIIYQELHLVpEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAAPDASDDTL--RAMLEQVG--LHKLLEDDGLNSWLGEggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA 507
Cdd:PRK11288 98 ENLYLGQLPHKGGIVnrRLLNYEAReqLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190
....*....|....*....|....*....|.
gi 489955000 508 tTESQIL-----DLLAnvmKGKTVLMVTHRL 533
Cdd:PRK11288 174 -REIEQLfrvirELRA---EGRVILYVSHRM 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
350-559 |
1.10e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 350 KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVpQRVH---LF 426
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDI-QMIFqdpLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 427 SATLRDNL--LLAAP----------DASDDTLRAMLEQVGLHKLLeddgLNSWLGEggrqLSGGELRRLAIARALLHDAP 494
Cdd:PRK15079 110 SLNPRMTIgeIIAEPlrtyhpklsrQEVKDRVKAMMLKVGLLPNL----INRYPHE----FSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 495 LMLLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLrGLVNF--DQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDL-AVVKHisDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-531 |
1.84e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQ-----GEIRF--NDVPLSGFSEAALRKTVSVVPQRVHLFS- 427
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLfgRNIYSPDVDPIEVRREVGMVFQYPNPFPh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 428 ATLRDNL--------LLAAPDASDDTLRAMLEQVGLHKLLEDDgLNSWLGeggrQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:PRK14267 100 LTIYDNVaigvklngLVKSKKELDERVEWALKKAALWDEVKDR-LNDYPS----NLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190
....*....|....*....|....*....|..
gi 489955000 500 EPTEGLDATTESQILDLLANVMKGKTVLMVTH 531
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-551 |
2.07e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 332 AVPEQVALTLSNVTFAyDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA 411
Cdd:COG3845 251 AEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 LRKT-VSVVP---QRVHLF-SATLRDNLLLAAPDASDDTLRAMLEQVGLHKLLED---------DGLNSWLgeggRQLSG 477
Cdd:COG3845 330 RRRLgVAYIPedrLGRGLVpDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEElieefdvrtPGPDTPA----RSLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 478 GELRRLAIARALLHDAPLMLLDEPTEGLD-ATTE---SQILDLLAnvmKGKTVLMVTHRLRGLVNF-DQIIVMDNGHII 551
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDvGAIEfihQRLLELRD---AGAAVLLISEDLDEILALsDRIAVMYEGRIV 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
335-565 |
2.21e-14 |
|
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: 75.74 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 335 EQVALTLSNVTFAYDKQaQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRfndvPLSGFseaalrk 414
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----PQPGI------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQRVHL-FSATLRDNLLLAAPDASDDTLRamLEQVGLHKLLEDDGLNSWLGEGGR-------------------- 473
Cdd:TIGR03719 69 KVGYLPQEPQLdPTKTVRENVEEGVAEIKDALDR--FNEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsqleia 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 474 --------------QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANvMKGkTVLMVTHRLRGLVNF 539
Cdd:TIGR03719 147 mdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTHDRYFLDNV 224
|
250 260
....*....|....*....|....*....
gi 489955000 540 DQ-IIVMDNGHIIE-QGSHAELL-AKQGR 565
Cdd:TIGR03719 225 AGwILELDRGRGIPwEGNYSSWLeQKQKR 253
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
356-561 |
2.61e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFS--EAAlRKTVSVVPQRVHLF-SATLRD 432
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRA-RLGIGYLPQEASIFrKLTVED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLlaapdasddtlrAMLEQVGLHK---------LLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTE 503
Cdd:COG1137 98 NIL------------AVLELRKLSKkereerleeLLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 504 GLDATTESQILDLLAN-VMKGKTVLMVTHRLR---GLVnfDQIIVMDNGHIIEQGSHAELLA 561
Cdd:COG1137 166 GVDPIAVADIQKIIRHlKERGIGVLITDHNVRetlGIC--DRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-564 |
2.82e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRfndvplsgFSEAAlrkTVS 417
Cdd:PRK15064 319 ALEVENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSENA---NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQ-RVHLFSATLrdNLL-----LAAPDASDDTLRAMleqvgLHKLL--EDDglnswLGEGGRQLSGGELRRLAIARAL 489
Cdd:PRK15064 386 YYAQdHAYDFENDL--TLFdwmsqWRQEGDDEQAVRGT-----LGRLLfsQDD-----IKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 490 LHDAPLMLLDEPTEGLDatTES-QILDLLANVMKGkTVLMVTHRlRGLVN--FDQII-VMDNGHIIEQGSHAELLAKQG 564
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMD--MESiESLNMALEKYEG-TLIFVSHD-REFVSslATRIIeITPDGVVDFSGTYEEYLRSQG 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-533 |
3.29e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 366 GQRIAILGRTGCGKSTLLQLLTrawdpqqGEI-----RFNDVP-----LSGFSEAAL----------RKTVSVVPQRVHL 425
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILS-------GELipnlgDYEEEPswdevLKRFRGTELqnyfkklyngEIKVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 426 ----FSATLRDnlLLAAPDASDDtLRAMLEQVGLHKLLEDDGlnswlgeggRQLSGGELRRLAIARALLHDAPLMLLDEP 501
Cdd:PRK13409 172 ipkvFKGKVRE--LLKKVDERGK-LDEVVERLGLENILDRDI---------SELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 489955000 502 TEGLDATTESQILDLLANVMKGKTVLMVTHRL 533
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-559 |
4.31e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGF-SEAALRKTVSVVPQRVHLF-SATLRD 432
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFrEMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLAAPDASDDTLRAMLEQVGLHKLLEDDGLN---SWLGEGG------RQ---LSGGELRRLAIARALLHDAPLMLLDE 500
Cdd:PRK11300 100 NLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDraaTWLERVGllehanRQagnLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 501 PTEGLDAtTESQILDLLANVMK---GKTVLMVTHRLrGLVN--FDQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK11300 180 PAAGLNP-KETKELDELIAELRnehNVTVLLIEHDM-KLVMgiSDRIYVVNQGTPLANGTPEEI 241
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
356-555 |
5.41e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.37 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDA---GQRI-AILGRTGCGKSTLLQL---LTRawdPQQGEIRFNDVPL----SGFSEAALRKTVSVVPQRVH 424
Cdd:PRK11144 10 LGDLCLTVNLtlpAQGItAIFGRSGAGKTSLINAisgLTR---PQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 425 LFSA-TLRDNLL--LAAPDASD-DTLRAMLeqvGLHKLLEddglnswlgeggR---QLSGGELRRLAIARALLHDAPLML 497
Cdd:PRK11144 87 LFPHyKVRGNLRygMAKSMVAQfDKIVALL---GIEPLLD------------RypgSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 498 LDEPTEGLDATTESQILDLLANVMKG-KT-VLMVTHRLRGLVNF-DQIIVMDNGHIIEQGS 555
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREiNIpILYVSHSLDEILRLaDRVVVLEQGKVKAFGP 212
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
355-562 |
5.62e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.40 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKS----TLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTV----SVV---PQRV 423
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIIgreiAMIfqePSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 424 HLFSATLRDNLLLAAPDasdDTLR---------------AMLEQVGL--HKlledDGLNSWlgegGRQLSGGELRRLAIA 486
Cdd:COG4170 102 LDPSAKIGDQLIEAIPS---WTFKgkwwqrfkwrkkraiELLHRVGIkdHK----DIMNSY----PHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLA--NVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLArlNQLQGTSILLISHDLESISQWaDTITVLYCGQTVESGPTEQILKS 249
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-562 |
6.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.46 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDK-QAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVS 417
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 418 VVPQRV--HLFSATLRDNLLLAAPDASDDtLRAMLEQVglHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPL 495
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIP-HEEMKERV--NEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 496 MLLDEPTEGLDATTEsqiLDLLANVMK-----GKTVLMVTHRLRGLVNFDQIIVMDNGHIIEQGSHAELLAK 562
Cdd:PRK13650 162 IILDEATSMLDPEGR---LELIKTIKGirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
356-531 |
1.17e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPlsgfseaalrKTVSVVPQRVHLF--------S 427
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----------IDDPDVAEACHYLghrnamkpA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 428 ATLRDNLLLAAP--DASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGL 505
Cdd:PRK13539 88 LTVAENLEFWAAflGGEELDIAAALEAVGLAPLAH---------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 489955000 506 DATTESQILDLLANVMK-GKTVLMVTH 531
Cdd:PRK13539 159 DAAAVALFAELIRAHLAqGGIVIAATH 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-560 |
