|
Name |
Accession |
Description |
Interval |
E-value |
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-570 |
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: 718.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMR 92
Cdd:COG4987 12 PHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLADLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 93 VWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVV 172
Cdd:COG4987 92 VRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 173 VPIFIRAWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMN 252
Cdd:COG4987 172 LPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 253 LAMWTILVMAIIKVEQGELPGVYIAMLALATLSAFEAVTPLPLTFIYLEESMSAAKRLFELAETENYSPSRKDEQFVPKG 332
Cdd:COG4987 252 LAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHM 412
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNAS 492
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 493 VLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQL 570
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-570 |
2.77e-167 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 487.75 E-value: 2.77e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMR 92
Cdd:COG1132 18 PYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 93 VWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIgAAVV 172
Cdd:COG1132 98 RDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLP-LLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 173 VPIFIRAWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMN 252
Cdd:COG1132 177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 253 LAMWTILVMAIIKVEQGEL-PGVYIAMLALATLsAFEAVTPLPLTFIYLEESMSAAKRLFELAETENYSPSRKDEQ-FVP 330
Cdd:COG1132 257 LGLALVLLVGGLLVLSGSLtVGDLVAFILYLLR-LFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVpLPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 331 KGYEIEFNNLHFRYsAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA 410
Cdd:COG1132 336 VRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 HMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKN 490
Cdd:COG1132 415 QIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 491 ASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQL 570
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-569 |
3.15e-158 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 464.30 E-value: 3.15e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 14 HWLPMLWAVLLGFLAVGSNIGLLTTSAYLISRAAqhppVLDLMVAIV--------GVRFFGIARAVFRYLERYFSHDVTF 85
Cdd:PRK11160 14 HWFMLSLGILLAIVTLLASIGLLTLSGWFLSASA----VAGLAGLYSfnymlpaaGVRGAAIGRTAGRYGERLVSHDATF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 86 RVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAF 165
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALTLGGI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 166 FIGAAVVVP-IFIRAwGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAG 244
Cdd:PRK11160 170 LLLLLLLLPlLFYRL-GKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 245 SLTGLCMNLAMWTILVMAIIKVEQGELPGVYIAMLALATLSAFEAVTPLPLTFIYLEESMSAAKRLFELAETENYSPSRK 324
Cdd:PRK11160 249 ALMILANGLTVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQKPEVTFPT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 325 DEQFVPKGYEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYH 404
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 405 QSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDfILTLPEGYDTYVGEGGLKLSGGQRQRVAIA 484
Cdd:PRK11160 409 EAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEK-LLEDDKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVY 564
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRY 567
|
....*
gi 134052199 565 ARMWQ 569
Cdd:PRK11160 568 YQLKQ 572
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-531 |
2.73e-156 |
|
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: 457.98 E-value: 2.73e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 21 AVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIE 100
Cdd:TIGR02868 18 AVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAALRSLGALRVRVYERLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 101 PLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAW 180
Cdd:TIGR02868 98 RQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 181 GRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILV 260
Cdd:TIGR02868 178 ARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 261 MAIIKVEQGELPGVYIAMLALATLSAFEAVTPLPLTFIYLEESMSAAKRLFELAETENYSP---SRKDEQFVPKGYEIEF 337
Cdd:TIGR02868 258 AGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAegsAPAAGAVGLGKPTLEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 338 NNLHFRYsAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQ 417
Cdd:TIGR02868 338 RDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 418 RTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILD 497
Cdd:TIGR02868 417 DAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLD 496
|
490 500 510
....*....|....*....|....*....|....
gi 134052199 498 EVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHL 531
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-311 |
1.34e-124 |
|
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: 367.96 E-value: 1.34e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 25 GFLAVGSNIGLLTTSAYLISRAAQHP---PVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEP 101
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGlaaPTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 102 LATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWG 181
Cdd:cd18585 81 LAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 182 RRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVM 261
Cdd:cd18585 161 KKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 134052199 262 AIIKVEQGELPGVYIAMLALATLSAFEAVTPLPLTFIYLEESMSAAKRLF 311
Cdd:cd18585 241 GAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-569 |
1.56e-122 |
|
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: 377.25 E-value: 1.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGsnIGLLTT--SAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSN 90
Cdd:COG2274 153 RYRRLLLQVLLASLLINL--LALATPlfTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLR 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 91 MRVWFYKAIEPLATSQLMHYHSGDLLSRIvSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAA 170
Cdd:COG2274 231 LSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYV 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 171 VVVpIFIRAWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLC 250
Cdd:COG2274 310 LLG-LLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 251 MNLAMWTILVMAIIKVEQGEL-PGVYIAMLALATlSAFEAVTPLPLTFIYLEESMSAAKRLFEL--AETENYSPSRKDEQ 327
Cdd:COG2274 389 QQLATVALLWLGAYLVIDGQLtLGQLIAFNILSG-RFLAPVAQLIGLLQRFQDAKIALERLDDIldLPPEREEGRSKLSL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 328 FVPKGyEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK 407
Cdd:COG2274 468 PRLKG-DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAI 487
Cdd:COG2274 547 LRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARAL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 488 LKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
..
gi 134052199 568 WQ 569
Cdd:COG2274 707 VQ 708
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-562 |
1.33e-119 |
|
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: 364.85 E-value: 1.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGSNIGLLTTSAYLISRA-AQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNM 91
Cdd:COG4988 14 GARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLiIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 92 RVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAffigAAV 171
Cdd:COG4988 94 RRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLV----TAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 172 VVPIFIRAWG---RRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTG 248
Cdd:COG4988 170 LIPLFMILVGkgaAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSSAVLE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 249 LCMNLAMWTILVMAIIKVEQGEL---PGVYIAMLA------LATL-SAFEAVTplpltfiyleESMSAAKRLFELAETEN 318
Cdd:COG4988 250 FFASLSIALVAVYIGFRLLGGSLtlfAALFVLLLApefflpLRDLgSFYHARA----------NGIAAAEKIFALLDAPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 319 YSPSRKDEQFVPKGY-EIEFNNLHFRYsAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGG 397
Cdd:COG4988 320 PAAPAGTAPLPAAGPpSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 398 REVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQ 477
Cdd:COG4988 399 VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 478 RQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
....*
gi 134052199 558 LEQGG 562
Cdd:COG4988 559 LAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-570 |
5.78e-109 |
|
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: 338.72 E-value: 5.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLD--LMVAIVGVRFFGIAR---AVFRYLeryfsHDVTF-R 86
Cdd:COG5265 30 PYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAalLVVPVGLLLAYGLLRllsVLFGEL-----RDALFaR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 87 VLSNmrvwfykAIEPLATSQLMHYHSGDL----------LSRI----VSDVETLKNFYLRVLSPPLV-ALLTLGVVFFLl 151
Cdd:COG5265 105 VTQR-------AVRRLALEVFRHLHALSLrfhlerqtggLSRDiergTKGIEFLLRFLLFNILPTLLeIALVAGILLVK- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 152 acFDLRMAFIFLAFfIGAAVVVPIFIRAW--GRRSGQGILGSKAqlNTCLVDGiqgmtdLL------SFDQQGRQLEKID 223
Cdd:COG5265 177 --YDWWFALITLVT-VVLYIAFTVVVTEWrtKFRREMNEADSEA--NTRAVDS------LLnyetvkYFGNEAREARRYD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 224 KTNDNLS----KLQGRLAKINglAGSltGLCMNLAMWTILVMAIIKVEQGELpgvyiamlalaTLSAFEAVT-------- 291
Cdd:COG5265 246 EALARYEraavKSQTSLALLN--FGQ--ALIIALGLTAMMLMAAQGVVAGTM-----------TVGDFVLVNayliqlyi 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 292 PLP-LTFIYLE--ESMSAAKRLFELAETENYSPSRKDEQ-FVPKGYEIEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAI 367
Cdd:COG5265 311 PLNfLGFVYREirQALADMERMFDLLDQPPEVADAPDAPpLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 368 VGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAAR 447
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAAR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 448 RARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVI 527
Cdd:COG5265 470 AAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 134052199 528 SHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQL 570
Cdd:COG5265 550 AHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-569 |
6.03e-105 |
|
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: 315.32 E-value: 6.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQ 569
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-568 |
7.51e-103 |
|
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: 309.93 E-value: 7.51e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMW 568
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
67-573 |
3.33e-92 |
|
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: 294.32 E-value: 3.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 67 IARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLknfyLRVLSPPLVALL--TL 144
Cdd:TIGR02203 65 VLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQV----ASAATDAFIVLVreTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 145 GVVFFLLACFDL--RMAFIFLAFFIGAAVVVPIFIRAWgRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKI 222
Cdd:TIGR02203 141 TVIGLFIVLLYYswQLTLIVVVMLPVLSILMRRVSKRL-RRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 223 DKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQ-----GELPGVYIAMLALatlsaFEAVTPLPLTF 297
Cdd:TIGR02203 220 DAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAgsltaGDFTAFITAMIAL-----IRPLKSLTNVN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 298 IYLEESMSAAKRLFELAETenysPSRKDEQFVPKGY---EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAG 374
Cdd:TIGR02203 295 APMQRGLAAAESLFTLLDS----PPEKDTGTRAIERargDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 375 KSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPG-ASEKEMIQAARRARIHD 453
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 454 FILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVG 533
Cdd:TIGR02203 451 FVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLST 530
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 134052199 534 LECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQLSVR 573
Cdd:TIGR02203 531 IEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQFR 570
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-570 |
1.49e-90 |
|
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: 278.65 E-value: 1.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRY-SAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQL 570
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-562 |
3.89e-89 |
|
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: 274.49 E-value: 3.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:cd03254 2 EIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGG 562