1.41e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.71 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWD--PQ---QGEIRFNDVPLSGFSEAALRKTVSVVPQ------RVH 424
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpipNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 425 LFSAT---LRDNLLLAAPDASDDTLRAMLEQVGLHKLLEDDglnswLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEP 501
Cdd:PRK14247 99 IFENValgLKLNRLVKSKKELQERVRWALEKAQLWDEVKDR-----LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 502 TEGLDATTESQILDLLANVMKGKTVLMVTH------RLRGLVNFdqiivMDNGHIIEQGSHAELL 560
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRISDYVAF-----LYKGQIVEWGPTREVF 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
334-531 |
1.78e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRfndvPLSGFseaalr 413
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPPKKQ-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----PAPGI------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 kTVSVVPQRVHL-FSATLRDNL-------------------LLAAPDASDDTLraMLEQVGLHKLLedDGLNSWlgEGGR 473
Cdd:PRK11819 71 -KVGYLPQEPQLdPEKTVRENVeegvaevkaaldrfneiyaAYAEPDADFDAL--AAEQGELQEII--DAADAW--DLDS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 474 Q-------------------LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANvMKGkTVLMVTH 531
Cdd:PRK11819 144 QleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD-YPG-TVVAVTH 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
355-555 |
2.30e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFND--VPL----SGFseaalrktvsvVPQrvhlfsA 428
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSALlelgAGF-----------HPE------L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 TLRDNLLLAApdasddtlrAMLeqvGLHKL----LEDD-----GLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:COG1134 104 TGRENIYLNG---------RLL---GLSRKeideKFDEivefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 500 EPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGS 555
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
366-533 |
2.78e-13 |
|
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: 72.51 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 366 GQRIAILGRTGCGKSTLLQLLTrawdpqqGEI-----RFNDVP-----LSGFSEAAL----------RKTVSVVPQRVHL 425
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILS-------GELkpnlgDYDEEPswdevLKRFRGTELqdyfkklangEIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 426 ----FSATLRDnlLLAAPDASDDtLRAMLEQVGLHKLLEDDGlnswlgeggRQLSGGELRRLAIARALLHDAPLMLLDEP 501
Cdd:COG1245 172 ipkvFKGTVRE--LLEKVDERGK-LDELAEKLGLENILDRDI---------SELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 489955000 502 TEGLDAT---TESQILDLLANvmKGKTVLMVTHRL 533
Cdd:COG1245 240 SSYLDIYqrlNVARLIRELAE--EGKYVLVVEHDL 272
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
356-564 |
3.27e-13 |
|
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: 68.71 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT--RAWDPQQGEIRFNDVPLSGFS--EAAlRKTVSVVPQRvhlfsatlr 431
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPpeERA-RLGIFLAFQY--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 dnlllaaPdasddtlrAMLEQVGLHKLLEDdglnswLGEGgrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTes 511
Cdd:cd03217 86 -------P--------PEIPGVKNADFLRY------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA-- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 512 qiLDLLANVM-----KGKTVLMVTH--RLRGLVNFDQIIVMDNGHIIEQG--SHAELLAKQG 564
Cdd:cd03217 140 --LRLVAEVInklreEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGdkELALEIEKKG 199
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
339-548 |
6.59e-13 |
|
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: 67.65 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYD--KQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ--QGEIRFNDVPLsgfsEAALRK 414
Cdd:cd03232 4 LTWKNLNYTVPvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 TVSVVPQR-VHLFSATLRDNLLLAApdasddtlramleqvglhklleddglnsWLgeggRQLSGGELRRLAIARALLHDA 493
Cdd:cd03232 80 STGYVEQQdVHSPNLTVREALRFSA----------------------------LL----RGLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLV--NFDQIIVMDNG 548
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
351-555 |
8.53e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 351 QAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQ----LLTRAWDPQQG-EIRFNDVPLSGFSEAALRKT---VSVVPQR 422
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHiELLGRTVQREGRLARDIRKSranTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFSA-TLRDNLLLAAPDASD---DTLRAMLEQVGLHKL--LEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:PRK09984 95 FNLVNRlSVLENVLIGALGSTPfwrTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGS 555
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYcERIVALRQGHVFYDGS 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
350-561 |
9.29e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 350 KQAQNALEDI-TLSVD-----AGQRIAILGRTGCGKSTLLQLLtrawdpqQGEIrfndVPLSGFSEAALRKTVSV-VPQR 422
Cdd:PRK10938 7 SQGTFRLSDTkTLQLPsltlnAGDSWAFVGANGSGKSALARAL-------AGEL----PLLSGERQSQFSHITRLsFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 423 VHLFSAT-LRDNLLLAAPDaSDDTLRAMLE--QVGLHK------LLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDA 493
Cdd:PRK10938 76 QKLVSDEwQRNNTDMLSPG-EDDTGRTTAEiiQDEVKDparceqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 494 PLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDFvQFAGVLADCTLAETGEREEILQ 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
343-555 |
9.31e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKS----TLLQLLTRawdpqQGEI----RFNDVPLSGFSEAALRK 414
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 415 ----TVSVVPQ----------RVhlfSATLRDNLLL----AAPDASDDTLRaMLEQVglhKLLEddgLNSWLGEGGRQLS 476
Cdd:PRK09473 94 lraeQISMIFQdpmtslnpymRV---GEQLMEVLMLhkgmSKAEAFEESVR-MLDAV---KMPE---ARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 477 GGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLaNVMK---GKTVLMVTHRLrGLVN--FDQIIVMDNGHII 551
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL-NELKrefNTAIIMITHDL-GVVAgiCDKVLVMYAGRTM 241
|
....
gi 489955000 552 EQGS 555
Cdd:PRK09473 242 EYGN 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-561 |
1.05e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 351 QAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ--QGEIRFNDVPLSgfsEAALRKTVSVVPQRVHLFSA 428
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT---KQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 TLRDNL----LLAAPDA--SDDTLRA---MLEQVGLHKLLEDDGLNSWLgeggRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:PLN03211 156 TVRETLvfcsLLRLPKSltKQEKILVaesVISELGLTKCENTIIGNSFI----RGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 500 EPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLV--NFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-531 |
2.78e-12 |
|
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: 67.05 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAG-----QRIAILGRTGCGKSTLLQLLTRAWDPQQGEIrfndvplsgfseAALRKTVSVVPQRVHL-FSAT 429
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYIKAdYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDNLLLAAPDASDDTL--RAMLEQVGLHKLLEDDGLNswlgeggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDa 507
Cdd:cd03237 78 VRDLLSSITKDFYTHPYfkTEIAKPLQIEQILDREVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD- 147
|
170 180 190
....*....|....*....|....*....|
gi 489955000 508 tTESQIldLLANVMK------GKTVLMVTH 531
Cdd:cd03237 148 -VEQRL--MASKVIRrfaennEKTAFVVEH 174
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-531 |
5.99e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN---DVPLSGFSEAAL----- 412
Cdd:PRK11147 322 MENVNYQID--GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklEVAYFDQHRAELdpekt 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 --------RKTVSVVPQRVHLFSaTLRDnlLLAAPdasddtLRAMLEQvglhklleddglnswlgeggRQLSGGELRRLA 484
Cdd:PRK11147 400 vmdnlaegKQEVMVNGRPRHVLG-YLQD--FLFHP------KRAMTPV--------------------KALSGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANvMKGkTVLMVTH 531
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
356-573 |
6.08e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 6.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQL----LTRAWDPQ----QGEIRFNDVPLSGFSEAALRKTVSVVPQRVH-LF 426
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 427 SATLRDNLLLAA-PDASDDTLRAMLEQVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARAL--LHDAP-------LM 496
Cdd:PRK13547 97 AFSAREIVLLGRyPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWPPHdaaqpprYL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELL--AKQGRYYQFKQ 571
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHaDRIAMLADGAIVAHGAPADVLtpAHIARCYGFAV 256
|
..
gi 489955000 572 RL 573
Cdd:PRK13547 257 RL 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
316-559 |
1.10e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 316 DIAEQEPEvkfsagQTAVPEQVALTLSNVTfaydkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQG 395
Cdd:COG1129 240 ELEDLFPK------RAAAPGEVVLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 396 EIRFNDVPLSGFS-EAAL----------RKTVSVVPQRvhlfsaTLRDNLLLAApdasddtlramLEQVGLHKLL----E 460
Cdd:COG1129 308 EIRLDGKPVRIRSpRDAIragiayvpedRKGEGLVLDL------SIRENITLAS-----------LDRLSRGGLLdrrrE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 461 DDGLNSWLGEGG----------RQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDL---LANvmKGKTVL 527
Cdd:COG1129 371 RALAEEYIKRLRiktpspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLireLAA--EGKAVI 448
|
250 260 270
....*....|....*....|....*....|....*
gi 489955000 528 MVT---HRLRGLVnfDQIIVMDNGHIIEQGSHAEL 559
Cdd:COG1129 449 VISselPELLGLS--DRILVMREGRIVGELDREEA 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
343-555 |
1.16e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 343 NVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFND----------VPLSGFSEAAL 412
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 RKT-------------VSVVP---------QRVHLFSATLRDNLLLAApdasddtlRAMLEQVglhKLLEDDGLnswLGE 470
Cdd:PRK10261 99 RHVrgadmamifqepmTSLNPvftvgeqiaESIRLHQGASREEAMVEA--------KRMLDQV---RIPEAQTI---LSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 471 GGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKT--VLMVTHRLRGLVNF-DQIIVMDN 547
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQ 244
|
....*...
gi 489955000 548 GHIIEQGS 555
Cdd:PRK10261 245 GEAVETGS 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
302-533 |
1.27e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 302 QHLGQVIASALRITDIAEQEPEVkFSAGQTAVPEQVALTLSNVTFAYDKQAqnALEDITLSVDAGQRIAILGRTGCGKST 381
Cdd:PRK10938 225 QALVAQLAHSEQLEGVQLPEPDE-PSARHALPANEPRIVLNNGVVSYNDRP--ILHNLSWQVNPGEHWQIVGPNGAGKST 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 382 LLQLLTRawDPQQGeiRFNDVPL------SGFSEAALRKTVSVVPQRVHL---FSATLRDNLLLAAPD------ASDDTL 446
Cdd:PRK10938 302 LLSLITG--DHPQG--YSNDLTLfgrrrgSGETIWDIKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDsigiyqAVSDRQ 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 447 RaMLEQVGLHKLleddGLNSWLGEGG-RQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTES---QILDLLanVMK 522
Cdd:PRK10938 378 Q-KLAQQWLDIL----GIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVL--ISE 450
|
250 260
....*....|....*....|...
gi 489955000 523 GKTVLM------------VTHRL 533
Cdd:PRK10938 451 GETQLLfvshhaedapacITHRL 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
355-548 |
1.74e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA-ALRKTVSVVPQRVHLFSA-TLRD 432
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 NLLLA-----------APDASDDTLRA--MLEQVGLHKLLEDDGLNswlgeggrqLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:PRK09700 100 NLYIGrhltkkvcgvnIIDWREMRVRAamMLLRVGLKVDLDEKVAN---------LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489955000 500 EPTEGLdATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNG 548
Cdd:PRK09700 171 EPTSSL-TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-561 |
2.49e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFN------DVPLSGFSEAA-LRKTVSVVPQRVHLFS 427
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPGPDGRGrAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 428 -ATLRDNLLLAAPDASDDTLRAM-----LEQVGLhkllEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEP 501
Cdd:TIGR03269 379 hRTVLDNLTEAIGLELPDELARMkavitLKMVGF----DEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 502 TEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
366-533 |
2.89e-11 |
|
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: 63.92 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 366 GQRIAILGRTGCGKSTLLQLLTRAWDPQQGeiRFNDVP-------------LSGFSEAALRKTVSVV--PQRVHLFSATL 430
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeildefrgseLQNYFTKLLEGDVKVIvkPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 RDN--LLLAAPDASDdTLRAMLEQVGLHKLLEDDGlnswlgeggRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDA- 507
Cdd:cd03236 104 KGKvgELLKKKDERG-KLDELVDQLELRHVLDRNI---------DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIk 173
|
170 180
....*....|....*....|....*...
gi 489955000 508 --TTESQILDLLANvmKGKTVLMVTHRL 533
Cdd:cd03236 174 qrLNAARLIRELAE--DDNYVLVVEHDL 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
341-532 |
4.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 341 LSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfSEAALRKTVSVVP 420
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 421 QRVHLF-SATLRDNLLLAAPDASDDtlramleqVGLHKLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLD 499
Cdd:PRK13540 81 HRSGINpYLTLRENCLYDIHFSPGA--------VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 489955000 500 EPTEGLDA-TTESQILDLLANVMKGKTVLMVTHR 532
Cdd:PRK13540 153 EPLVALDElSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-554 |
4.83e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 354 NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDV---PLSGFSEAALRKTVSVVPQRVHlfsatl 430
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPY------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 rdnlllAAPDASDDTLRAMLEQVGLHKLLEDDGLN---SWLGEG-----------GRQLSGGELRRLAIARALLHDAPLM 496
Cdd:PRK10261 412 ------ASLDPRQTVGDSIMEPLRVHGLLPGKAAAarvAWLLERvgllpehawryPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489955000 497 LLDEPTEGLDATTESQILDLLANVMK--GKTVLMVTHRLRGLVNFD-QIIVMDNGHIIEQG 554
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
22-314 |
6.53e-11 |
|
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: 63.34 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 22 IVLAIVTLLASIGLLTLSGWFLSASAAAGFAGLYSFNYMLPAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFS 101
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 102 KLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVPIALtlggIMLMTLIILPPLF 181
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTL----VALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 182 YRAGKTTgENLTRLRGEYRQQLTAWLQ----GQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGI 257
Cdd:cd07346 157 RYFRRRI-RKASREVRESLAELSAFLQeslsGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 258 AVIAMLWMASGGV-GGNAQPGPLIAlFVFCALAAFEALAPVTGAFQHLGQVIASALRI 314
Cdd:cd07346 236 GTALVLLYGGYLVlQGSLTIGELVA-FLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
356-564 |
1.25e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT--RAWDPQQGEIRFNDvplsgfsEAALRKTVSvvpQRVHL--FSA--- 428
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKG-------ESILDLEPE---ERAHLgiFLAfqy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 429 -------TLRDNLLLA---------APDASD----DTLRAMLEQVGLHKLLeddgLNSWLGEGgrqLSGGELRRLAIARA 488
Cdd:CHL00131 93 pieipgvSNADFLRLAynskrkfqgLPELDPleflEIINEKLKLVGMDPSF----LSRNVNEG---FSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 489 LLHDAPLMLLDEPTEGLDA---TTESQILDLLANvmKGKTVLMVTH--RLRGLVNFDQIIVMDNGHIIEQGSH--AELLA 561
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIdalKIIAEGINKLMT--SENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAelAKELE 243
|
...