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
52-570 |
3.98e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 286.53 E-value: 3.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 52 VLDLM-VAIVGVRFFgiaRAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFY 130
Cdd:PRK11176 63 VLKWMpLVVIGLMIL---RGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 131 LRVL------SPPLVALLT--------LGVVFFLLAcfdlrmafIFLAFFIGaaVVVPIFirawgRRSGQGILGSKAQLN 196
Cdd:PRK11176 140 SGALitvvreGASIIGLFImmfyyswqLSLILIVIA--------PIVSIAIR--VVSKRF-----RNISKNMQNTMGQVT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 197 TCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGEL-PG-- 273
Cdd:PRK11176 205 TSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLtAGti 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 274 --VYIAMLALatLSAFEAVTPLPLTFiylEESMSAAKRLFEL--AETENYSPSRKDEQfvPKGyEIEFNNLHFRYSAKDP 349
Cdd:PRK11176 285 tvVFSSMIAL--MRPLKSLTNVNAQF---QRGMAACQTLFAIldLEQEKDEGKRVIER--AKG-DIEFRNVTFTYPGKEV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 350 WILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVREN 429
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 ILLARPGA-SEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:PRK11176 437 IAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 509 REIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQL 570
Cdd:PRK11176 517 RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKM 578
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-543 |
7.48e-75 |
|
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: 247.59 E-value: 7.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 16 LPMLWAVLLGFLAVGSNIGLLTTSAYLISRA-AQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVW 94
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLiSAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 95 FYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLspPLVALLTLGVVFFLLACF--DLRMAFIFLaffiGAAVV 172
Cdd:TIGR02857 83 LLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYL--PQLVLAVIVPLAILAAVFpqDWISGLILL----LTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 173 VPIFIRAWGRRS---GQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLtgl 249
Cdd:TIGR02857 157 IPIFMILIGWAAqaaARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAV--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 250 cmnLAMWTILVMAIIKVEQGElpGVYIAMLALAT-----LSAFEAVTPL-PLTFIYLE--ESMSAAKRLFE-LAETENYS 320
Cdd:TIGR02857 234 ---LELFATLSVALVAVYIGF--RLLAGDLDLATglfvlLLAPEFYLPLrQLGAQYHAraDGVAAAEALFAvLDAAPRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 321 PSRKDeQFVPKGYEIEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV 400
Cdd:TIGR02857 309 AGKAP-VTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 401 RDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQR 480
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQR 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVL 543
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-567 |
1.48e-74 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 248.34 E-value: 1.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 19 LWAVLLGFLAVGSNIGLLTTSAYLISRAAQ----------------HPPVLDLMVAIVGVRFFGIARAVF--RYLERyFS 80
Cdd:PRK13657 6 LYARVLQYLGAEKRLGILLAVANVLLAAATfaepilfgriidaisgKGDIFPLLAAWAGFGLFNIIAGVLvaRHADR-LA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 81 HDvtfRVLSNMRVWFYKAIE-PLATSQLMHyhSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMA 159
Cdd:PRK13657 85 HR---RRLAVLTEYFERIIQlPLAWHSQRG--SGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 160 FIFLAFfigaAVVVPIFIRAWGRR--SGQG-ILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRL 236
Cdd:PRK13657 160 LVLVVL----GIVYTLITTLVMRKtkDGQAaVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 237 AKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGELP-GVYIAMLALATLsafeAVTPLPLTFIYLEESMSAAKRLFELAE 315
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRvGEVVAFVGFATL----LIGRLDQVVAFINQVFMAAPKLEEFFE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 316 TENYSPSRKDEQFVP-----KGyEIEFNNLHFRYSAKDPWIlRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQR 390
Cdd:PRK13657 312 VEDAVPDVRDPPGAIdlgrvKG-AVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 391 GSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGG 470
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 471 LKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVE 550
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
570
....*....|....*..
gi 134052199 551 KGTHSQLLEQGGVYARM 567
Cdd:PRK13657 550 SGSFDELVARGGRFAAL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
335-570 |
1.64e-74 |
|
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: 237.00 E-value: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQL 570
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-547 |
3.72e-72 |
|
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: 228.42 E-value: 3.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENIllarpgasekemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-567 |
8.59e-72 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 240.90 E-value: 8.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 306 AAKRLFELAETENYSPSRKDEQFVP-KGYEIEFNNLHFrYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG 384
Cdd:PRK11174 320 AAESLVTFLETPLAHPQQGEKELASnDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 385 FFDYQrGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDT 464
Cdd:PRK11174 399 FLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 465 YVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLV 544
Cdd:PRK11174 478 PIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
250 260
....*....|....*....|...