gi 489955000 562 KQG 564
Cdd:CHL00131 244 KKG 246
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
355-561 |
2.59e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKStllqLLTRA--------WDPQQGEIRFNDVPLSGFSEAALRK----TVSVV--- 419
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKS----LIAKAicgvtkdnWRVTADRMRFDDIDLLRLSPRERRKlvghNVSMIfqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 420 PQRVHLFSATLRDNLLLAAPDASDD----------TLRA--MLEQVGL--HKlledDGLNSWLGEggrqLSGGELRRLAI 485
Cdd:PRK15093 98 PQSCLDPSERVGRQLMQNIPGWTYKgrwwqrfgwrKRRAieLLHRVGIkdHK----DAMRSFPYE----LTEGECQKVMI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 486 ARALLHDAPLMLLDEPTEGLDATTESQILDLLA--NVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLA 561
Cdd:PRK15093 170 AIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQWaDKINVLYCGQTVETAPSKELVT 248
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
338-562 |
4.80e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.40 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAYDKQAQnALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEI-----RFNDVplsgfsEAAL 412
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNEL------EPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 413 RKtVSVVPQRVHLFS-ATLRDNLLLAAPDA--SDDTLRAMLEQVGlhKLLEddgLNSWLGEGGRQLSGGELRRLAIARAL 489
Cdd:PRK11650 76 RD-IAMVFQNYALYPhMSVRENMAYGLKIRgmPKAEIEERVAEAA--RILE---LEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQ----ILDLLANVmkGKTVLMVTH-RLRGLVNFDQIIVMDNGHiIEQ-GSHAELLAK 562
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQmrleIQRLHRRL--KTTSLYVTHdQVEAMTLADRVVVMNGGV-AEQiGTPVEVYEK 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
353-564 |
5.49e-10 |
|
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: 59.97 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 353 QNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLtrAWDPQ----QGEIRFNDVPLSGFS--EAAlRKTVSVVPQ----- 421
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPSyevtSGTILFKGQDLLELEpdERA-RAGLFLAFQypeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 422 -----RVHLFSA--TLRDNLLLAAPDASD--DTLRAMLEQVGLHKLLEDDGLNswlgEGgrqLSGGELRRLAIARALLHD 492
Cdd:TIGR01978 90 pgvsnLEFLRSAlnARRSARGEEPLDLLDfeKLLKEKLALLDMDEEFLNRSVN----EG---FSGGEKKRNEILQMALLE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 493 APLMLLDEPTEGL--DATTE-SQILDLLANvmKGKTVLMVTH--RLRGLVNFDQIIVMDNGHIIEQG--SHAELLAKQG 564
Cdd:TIGR01978 163 PKLAILDEIDSGLdiDALKIvAEGINRLRE--PDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSGdvELAKELEAKG 239
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
68-281 |
8.24e-10 |
|
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: 60.09 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 68 GTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVV 147
Cdd:cd18544 49 GLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 148 IVVVTLGLSFLDVPIAltlggimLMTLIILPPLF-----YRagKTTGENLTRLRgEYRQQLTAWLQ----GQAELTLFGA 218
Cdd:cd18544 129 LIGILIAMFLLNWRLA-------LISLLVLPLLLlatylFR--KKSRKAYREVR-EKLSRLNAFLQesisGMSVIQLFNR 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 219 SKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAMLWMASGGV-GGNAQPGPLIA 281
Cdd:cd18544 199 EKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVlSGAVTLGVLYA 262
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
344-559 |
8.42e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 344 VTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKS----TLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTV--- 416
Cdd:PRK11022 11 VHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVgae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 ----------SVVPQRVHLFSATlrdNLLLAAPDASDDTLRA----MLEQVGLhklledDGLNSWLGEGGRQLSGGELRR 482
Cdd:PRK11022 91 vamifqdpmtSLNPCYTVGFQIM---EAIKVHQGGNKKTRRQraidLLNQVGI------PDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 483 LAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGK--TVLMVTHRLrGLV--NFDQIIVMDNGHIIEQGSHAE 558
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDL-ALVaeAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 489955000 559 L 559
Cdd:PRK11022 241 I 241
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
411-564 |
8.49e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 ALRKTVS----VVPQRVHLFSAtlRDNLLLAAP--DASDDTLRAMLEQvglhkLLEDDGLNSWLGEGGRQLSGGELRRLA 484
Cdd:NF000106 82 ALRRTIG*hrpVR*GRRESFSG--RENLYMIGR*lDLSRKDARARADE-----LLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 485 IARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAELLAK 562
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTK 234
|
..
gi 489955000 563 QG 564
Cdd:NF000106 235 VG 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-513 |
9.09e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF-NDVPLSGFSEAAL---RKTVSVVPQRVHLfsatlr 431
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLeflRADESPLQHLARL------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 dnlllaAPDASDDTLRAMLEQVGLHklleddglNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLD----- 506
Cdd:PRK10636 402 ------APQELEQKLRDYLGGFGFQ--------GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrq 467
|
....*..
gi 489955000 507 ATTESQI 513
Cdd:PRK10636 468 ALTEALI 474
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
339-550 |
2.01e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTR-----AWDpqqGEIRFNDVPL--SGFSEAA 411
Cdd:TIGR02633 2 LEMKGIVKTFG--GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgTWD---GEIYWSGSPLkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 lRKTVSVVPQRVHLF-SATLRDNLLLAAP--------DASDDTLRA--MLEQVGLhklledDGLNSWLGEGgrQLSGGEL 480
Cdd:TIGR02633 77 -RAGIVIIHQELTLVpELSVAENIFLGNEitlpggrmAYNAMYLRAknLLRELQL------DADNVTRPVG--DYGGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489955000 481 RRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV-MKGKTVLMVTHRLRGLVNF-DQIIVMDNG-HI 550
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAVcDTICVIRDGqHV 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
356-509 |
2.18e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF-NDVPLSGFSEAALRK---TV-SVVPQRVHLFSATL 430
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQQDPPRNvegTVyDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 431 R---DNLLLAAPDASDDTLRAM------LEQVGLHKLleDDGLNSWLGEGG-------RQLSGGELRRLAIARALLHDAP 494
Cdd:PRK11147 99 KryhDISHLVETDPSEKNLNELaklqeqLDHHNLWQL--ENRINEVLAQLGldpdaalSSLSGGWLRKAALGRALVSNPD 176
|
170
....*....|....*
gi 489955000 495 LMLLDEPTEGLDATT 509
Cdd:PRK11147 177 VLLLDEPTNHLDIET 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
339-533 |
2.41e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTR-----AWDpqqGEIRFNDVPL--SGFSEAA 411
Cdd:PRK13549 6 LEMKNITKTFG--GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgTYE---GEIIFEGEELqaSNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 lRKTVSVVPQRVHLFSA-TLRDNLLLAAP-------DASDDTLRA--MLEQVGLH-----KLLEddglnswLGEGGRQLs 476
Cdd:PRK13549 81 -RAGIAIIHQELALVKElSVLENIFLGNEitpggimDYDAMYLRAqkLLAQLKLDinpatPVGN-------LGLGQQQL- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 477 ggelrrLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRL 533
Cdd:PRK13549 152 ------VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKL 203
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
334-532 |
2.49e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRA--WDPQQGEIRFNDVPLSgfseaa 411
Cdd:COG2401 24 SERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQFG------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 412 lrktvsvvpqrvhlfsatlRDNLLLAAPDASDDTLRAMleqvglhKLLEDDGLNS---WLGEgGRQLSGGELRRLAIARA 488
Cdd:COG2401 98 -------------------REASLIDAIGRKGDFKDAV-------ELLNAVGLSDavlWLRR-FKELSTGQKFRFRLALL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489955000 489 LLHDAPLMLLDEPTEGLDATTeSQILDllANVMK-----GKTVLMVTHR 532
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQT-AKRVA--RNLQKlarraGITLVVATHH 196
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
59-314 |
3.19e-09 |
|
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: 58.20 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 59 YMLPAAGVrGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVI 138
Cdd:cd18552 39 LLVPLAII-GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 139 SPMVgafvvivvvtlglsfLDVPIALTLGGIM--------LMTLIILPPLFY---RAGKttgenltRLRGEYRQQLTAW- 206
Cdd:cd18552 118 TVLV---------------RDPLTVIGLLGVLfyldwkltLIALVVLPLAALpirRIGK-------RLRKISRRSQESMg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 207 ---------LQGQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAMLWMASGGV-GGNAQP 276
Cdd:cd18552 176 dltsvlqetLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQViSGELTP 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 489955000 277 GPLIAlFVFCALAAFEALAPVTGAFQHLGQVIASALRI 314
Cdd:cd18552 256 GEFIS-FITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-533 |
4.36e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.64 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 316 DIAEQEPEVKFSAGQTAVpeqvaLTLSNVTFAYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQG 395
Cdd:TIGR01257 1920 DVAEERQRIISGGNKTDI-----LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG 1994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 396 EIRF-NDVPLSGFSEaaLRKTVSVVPQrvhlFSA-----TLRDNLLLAApdasddTLRAM----LEQV---GLHKLledd 462
Cdd:TIGR01257 1995 DATVaGKSILTNISD--VHQNMGYCPQ----FDAiddllTGREHLYLYA------RLRGVpaeeIEKVanwSIQSL---- 2058
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 463 GLNSWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRL 533
Cdd:TIGR01257 2059 GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSM 2130
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
353-554 |
5.46e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.79 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 353 QNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAwdpqQGEIRFNDVpLSGFSEaalRKTVSVvpqrvhlfsatlrd 432
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISF-LPKFSR---NKLIFI-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 433 nlllaapdasdDTLRAMLEqVGLHKLLEDDGLNSwlgeggrqLSGGELRRLAIARALLHDAP--LMLLDEPTEGLDATTE 510
Cdd:cd03238 66 -----------DQLQFLID-VGLGYLTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489955000 511 SQILDLLAN-VMKGKTVLMVTHRLRGLVNFDQIIVM------DNGHIIEQG 554
Cdd:cd03238 126 NQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
355-559 |
1.23e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRF--NDVPLSG--FSEAAlrkTVSVVPQRVHLFSA-T 429
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGpkSSQEA---GIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 430 LRDNLLLAapdasddtlRAMLEQVG--LHKLL--EDDGLNSWLG--EGGRQLSG----GELRRLAIARALLHDAPLMLLD 499
Cdd:PRK10762 96 IAENIFLG---------REFVNRFGriDWKKMyaEADKLLARLNlrFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 500 EPTEGL-DATTESqildlLANVMK-----GKTVLMVTHRLRGLVNF-DQIIVMDNGHIIEQGSHAEL 559
Cdd:PRK10762 167 EPTDALtDTETES-----LFRVIRelksqGRGIVYISHRLKEIFEIcDDVTVFRDGQFIAEREVADL 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
358-555 |
1.81e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 358 DITLSVDA----GQRIAILGRTGCGKSTLLQLLTRAWD----PQQGEIRFNDVPLSGFSEaalRKTVSVV---PQRVHLF 426
Cdd:TIGR00956 75 DILKPMDGlikpGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKK---HYRGDVVynaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 427 SATLRDNLLLAA--------PDA-SDDTLRAMLEQVGLHKLLEDDGLNSWLG-EGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:TIGR00956 152 HLTVGETLDFAArcktpqnrPDGvSREEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 497 LLDEPTEGLDATTESQILDLL---ANVMKgKTVLMV-------THRLrglvnFDQIIVMDNGHIIEQGS 555
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALktsANILD-TTPLVAiyqcsqdAYEL-----FDKVIVLYEGYQIYFGP 294
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
356-548 |
4.36e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDP---QQGEIRFNDVPL-SGFSeaalRKTVSVVPQRVHLFSATLR 431
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLdSSFQ----RSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAA--------PDAS-DDTLRAMLEQVGLHKLLEddglnSWLGEGGRQLSGGELRRLAIARALLHDAPLML-LDEP 501
Cdd:TIGR00956 855 ESLRFSAylrqpksvSKSEkMEYVEEVIKLLEMESYAD-----AVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489955000 502 TEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLV--NFDQIIVMDNG 548
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILfeEFDRLLLLQKG 979
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
334-531 |
4.43e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 334 PEQVALTLSNVTFAYdKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIrfndvplsgFSEAALR 413
Cdd:PLN03073 504 PGPPIISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKVR 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 ktVSVVPQRvHLFSATLRDNLLL----AAPDASDDTLRAMLEQVGLHKLLEDDGLNSwlgeggrqLSGGELRRLAIARAL 489
Cdd:PLN03073 574 --MAVFSQH-HVDGLDLSSNPLLymmrCFPGVPEQKLRAHLGSFGVTGNLALQPMYT--------LSGGQKSRVAFAKIT 642
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489955000 490 LHDAPLMLLDEPTEGLDATTESQILDLLANVMKGktVLMVTH 531
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
356-554 |
7.18e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT--RAWDPQQGEIRFNDVP--------LSGFSEAALRKTVSVVPQRVHL 425
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPkkqetfarISGYCEQNDIHSPQVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 426 FSATLRdnllLAAPDASDDTLRaMLEQVglHKLLEDDGL-NSWLG-EGGRQLSGGELRRLAIARALLHDAPLMLLDEPTE 503
Cdd:PLN03140 976 YSAFLR----LPKEVSKEEKMM-FVDEV--MELVELDNLkDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 504 GLDATTESQILDLLAN-VMKGKTVLMVTHR--LRGLVNFDQIIVMD-NGHIIEQG 554
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNtVDTGRTVVCTIHQpsIDIFEAFDELLLMKrGGQVIYSG 1103
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
355-552 |
9.74e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTrAWDPQ---QGEIRFNDVPLSgF-----SEA----------ALrktv 416
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-GVYPHgsyEGEILFDGEVCR-FkdirdSEAlgiviihqelAL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 svVPQrvhlfsATLRDNLLLAAPDAS------DDTL---RAMLEQVGLHkllED-DGLNSWLGEGGRQLsggelrrLAIA 486
Cdd:NF040905 90 --IPY------LSIAENIFLGNERAKrgvidwNETNrraRELLAKVGLD---ESpDTLVTDIGVGKQQL-------VEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489955000 487 RALLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGHIIE 552
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVaDSITVLRDGRTIE 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
347-506 |
1.30e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 347 AYDKQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALRKTVSVVPqrvhlf 426
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 427 saTLRDNLllaapdasdDTLRAMLEQVGLH---------KLLEDDGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLML 497
Cdd:PRK13543 92 --GLKADL---------STLENLHFLCGLHgrrakqmpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
....*....
gi 489955000 498 LDEPTEGLD 506
Cdd:PRK13543 161 LDEPYANLD 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-552 |
1.89e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 320 QEPEVKFSAGQTA---VPEQVALTLSNVTFAYDKQAQnaleDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGE 396
Cdd:PRK09700 244 RELQNRFNAMKENvsnLAHETVFEVRNVTSRDRKKVR----DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 397 IRFNDVPLSGFSE-AALRKTVSVVPQR------VHLFSatLRDNLLLAA--PDASDDTLRAMLEQVGLHKLLED--DGLN 465
Cdd:PRK09700 320 IRLNGKDISPRSPlDAVKKGMAYITESrrdngfFPNFS--IAQNMAISRslKDGGYKGAMGLFHEVDEQRTAENqrELLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 466 ---SWLGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-D 540
Cdd:PRK09700 398 lkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcD 477
|
250
....*....|..
gi 489955000 541 QIIVMDNGHIIE 552
Cdd:PRK09700 478 RIAVFCEGRLTQ 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
302-550 |
2.85e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 302 QHLGQVIASALRITDIAEQEPEVKFSAGQTAVPEQ---VALTLSNVTfAYD--KQAQNALEDITLSVDAGQRIAILGRTG 376
Cdd:TIGR02633 218 QHVATKDMSTMSEDDIITMMVGREITSLYPHEPHEigdVILEARNLT-CWDviNPHRKRVDDVSFSLRRGEILGVAGLVG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 377 CGKSTLLQLLTRAWDPQ-QGEIRFNDVPLSGFSEA-ALRKTVSVVPQ--RVHLFSATLR--DNLLLAAPD---------- 440
Cdd:TIGR02633 297 AGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAGIAMVPEdrKRHGIVPILGvgKNITLSVLKsfcfkmrida 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 441 -ASDDTLRAMLEQVGLHKLLEDDGLNSwlgeggrqLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLL-A 518
Cdd:TIGR02633 377 aAELQIIGSAIQRLKVKTASPFLPIGR--------LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQ 448
|
250 260 270
....*....|....*....|....*....|...