gi 134052199 545 EGKVVEKGTHSQLLEQGGVYARM 567
Cdd:PRK11174 558 DGQIVQQGDYAELSQAGGLFATL 580
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
111-567 |
4.55e-67 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 230.99 E-value: 4.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 111 HSGDLLSRIvsdveTLKNFYLRVLSPPLVALLT--LGVVFFLL--ACFDLRMAFIFLAFfigAAVVVPIFIRAWGRR--S 184
Cdd:TIGR03796 249 HAGDIASRV-----QLNDQVAEFLSGQLATTALdaVMLVFYALlmLLYDPVLTLIGIAF---AAINVLALQLVSRRRvdA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 185 GQGILGSKAQLNTCLVDGIQGMTDL----LSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLamwtILV 260
Cdd:TIGR03796 321 NRRLQQDAGKLTGVAISGLQSIETLkasgLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSAL----ILV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 261 MAIIKVEQGELP-GVYIAMLALATlSAFEAVTPLPLTFIYLEESMSAAKRL--------FELAETENYSPSRKDEQFVPK 331
Cdd:TIGR03796 397 VGGLRVMEGQLTiGMLVAFQSLMS-SFLEPVNNLVGFGGTLQELEGDLNRLddvlrnpvDPLLEEPEGSAATSEPPRRLS 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 332 GYeIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAH 411
Cdd:TIGR03796 476 GY-VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANS 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNA 491
Cdd:TIGR03796 555 VAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNP 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 492 SVLILDEVTAGLDPVVGREIMQDLFQlmKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
113-567 |
2.82e-63 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 220.75 E-value: 2.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 113 GDLLSRIVSDVETLKN---FYLRVLSPPLVALLTLgVVFFLLACFDLRM-AFIFLAFFIGAAVVVPIFIRAWGRRSGQGI 188
Cdd:TIGR00958 258 GELTSRLSSDTQTMSRslsLNVNVLLRNLVMLLGL-LGFMLWLSPRLTMvTLINLPLVFLAEKVFGKRYQLLSEELQEAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 189 lgskAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQ 268
Cdd:TIGR00958 337 ----AKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLT 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 269 GELPGVYIAMLALATLSAFEAVTPLPLTFIYLEESMSAAKRLFELAETENYSPSrkDEQFVPKGYE--IEFNNLHFRY-S 345
Cdd:TIGR00958 413 GKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEglIEFQDVSFSYpN 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 346 AKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNAT 425
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGS 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 426 VRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDP 505
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 506 vvgrEIMQDLFQLM--KDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:TIGR00958 651 ----ECEQLLQESRsrASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
55-572 |
3.17e-63 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 220.38 E-value: 3.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 55 LMVAIVGVRFFGIARAVFRylERYFSHdVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRiVSDVETLKNFY---- 130
Cdd:TIGR01846 181 LALAMLAVAIFEPALGGLR--TYLFAH-LTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVAR-VRELEQIRNFLtgsa 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 131 LRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFirawgRRSGQGILGSKAQLNTCLVDGIQGMTDLL 210
Cdd:TIGR01846 257 LTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPIL-----RKRVEDKFERSAAATSFLVESVTGIETIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 211 SFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGEL-PGVYIAMLALATlsafEA 289
Cdd:TIGR01846 332 ATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALsPGQLVAFNMLAG----RV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 290 VTP-LPLTFIY--LEESMSAAKRLFELAE--TENYSPSRKDeqfVPK-GYEIEFNNLHFRYSAKDPWILRDVSFTIPQGR 363
Cdd:TIGR01846 408 TQPvLRLAQLWqdFQQTGIALERLGDILNspTEPRSAGLAA---LPElRGAITFENIRFRYAPDSPEVLSNLNLDIKPGE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 364 RLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMI 443
Cdd:TIGR01846 485 FIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 444 QAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKT 523
Cdd:TIGR01846 565 HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRT 644
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 134052199 524 SLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQLSV 572
Cdd:TIGR01846 645 VIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-552 |
4.06e-63 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 206.67 E-value: 4.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKG 552
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
60-567 |
3.33e-62 |
|
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: 217.68 E-value: 3.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 60 VGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIvSDVETLKNFYLRVLSPPLV 139
Cdd:TIGR01193 200 IGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRF-TDASSIIDALASTILSLFL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 140 ALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWGRRSgQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQL 219
Cdd:TIGR01193 279 DMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLN-HDAMQANAVLNSSIIEDLNGIETIKSLTSEAERY 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 220 EKIDKTNDNLSKLQGRLAK---INGLAGSLTGLCMNLA-MW--TILVMAIiKVEQGELpgvyIAMLALatLSAFeaVTPL 293
Cdd:TIGR01193 358 SKIDSEFGDYLNKSFKYQKadqGQQAIKAVTKLILNVViLWtgAYLVMRG-KLTLGQL----ITFNAL--LSYF--LTPL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 294 PlTFIYLEESMSAAK----RLFE--LAETENYSPSRKDEQFVPKGyEIEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAI 367
Cdd:TIGR01193 429 E-NIINLQPKLQAARvannRLNEvyLVDSEFINKKKRTELNNLNG-DIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTI 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 368 VGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILL-ARPGASEKEMIQAA 446