gi 489955000 519 NVMKGKTVLMVTHRLRGLVNF-DQIIVMDNGHI 550
Cdd:TIGR02633 449 LAQEGVAIIVVSSELAEVLGLsDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
355-551 |
3.58e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 355 ALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSgF--SEAALRKTVSVVPQRVHLF-SATLR 431
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID-FksSKEALENGISMVHQELNLVlQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 432 DNLLLAA-PDAS---------DDTlRAMLEQVGLHKLLEDDGLNswlgeggrqLSGGELRRLAIARALLHDAPLMLLDEP 501
Cdd:PRK10982 92 DNMWLGRyPTKGmfvdqdkmyRDT-KAIFDELDIDIDPRAKVAT---------LSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489955000 502 TEGLdatTESQILDLLANVMK----GKTVLMVTHRLRGLVNF-DQIIVMDNGHII 551
Cdd:PRK10982 162 TSSL---TEKEVNHLFTIIRKlkerGCGIVYISHKMEEIFQLcDEITILRDGQWI 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
356-515 |
6.12e-07 |
|
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: 52.24 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDvplsgfseaalrkTVSV--VPQRvhlfsatlRDN 433
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-------------TVKLayVDQS--------RDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 434 LllaapdasdDTLRAMLEQV--GL-HKLLEDDGLNS--WLG----EGGRQ------LSGGELRRLAIARALLHDAPLMLL 498
Cdd:TIGR03719 397 L---------DPNKTVWEEIsgGLdIIKLGKREIPSraYVGrfnfKGSDQqkkvgqLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180
....*....|....*....|.
gi 489955000 499 DEPTEGLDATT----ESQILD 515
Cdd:TIGR03719 468 DEPTNDLDVETlralEEALLN 488
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
475-566 |
1.50e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 475 LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNF-DQIIVMDNGH--- 549
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGItDRILVMSNGLvag 471
|
90
....*....|....*....
gi 489955000 550 IIE--QGSHAELLAKQGRY 566
Cdd:PRK10982 472 IVDtkTTTQNEILRLASLH 490
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-314 |
1.59e-06 |
|
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: 50.23 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 18 LTLGIVLAIVTLLASIGLLTLSGWFLSASAAAGFAGLYSFNYMLPAAGVrgtAITRTAGRYFERLVSHDATFRVLQHLRI 97
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGA---YLLRALLNFLRIYLNHVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 98 YTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVPIALTlggimlmTLIIL 177
Cdd:cd18778 78 DLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALL-------TLIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 178 PPLFYRAGKTTGenltRLRGEYRQQ------LTAWLQ----GQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAFS 247
Cdd:cd18778 151 PFLALGAWLYSK----KVRPRYRKVrealgeLNALLQdnlsGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIF 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 248 QALMMLIGGIAVIAMLWMasGG---VGGNAQPGPLIALFVFCALaAFEALAPVTGAFQHLGQVIASALRI 314
Cdd:cd18778 227 HPLMEFLTSLGTVLVLGF--GGrlvLAGELTIGDLVAFLLYLGL-FYEPITSLHGLNEMLQRALAGAERV 293
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-558 |
1.62e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 337 VALTLSNVtfaydkQAQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEA------ 410
Cdd:PRK11288 256 VRLRLDGL------KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairag 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 411 -AL----RKTVSVVPqrvhlfSATLRDNLLLAAPDASddtLRAmleqvglhKLLEDDGLNSWLGE-----------GGRQ 474
Cdd:PRK11288 330 iMLcpedRKAEGIIP------VHSVADNINISARRHH---LRA--------GCLINNRWEAENADrfirslniktpSREQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 475 ----LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMK-GKTVLMVTHRLR---GLVnfDQIIVMD 546
Cdd:PRK11288 393 limnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPevlGVA--DRIVVMR 470
|
250
....*....|..
gi 489955000 547 NGHIIEQGSHAE 558
Cdd:PRK11288 471 EGRIAGELAREQ 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
366-549 |
1.64e-06 |
|
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: 48.14 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 366 GQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIrfndvplsgfseaalrktvsvvpqrvhlfsatlrdnlLLAAPDASDDT 445
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------IYIDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 446 LRAMLEQVGLhklleddglnswlGEGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLL-------A 518
Cdd:smart00382 45 VLDQLLLIIV-------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllL 111
|
170 180 190
....*....|....*....|....*....|....*..
gi 489955000 519 NVMKGKTVLMVTHRLRGLVN------FDQIIVMDNGH 549
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-561 |
1.70e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 475 LSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLaNVMK--GKTVLMVTHRLRGLVNF-DQIIVMDNGHI- 550
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKaeGLSIILVSSEMPEVLGMsDRILVMHEGRIs 474
|
90
....*....|....*
gi 489955000 551 ----IEQGSHAELLA 561
Cdd:PRK10762 475 geftREQATQEKLMA 489
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
457-555 |
1.72e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 457 KLLEDDGLNSW-LGEGGRQLSGGELRRLAIARALLHDAP---LMLLDEPTEGLDATTESQILDLLAN-VMKGKTVLMVTH 531
Cdd:cd03271 151 QTLCDVGLGYIkLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEH 230
|
90 100 110
....*....|....*....|....*....|
gi 489955000 532 RLRGLVNFDQIIVM------DNGHIIEQGS 555
Cdd:cd03271 231 NLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
363-533 |
2.69e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 363 VDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNdvplsgfseaalRKTVSVVPQRVhlfsatlrdnlllaapdas 442
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQYI------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 443 ddtlramleqvglhklleddglnswlgeggrQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLAN-VM 521
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlSE 119
|
170
....*....|...
gi 489955000 522 KG-KTVLMVTHRL 533
Cdd:cd03222 120 EGkKTALVVEHDL 132
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
457-559 |
3.49e-06 |
|
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: 50.01 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 457 KLLEDDGLNSW-LGEGGRQLSGGELRRLAIARALLHDA---PLMLLDEPTEGLDATTESQILDLLAN-VMKGKTVLMVTH 531
Cdd:TIGR00630 811 QTLCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEH 890
|
90 100 110
....*....|....*....|....*....|....
gi 489955000 532 RLRGLVNFDQIIVM------DNGHIIEQGSHAEL 559
Cdd:TIGR00630 891 NLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
358-550 |
5.65e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 358 DITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAA-LRKTVSVVP---QRVHLF------- 426
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 427 --SATLRDNLLLAAPDASDdtlRAMLEQ----VGLhKLLEDDglnswlgEGGRQLSGGELRRLAIARALLHDAPLMLLDE 500
Cdd:PRK15439 361 nvCALTHNRRGFWIKPARE---NAVLERyrraLNI-KFNHAE-------QAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489955000 501 PTEGLDATTESQILDLLANVMK-GKTVLMVTHRLRGLVNF-DQIIVMDNGHI 550
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
372-506 |
5.86e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 372 LGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGfSEAALRKTVSVVPQRVHLFSA-TLRDNLLLAA------PDASDD 444
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRVGYMSQAFSLYGElTVRQNLELHArlfhlpAAEIAA 376
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 445 TLRAMLEQVGLHKLLedDGLNSWLGEGGRQlsggelrRLAIARALLHDAPLMLLDEPTEGLD 506
Cdd:NF033858 377 RVAEMLERFDLADVA--DALPDSLPLGIRQ-------RLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
338-561 |
1.04e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 338 ALTLSNVTFAydKQAQ-NALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQ---QGEIRFNDvplSGFSEAALR 413
Cdd:PLN03140 164 ALGMLGINLA--KKTKlTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG---YRLNEFVPR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 414 KTVSVVPQR-VHLFSATLRDNLLLAA-------------------------PDASDDTLRAMLEQVGLHKLLEDDGLNSW 467
Cdd:PLN03140 239 KTSAYISQNdVHVGVMTVKETLDFSArcqgvgtrydllselarrekdagifPEAEVDLFMKATAMEGVKSSLITDYTLKI 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 468 LG-----------EGGRQLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANV--MKGKTVLMV----- 529
Cdd:PLN03140 319 LGldickdtivgdEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvhLTEATVLMSllqpa 398
|
250 260 270
....*....|....*....|....*....|....
gi 489955000 530 --THRLrglvnFDQIIVMDNGHIIEQGSHAELLA 561
Cdd:PLN03140 399 peTFDL-----FDDIILLSEGQIVYQGPRDHILE 427
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-506 |
1.20e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNdvplSGFSEAALRKTVSVVPQ-------------- 421
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFP----GNWQLAWVNQETPALPQpaleyvidgdreyr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 422 --RVHLFSATLR-DNLLLAAPDASDDTLRAMLEQVGLHKLLEDDGL-NSWLGEGGRQLSGGELRRLAIARALLHDAPLML 497
Cdd:PRK10636 93 qlEAQLHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
....*....
gi 489955000 498 LDEPTEGLD 506
Cdd:PRK10636 173 LDEPTNHLD 181
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
78-314 |
1.79e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 46.71 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 78 YFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLylrVISPMVGAFVVIVVVTLGLSF 157
Cdd:cd18576 54 FFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDT---LTTTLAEFLRQILTLIGGVVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 158 LdVPIALTLGGIMLMTLiilpPLFYRAGKTTGENLTRLRGEYRQQLtAWLQGQAELTLFG------------ASKRYRAR 225
Cdd:cd18576 131 L-FFISWKLTLLMLATV----PVVVLVAVLFGRRIRKLSKKVQDEL-AEANTIVEETLQGirvvkaftredyEIERYRKA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 226 MENTElnwhEAQRRQSELTAFSQALMMLIGGIAVIAMLWMASGGV-GGNAQPGPLIALFVFCAL--AAFEALAPVTGAFQ 302
Cdd:cd18576 205 LERVV----KLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVlAGELTAGDLVAFLLYTLFiaGSIGSLADLYGQLQ 280
|
250
....*....|..
gi 489955000 303 hlgQVIASALRI 314
Cdd:cd18576 281 ---KALGASERV 289
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
339-544 |
1.81e-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: 46.06 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDKQAQNALEDITLsvdagqriaILGRTGCGKSTLLQLLTRAWdpqqgeirFNDVPLSGFSEAALRKTVSV 418
Cdd:cd03240 4 LSIRNIRSFHERSEIEFFSPLTL---------IVGQNGAGKTTIIEALKYAL--------TGELPPNSKGGAHDPKLIRE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQR--VHL-FS-ATLRDNLLLAAPDASDDTLraMLEQVGLHKLLEDdglnswlgEGGRqLSGGE------LRRLAIARA 488
Cdd:cd03240 67 GEVRaqVKLaFEnANGKKYTITRSLAILENVI--FCHQGESNWPLLD--------MRGR-CSGGEkvlaslIIRLALAET 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489955000 489 LLHDAPLMLLDEPTEGLDattESQILDLLANVMKgktvlmvthRLRGLVNFdQIIV 544
Cdd:cd03240 136 FGSNCGILALDEPTTNLD---EENIEESLAEIIE---------ERKSQKNF-QLIV 178
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
90-285 |
2.04e-05 |
|
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: 46.48 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 90 RVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFvVIVVVTLGLSFLdVPIALTLggI 169
Cdd:pfam00664 71 RLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSL-ATIVGGIIVMFY-YGWKLTL--V 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 170 MLMTLIILPPLFYRAGKTTGENLTRLRGEY--RQQLTAW-LQGQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAF 246
Cdd:pfam00664 147 LLAVLPLYILVSAVFAKILRKLSRKEQKAVakASSVAEEsLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489955000 247 SQALMMLIGGIAVIAMLWMASGGVG-GNAQPGPLIALFVF 285
Cdd:pfam00664 227 SFGITQFIGYLSYALALWFGAYLVIsGELSVGDLVAFLSL 266
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
61-270 |
2.21e-05 |
|
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: 46.66 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 61 LPAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISP 140
Cdd:cd18542 40 LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 141 MVGAFVVIVVVTLGLSFLDVPIAltlggimLMTLIILPPLFYRAGKtTGENLTRLRGEYRQQLtawlqgqAELT------ 214
Cdd:cd18542 120 LVRAVLLFIGALIIMFSINWKLT-------LISLAIIPFIALFSYV-FFKKVRPAFEEIREQE-------GELNtvlqen 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 215 --------LFGASKRYRARMENTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAMLWMasGGV 270
Cdd:cd18542 185 ltgvrvvkAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWV--GGY 246
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-545 |
2.91e-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: 44.66 E-value: 2.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489955000 474 QLSGGELRRLAIARAL----LHDAPLMLLDEPTEGLDATTESQILDLLA-NVMKGKTVLMVTHRLRGLVNFDQIIVM 545
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILeHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
61-227 |
8.26e-05 |
|
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: 44.71 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 61 LPAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISP 140
Cdd:cd18584 38 PLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 141 MVGAFVVIVVVTLGLSFLDVPIALtlggIMLMTLIILPPLFYRAGKTTG-------ENLTRLRGeyrqQLTAWLQGQAEL 213
Cdd:cd18584 118 LVLAAIVPLLILVAVFPLDWVSAL----ILLVTAPLIPLFMILIGKAAQaasrrqwAALSRLSG----HFLDRLRGLPTL 189
|
170
....*....|....
gi 489955000 214 TLFGASKRYRARME 227
Cdd:cd18584 190 KLFGRARAQAARIA 203
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
70-314 |
8.92e-05 |
|
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: 44.72 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 70 AITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVD-TLDHLYLRVISPMVGAFVVI 148
Cdd:cd18554 56 LILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEqTKDFITTGLMNIWLDMITII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 149 VVVTLGLsFLDVpiALTLGGIMLMTL-IILPPLFYRAGKTTGENLTRLRGEYRQQLTAWLQGQAELTLFGASKRYRARME 227
Cdd:cd18554 136 IAICIML-VLNP--KLTFVSLVIFPFyILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 228 NTELNWHEAQRRQSELTAFSQALMMLIGGIAVIAMLWMASGGV-GGNAQPGPLIALFVFCALaAFEALAPVTGAFQHLGQ 306
Cdd:cd18554 213 KRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLViEGNLTVGTLVAFVGYMER-MYSPLRRLVNSFTTLTQ 291
|
....*...
gi 489955000 307 VIASALRI 314
Cdd:cd18554 292 SFASMDRV 299
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
90-314 |
1.21e-04 |
|
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: 44.35 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 90 RVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISPMVGAFVVIVVVTLGLSFLDVPIAL-TLGG 168
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLvTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 169 IMLMTLIILP--PLFYRAGKTTGENLtrlrGEYRQQLTAWLQGQAELTLFGASKRYRARMENTELNWHEAQRRQSELTAF 246
Cdd:cd18551 146 VPLAFLIILPlgRRIRKASKRAQDAL----GELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEAL 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 247 SQALMMLIGGIAVIAMLWMasGGV---GGNAQPGPLIALFVFcalaAFEALAPVT---GAFQHLGQVIASALRI 314
Cdd:cd18551 222 IGPLMGLAVQLALLVVLGV--GGArvaSGALTVGTLVAFLLY----LFQLITPLSqlsSFFTQLQKALGALERI 289
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
356-571 |
1.35e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 356 LEDITLSVDAGQRIAILGRTGCGKSTLLQLLT-RAWD--PQQGEIRFNDVPLSGFSEAALRKTVSVVPQRVHL------- 425
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILHVEQEVVGDDTTALQCVLNTDIERTQLleeeaql 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 426 --------FSATLRDNLLLAAPDASDDTLRAMLEQVglHKLLEddGLNSWLGEG-------------------GRQLSGG 478
Cdd:PLN03073 273 vaqqreleFETETGKGKGANKDGVDKDAVSQRLEEI--YKRLE--LIDAYTAEAraasilaglsftpemqvkaTKTFSGG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 479 ELRRLAIARALLHDAPLMLLDEPTEGLDAtteSQILDLLANVMK-GKTVLMVTHRLrglvNFDQIIVMDNGHIIEQgsha 557
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKwPKTFIVVSHAR----EFLNTVVTDILHLHGQ---- 417
|
250
....*....|....
gi 489955000 558 ELLAKQGRYYQFKQ 571
Cdd:PLN03073 418 KLVTYKGDYDTFER 431
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
468-554 |
2.43e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 468 LGEGGRQLSGGELRRLAIARALLHDAP---LMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRglvnfdqiI 543
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMH--------V 874
|
90
....*....|.