Cdd:TIGR01193 506 VGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAAC 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 447 RRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQlMKDKTSLV 526
Cdd:TIGR01193 586 EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIF 664
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 134052199 527 ISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:TIGR01193 665 VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
117-560 |
8.05e-60 |
|
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: 208.06 E-value: 8.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 117 SRIVSDVETLKNFylrVLSPPLVALLTLG-VVFFLLACFDLR-----MAFIFLAFFIGAAVVVPIFIRAWGRRSGQGILG 190
Cdd:COG4618 116 AQALRDLDTLRQF---LTGPGLFALFDLPwAPIFLAVLFLFHpllglLALVGALVLVALALLNERLTRKPLKEANEAAIR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 191 SKAQLNTCL--VDGIQ--GMTDLLSFDQQGRQLEKIDktndnlskLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKV 266
Cdd:COG4618 193 ANAFAEAALrnAEVIEamGMLPALRRRWQRANARALA--------LQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 267 EQGEL-PGVYIA---MLALAtLSAFEAVTPLPLTFIyleESMSAAKRLFELAETenySPSRKD--EQFVPKGyEIEFNNL 340
Cdd:COG4618 265 IQGEItPGAMIAasiLMGRA-LAPIEQAIGGWKQFV---SARQAYRRLNELLAA---VPAEPErmPLPRPKG-RLSVENL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 341 HFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTH 420
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 LFNATVRENIllAR-PGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:COG4618 417 LFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 500 TAGLDPvVGREIMQDLFQLMKD--KTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG4618 495 NSNLDD-EGEAALAAAIRALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
124-571 |
5.69e-57 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 200.89 E-value: 5.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 124 ETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIgaavvVPIFIRAW--GR-RSGQG-ILGSKAQLNTCL 199
Cdd:TIGR01192 124 ETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGI-----LYILIAKLvmQRtKNGQAaVEHHYHNVFKHV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 200 VDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGELP-GVYIAM 278
Cdd:TIGR01192 199 SDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSvGEVIAF 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 279 LALATL-------------SAFEAVTPLPlTFIYLEESMSAAKRLFELAETENYSPsrkdeqfvpkgyEIEFNNLHFRYs 345
Cdd:TIGR01192 279 IGFANLligrldqmsgfitQIFEARAKLE-DFFDLEDSVFQREEPADAPELPNVKG------------AVEFRHITFEF- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 346 AKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNAT 425
Cdd:TIGR01192 345 ANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRS 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 426 VRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDP 505
Cdd:TIGR01192 425 IRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDV 504
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 506 VVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMWQLS 571
Cdd:TIGR01192 505 ETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-552 |
7.57e-57 |
|
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: 188.68 E-value: 7.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYhQSKLMAHMAV 414
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENIllarpgasekemiqaarrarihdfiltlpegydtyvgegGLKLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKG 552
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
341-568 |
8.08e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 200.32 E-value: 8.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 341 HFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTH 420
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 LFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVT 500
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 501 AGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARMW 568
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMY 547
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
335-548 |
1.99e-56 |
|
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: 189.22 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAK-DPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKV 548
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-570 |
3.04e-56 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 199.17 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGSNIGLLTTSAYLISR--AAQHPP---VLDLMVAIVGVRFFGiarAVFRYLERYFSHDVTFRV 87
Cdd:PRK10790 20 PWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNmvAKGNLPlglVAGLAAAYVGLQLLA---AGLHYAQSLLFNRAAVGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 88 LSNMRVWFYKAI--EPLAT--SQLMhyhsGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFL 163
Cdd:PRK10790 97 VQQLRTDVMDAAlrQPLSAfdTQPV----GQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 164 AFFIGAAVVVPIFIRAWG---RRsgqgILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDnlSKLQGRLAKIN 240
Cdd:PRK10790 173 MIFPAVLVVMVIYQRYSTpivRR----VRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASR--SHYMARMQTLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 241 glagsLTGLCMN--LAMWTILVMAIIKVEQGELPgvyIAMLALATLSAF--------EAVTPLPLTFIYLEESMSAAKRL 310
Cdd:PRK10790 247 -----LDGFLLRplLSLFSALILCGLLMLFGFSA---SGTIEVGVLYAFisylgrlnEPLIELTTQQSMLQQAVVAGERV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 311 FEL--AETENYSPsrkDEQFVPKGyEIEFNNLHFRYSaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDY 388
Cdd:PRK10790 319 FELmdGPRQQYGN---DDRPLQSG-RIDIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 389 QRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPgASEKEMIQAARRARIHDFILTLPEGYDTYVGE 468
Cdd:PRK10790 394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 469 GGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLfQLMKDKTSL-VISHHLVGLECMDEILVLVEGK 547
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLvVIAHRLSTIVEADTILVLHRGQ 551
|
570 580
....*....|....*....|...
gi 134052199 548 VVEKGTHSQLLEQGGVYARMWQL 570
Cdd:PRK10790 552 AVEQGTHQQLLAAQGRYWQMYQL 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-553 |
1.57e-53 |
|
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: 181.54 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNATVRENIllaRP--GASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNA 491
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 492 SVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGT 553
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
110-567 |
7.22e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 180.15 E-value: 7.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 110 YHSGDLLSRI--VSDV-ETLKNFYLRVLSPPLVALLTLGVVFFllacFDLRMAFIFLAFFIgAAVVVPIFIRAWGRRSGQ 186
Cdd:TIGR03797 230 YSTGDLASRAmgISQIrRILSGSTLTTLLSGIFALLNLGLMFY----YSWKLALVAVALAL-VAIAVTLVLGLLQVRKER 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 187 GILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTglcmnlAMWTILVMAIIKV 266
Cdd:TIGR03797 305 RLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN------AVLPVLTSAALFA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 267 EQGELPGVyiAMLALATLSAF--------EAVTPLPLTFIyleESMSA------AKRLFElAETENyspsrkDEQFVPKG 332
Cdd:TIGR03797 379 AAISLLGG--AGLSLGSFLAFntafgsfsGAVTQLSNTLI---SILAViplwerAKPILE-ALPEV------DEAKTDPG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 Y---EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLM 409
Cdd:TIGR03797 447 KlsgAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQRTHLFNATVRENILLARPgASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILK 489
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 490 NASVLILDEVTAGLDPVVGREIMQDLFQLmkDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
117-560 |
3.52e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 176.00 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 117 SRIVSDVETLKNFylrVLSPPLVALLTLG-VVFFLLACFDLRMAFIFLAffIGAAVVvpIFIRAW-GRRSGQGILGSKAQ 194
Cdd:TIGR01842 102 LQALRDLDQLRQF---LTGPGLFAFFDAPwMPIYLLVCFLLHPWIGILA--LGGAVV--LVGLALlNNRATKKPLKEATE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 195 LNtclvdgIQGMTDLlsfDQQGRQLEKIDKTN--DNLSKLQGRL----AKINGLAGSLTGLCMNLA-----MWTILVMAI 263
Cdd:TIGR01842 175 AS------IRANNLA---DSALRNAEVIEAMGmmGNLTKRWGRFhskyLSAQSAASDRAGMLSNLSkyfriVLQSLVLGL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 264 ---IKVEQGELPGVYIA---MLALAtLSAFEavtplplTFIYLEESMSAA----KRLFELAeteNYSPSRKDEQFVPK-G 332
Cdd:TIGR01842 246 gayLAIDGEITPGMMIAgsiLVGRA-LAPID-------GAIGGWKQFSGArqayKRLNELL---ANYPSRDPAMPLPEpE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHM 412
Cdd:TIGR01842 315 GHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNAS 492
Cdd:TIGR01842 395 GYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 493 VLILDEVTAGLDPVVGREIMQDLFQLMKDK-TSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-547 |
8.00e-48 |
|
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: 165.72 E-value: 8.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKD---PWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmah 411
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLFNATVRENILLARPGASE--KEMIQAArrARIHDFILtLPEGYDTYVGEGGLKLSGGQRQRVAIARAILK 489
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKAC--ALEPDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 490 NASVLILDEVTAGLDPVVGREIMQDLFQ--LMKDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCILglLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-562 |
5.09e-47 |
|
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: 164.65 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYhQSKLMAHMAV 414
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLArpgASEKEMIQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNA 491
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYF---AELYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 492 SVLILDEVTAGLDpVVGREIMQDLFQLMKD--KTSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLLEQGG 562
Cdd:COG4555 152 KVLLLDEPTNGLD-VMARRLLREILRALKKegKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-560 |
7.16e-47 |
|
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: 164.04 E-value: 7.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQ--RTHLFNATVRENIL--LARPGASEKEMIQAARRArihdfiLTLpegydtyVGEGGLK------LSGGQRQRVAIA 484
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAfgPENLGLPREEIRERVEEA------LEL-------VGLEHLAdrppheLSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLV-ISHHL--VgLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIiVTHDLdlV-AELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-560 |
8.14e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.08 E-value: 8.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyHQSKLMAHMAV 414
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLArpgASEKEMIQAARRARIHDFI--LTLPEGYDTYVGegglKLSGGQRQRVAIARAILKNA 491
Cdd:COG1131 78 VPQEPALYpDLTVRENLRFF---ARLYGLPRKEARERIDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 492 SVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLvgLECM----DEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHY--LEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-547 |
5.28e-44 |
|
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: 155.70 E-value: 5.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 336 EFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVV 415
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 416 AQ--RTHLFNATVRENILLARP--GASEKEMIQAARRArIHDFILTLPEGYDTYvgegglKLSGGQRQRVAIARAILKNA 491
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEA-LELVGLEGLRDRSPF------TLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 492 SVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHLVGL-ECMDEILVLVEGK 547
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-560 |
8.54e-44 |
|
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: 163.15 E-value: 8.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA- 410
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 --HMAVVAQR-THLFNA--TVRENIllARPGASEKEMIQAARRARIHDfILT---LPEGY-DTYVGEgglkLSGGQRQRV 481
Cdd:COG1123 341 rrRVQMVFQDpYSSLNPrmTVGDII--AEPLRLHGLLSRAERRERVAE-LLErvgLPPDLaDRYPHE----LSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPVVGREIMqDLFQLMKDK---TSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQIL-NLLRDLQRElglTYLFISHDLaVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
...