gi 489955000 544 VMDNGHIIEQG 554
Cdd:PRK00635 875 VKVADYVLELG 885
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
470-531 |
9.79e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 9.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955000 470 EGGRQLSGGELR------RLAIARALLHDAPLMLLDEPTEGLDATTESQILDLLANVMKGKT----VLMVTH 531
Cdd:PRK01156 797 EGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISH 868
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
448-562 |
1.15e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 448 AMLEQVGLHKLLEDDGLNSwlgeggrqLSGGELRRLAIARALlhDAPLM----LLDEPTEGLDATTESQILDLLANVM-K 522
Cdd:PRK00635 458 SILIDLGLPYLTPERALAT--------LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRdQ 527
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489955000 523 GKTVLMVTHRLRGLVNFDQIIVMD------NGHIIEQGSHAELLAK 562
Cdd:PRK00635 528 GNTVLLVEHDEQMISLADRIIDIGpgagifGGEVLFNGSPREFLAK 573
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
357-509 |
1.29e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 357 EDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDvplsgfseaalrkTVSV--VPQrvhlfsatLRDNL 434
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-------------TVKLayVDQ--------SRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 435 llaAPDA------SD--DTLramleQVGLHKLleddglNS--WLG----EGGRQ------LSGGELRRLAIARALLHDAP 494
Cdd:PRK11819 400 ---DPNKtvweeiSGglDII-----KVGNREI------PSraYVGrfnfKGGDQqkkvgvLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|....*
gi 489955000 495 LMLLDEPTEGLDATT 509
Cdd:PRK11819 466 VLLLDEPTNDLDVET 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
474-550 |
1.74e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 474 QLSGGELRRLAIARALLHDAPLMLLDEPTEGLDATTESQILDLL-ANVMKGKTVLMVTHRLR---GLVnfDQIIVMDNGH 549
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLInQLVQQGVAIIVISSELPevlGLS--DRVLVMHEGK 482
|
.
gi 489955000 550 I 550
Cdd:PRK13549 483 L 483
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
95-314 |
3.07e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 39.69 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 95 LRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLY---LR--VISPM--VGAFVVIVVVTLGLSFLDVPIALTLG 167
Cdd:cd18548 74 LRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVmmlLRmlVRAPImlIGAIIMAFRINPKLALILLVAIPILA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 168 GIMLMTLIILPPLFYRAGKTTgENLTRLrgeYRQQLT------AwlqgqaeltlFGASKRYRARMENTELNWHEAQRRQS 241
Cdd:cd18548 154 LVVFLIMKKAIPLFKKVQKKL-DRLNRV---VRENLTgirvirA----------FNREDYEEERFDKANDDLTDTSLKAG 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 242 ELTAFSQALMMLIGGIAVIAMLWMASGGV-GGNAQPGPLIALFVFCALAAFeALAPVTGAFQHLGQVIASALRI 314
Cdd:cd18548 220 RLMALLNPLMMLIMNLAIVAILWFGGHLInAGSLQVGDLVAFINYLMQILM-SLMMLSMVFVMLPRASASAKRI 292
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
474-531 |
3.97e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 3.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489955000 474 QLSGGElR-------RLAIARALLH----DAPL--MLLDEPTEGLDATTESQILDLLaNVMKGKTV---LMVTH 531
Cdd:PRK02224 781 QLSGGE-RalfnlslRCAIYRLLAEgiegDAPLppLILDEPTVFLDSGHVSQLVDLV-ESMRRLGVeqiVVVSH 852
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
90-302 |
4.35e-03 |
|
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: 39.39 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 90 RVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLY-------LRVISPMVGAFVVIVVVTLGLSFLdvpi 162
Cdd:cd18575 66 RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVgsslsiaLRNLLLLIGGLVMLFITSPKLTLL---- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 163 altlggIMLMTLIILPPLFYRAGKTtgENLTRLrgeyRQQLTAWLQGQAELTL--------FG----ASKRYRARMENTe 230
Cdd:cd18575 142 ------VLLVIPLVVLPIILFGRRV--RRLSRA----SQDRLADLSAFAEETLsaiktvqaFTredaERQRFATAVEAA- 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489955000 231 lnWHEAQRR---QSELTAFSQALMMLiggiAVIAMLWMASGGV-GGNAQPGPLIAlFVFCAL---AAFEALAPVTGAFQ 302
Cdd:cd18575 209 --FAAALRRiraRALLTALVIFLVFG----AIVFVLWLGAHDVlAGRMSAGELSQ-FVFYAVlaaGSVGALSEVWGDLQ 280
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
368-404 |
4.43e-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: 4.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489955000 368 RIAILGRTGCGKSTLLQLLTRAW-----------DPQQGEIRFNDVPL 404
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKaivsdypgttrDPNEGRLELKGKQI 48
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
87-314 |
5.42e-03 |
|
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: 39.08 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 87 ATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLylrvispmvgafvvivvVTLGLSFLDVPIALTL 166
Cdd:cd18557 63 AGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSA-----------------VTDNLSQLLRNILQVI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 167 GGIMLM-------TLIILP--PLFYRAGKTTGENLTRLRGEYRQQLTA-------WLQGQAELTLFGA----SKRYRARM 226
Cdd:cd18557 126 GGLIILfilswklTLVLLLviPLLLIASKIYGRYIRKLSKEVQDALAKagqvaeeSLSNIRTVRSFSAeekeIRRYSEAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 227 ENTelnwHEAQRRQSELTAFSQALMMLIGGIAVIAMLWMASGGVG-GNAQPGPLIAlFVFCALAAFEALAPVTGAFQHLG 305
Cdd:cd18557 206 DRS----YRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLsGQLTVGELTS-FILYTIMVASSVGGLSSLLADIM 280
|
....*....
gi 489955000 306 QVIASALRI 314
Cdd:cd18557 281 KALGASERV 289
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
353-554 |
5.91e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 353 QNALEDITLSVDAGQRIAILGRTGCGKSTL-------------LQLLTRAWDPQQGEIRFNDVP-LSGFSEAAL--RKTV 416
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDsIEGLSPAIAidQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 417 SVVPqRVHLFSAT-LRDNL-LLAAPDASDDTLRAMLEqVGLHKLLeddglnswLGEGGRQLSGGELRRLAIARAL---Lh 491
Cdd:cd03270 88 SRNP-RSTVGTVTeIYDYLrLLFARVGIRERLGFLVD-VGLGYLT--------LSRSAPTLSGGEAQRIRLATQIgsgL- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 492 DAPLMLLDEPTEGLDATTESQILDLLANVM-KGKTVLMVTHRLRGLVNFDQIIVM------DNGHIIEQG 554
Cdd:cd03270 157 TGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
61-182 |
6.24e-03 |
|
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: 39.03 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 61 LPAAGVRGTAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARFRQGELLNRVVADVDTLDHLYLRVISP 140
Cdd:cd18564 55 LAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLP 134
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489955000 141 MVGAFVVIVVVTLGLSFLDVPIAltlggimLMTLIILPPLFY 182
Cdd:cd18564 135 LLTNLLTLVGMLGVMFWLDWQLA-------LIALAVAPLLLL 169
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
339-531 |
6.95e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 339 LTLSNVTFAYDkqaQNALEDITLSVDAGQRIAILGRTGCGKSTLLQLLTRAWDPQQGEIRFNDVPLSGFSEAALrktvSV 418
Cdd:PRK13541 2 LSLHQLQFNIE---QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955000 419 VPQRVHL-FSATLRDNLLLAAP-DASDDTLRAMLEQVGLHKLLEddglnswlgEGGRQLSGGELRRLAIARALLHDAPLM 496
Cdd:PRK13541 75 IGHNLGLkLEMTVFENLKFWSEiYNSAETLYAAIHYFKLHDLLD---------EKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489955000 497 LLDEPTEGLDATTEsqilDLLAN--VMK---GKTVLMVTH 531
Cdd:PRK13541 146 LLDEVETNLSKENR----DLLNNliVMKansGGIVLLSSH 181
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