gi 134052199 558 LEQ 560
Cdd:COG1123 493 FAN 495
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-548 |
9.14e-44 |
|
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: 154.96 E-value: 9.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDP--WILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA-- 410
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 --HMAVVAQRTHLFNA-TVRENILLARPGASEKemiQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIAR 485
Cdd:cd03255 81 rrHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLerVGLGDRLNHYPSE----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHLVGLECMDEILVLVEGKV 548
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-560 |
1.00e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 160.07 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ---RGSLQLGGREVRDYHQSKLMAH 411
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQ--RTHLFNATVRENIL--LARPGASEKEMIQAARRA--RIHdfiltLPEGYDTYVGEgglkLSGGQRQRVAIAR 485
Cdd:COG1123 85 IGMVFQdpMTQLNPVTVGDQIAeaLENLGLSRAEARARVLELleAVG-----LERRLDRYPHQ----LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-558 |
2.44e-42 |
|
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: 152.51 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHL-FNATVRENILLAR---------PGASEKEMIQAA-RRARIHDFIltlpegyDTYVGEgglkLSGGQRQRVAI 483
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHLA-------DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQL--MKDKTSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-548 |
7.38e-42 |
|
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: 148.52 E-value: 7.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENIllarpgasekemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQL-MKDKTSLVISHHLVGLECMDEILVLVEGKV 548
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-501 |
1.20e-41 |
|
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: 147.02 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNA-TVRENI 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 431 LLarpGASEKEMIQAARRARIHDFILTLPEGY--DTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTA 501
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-548 |
2.31e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.77 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQsklmaHMAV 414
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-----RIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHL---FNATVRENI---------LLARPGASEKEMIQAA-RRARIHDFIltlpegyDTYVGEgglkLSGGQRQRV 481
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVlmgrygrrgLFRRPSRADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPvVGREIMQDLFQLMKD--KTSLVISHHL-VGLECMDEILVLVEGKV 548
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDA-ATEEALYELLRELRRegKTILVVTHDLgAVREYFDRVLLLNRGLV 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-550 |
3.21e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDP--WILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA-- 410
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 --HMAVVAQRTHLF-NATVRENILLarP----GASEKEmiqaaRRARIHDfILT---LPEGYDTYVGEgglkLSGGQRQR 480
Cdd:COG1136 85 rrHIGFVFQFFNLLpELTALENVAL--PlllaGVSRKE-----RRERARE-LLErvgLGDRLDHRPSQ----LSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHLVGLECMDEILVLVEGKVVE 550
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-559 |
5.53e-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: 145.51 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---H 411
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLFNA-TVRENI---LLARPGASEKEMIQAARRArihdfiLT---LPEGYDTYVGEgglkLSGGQRQRVAIA 484
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVafpLREHTDLSEAEIRELVLEK------LElvgLPGAADKMPSE----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMqDLFQLMKDK---TSLVISHHLVGL-ECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVID-ELIRELRDElglTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-559 |
9.32e-40 |
|
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: 145.33 E-value: 9.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW--ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHM 412
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHL-FNA--TVREniLLARPGASEKEMIQAARRARIHDfILTLPEGY-DTYVGEgglkLSGGQRQRVAIARAIL 488
Cdd:COG1124 82 QMVFQDPYAsLHPrhTVDR--ILAEPLRIHGLPDREERIAELLE-QVGLPPSFlDRYPHQ----LSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 489 KNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLLE 559
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
335-552 |
3.10e-39 |
|
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: 143.03 E-value: 3.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW--ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV---RDYHQSKLM 409
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQrtHLFNA-----TVRENI---LLARPGASEKEmiQAARRARIHDFILTLPEGY-DTYVGEgglkLSGGQRQR 480
Cdd:cd03257 82 KEIQMVFQ--DPMSSlnprmTIGEQIaepLRIHGKLSKKE--ARKEAVLLLLVGVGLPEEVlNRYPHE----LSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMqDLFQLMKDK---TSLVISHHL-VGLECMDEILVLVEGKVVEKG 552
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQIL-DLLKKLQEElglTLLFITHDLgVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-557 |
4.86e-39 |
|
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: 143.03 E-value: 4.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---H 411
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLFNA-TVRENI--LLARPGASEKEMIQAARRARIHdfILTLPEGYDTYVGEgglkLSGGQRQRVAIARAIL 488
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafPLREHTRLSEEEIREIVLEKLE--AVGLRGAEDLYPAE----LSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 489 KNASVLILDEVTAGLDPVVGREImQDLFQLMKDK---TSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVI-DDLIRSLKKElglTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-548 |
5.73e-39 |
|
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: 140.61 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyHQSKLMAHMAV 414
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENillarpgasekemiqaarrarihdfiltlpegydtyvgeggLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03230 78 LPEEPSLYeNLTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHLVGLE--CmDEILVLVEGKV 548
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAErlC-DRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
335-549 |
6.91e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.89 E-value: 6.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAH--- 411
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENILLARPGAS----------EKEMIQAARRA--R--IHDFILTLPEgydtyvgegglKLSGG 476
Cdd:COG3638 82 IGMIFQQFNLVpRLSVLTNVLAGRLGRTstwrsllglfPPEDRERALEAleRvgLADKAYQRAD-----------QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 477 QRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQL-MKDKTSLVISHHLVGL--ECMDEILVLVEGKVV 549
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLarRYADRIIGLRDGRVV 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
330-553 |
7.32e-38 |
|
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: 138.70 E-value: 7.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 330 PKGYEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLM 409
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQRTHLFNATVRENilLARPGASEKEMIQAARRarihdfiltlpegydtyVGEGGLKLSGGQRQRVAIARAILK 489
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSN--LDPFDEYSDEEIYGALR-----------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 490 NASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGT 553
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-550 |
1.52e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.26 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---H 411
Cdd:COG2884 2 IRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHL-FNATVRENILLarP----GASEKEMiqaarRARIHDfILT---LPEGYDTYVGEgglkLSGGQRQRVAI 483
Cdd:COG2884 81 IGVVFQDFRLlPDRTVYENVAL--PlrvtGKSRKEI-----RRRVRE-VLDlvgLSDKAKALPHE----LSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHlvGLECMDE----ILVLVEGKVVE 550
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH--DLELVDRmpkrVLELEDGRLVR 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
300-567 |
1.04e-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: 146.63 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 300 LEESMSAAKRLFELAETENYSPSRKDEQFVPKGY----EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGK 375
Cdd:TIGR00957 1246 METNIVAVERLKEYSETEKEAPWQIQETAPPSGWpprgRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGK 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 376 STLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENiLLARPGASEKEMIQAARRARIHDFI 455
Cdd:TIGR00957 1326 SSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN-LDPFSQYSDEEVWWALELAHLKTFV 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 456 LTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLE 535
Cdd:TIGR00957 1405 SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM 1484
|
250 260 270
....*....|....*....|....*....|..
gi 134052199 536 CMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:TIGR00957 1485 DYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-529 |
1.46e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVRENIL----LARPGASEKEMIQAARRARIHDFILTLPEGydtyvgegglKLSGGQRQRVAIARAILKN 490
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDILDKPVE----------RLSGGERQRLALIRALLLQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 134052199 491 ASVLILDEVTAGLDPvVGREIMQDLFQLM---KDKTSLVISH 529
Cdd:COG4619 149 PDVLLLDEPTSALDP-ENTRRVEELLREYlaeEGRAVLWVSH 189
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
335-561 |
1.65e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 136.79 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyhQSKLMA---H 411
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEirkK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQR--THLFNATVR-------ENIllarpGASEKEMIQ----AARRARIHDFILTLPegydtyvgeggLKLSGGQR 478
Cdd:TIGR04520 79 VGMVFQNpdNQFVGATVEddvafglENL-----GVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 479 QRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQ 556
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEegITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
|
....*
gi 134052199 557 LLEQG 561
Cdd:TIGR04520 223 IFSQV 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-558 |
4.16e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.88 E-value: 4.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYsakDPWILRdVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlmAHMAV 414
Cdd:COG3840 2 LRLDDLTYRY---GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNA-TVRENILLA-RPG----ASEKE-MIQAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARAI 487
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPGlkltAEQRAqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 488 LKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLL 558
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALL 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-547 |
9.00e-36 |
|
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: 131.21 E-value: 9.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 336 EFNNLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVV 415
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 416 AQrthlfnatvrenillarpgasekemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVLI 495
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 496 LDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHL-VGLECMDEILVLVEGK 547
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-529 |
1.06e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.45 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAK--DPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHqsklmAHM 412
Cdd:COG1116 8 LELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLFN-ATVRENILLarpGASEKEMIQAARRARIHDFI----LtlpEGY-DTYVGEgglkLSGGQRQRVAIARA 486
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVAL---GLELRGVPKAERRERARELLelvgL---AGFeDAYPHQ----LSGGMRQRVAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 134052199 487 ILKNASVLILDEVTAGLDPVVgREIMQDLfqLMK-----DKTSLVISH 529
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALT-RERLQDE--LLRlwqetGKTVLFVTH 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-559 |
1.28e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQR--THLFNATVRENILLARpgasEKEMIQaarRARIHDFILTLPE--GYDTYVGEGGLKLSGGQRQRVAIARAILKN 490
Cdd:PRK13632 88 IFQNpdNQFIGATVEDDIAFGL----ENKKVP---PKKMKDIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 491 ASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVIS--HHLVGLECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-567 |
1.53e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQR--THLFNATVRENIL--LARPGASEKEMI----QAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARA 486
Cdd:PRK13635 86 VFQNpdNQFVGATVQDDVAfgLENIGVPREEMVervdQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 487 ILKNASVLILDEVTAGLDPvVGREIMQDLFQLMKDK---TSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGV 563
Cdd:PRK13635 155 LALQPDIIILDEATSMLDP-RGRREVLETVRQLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
....
gi 134052199 564 YARM 567
Cdd:PRK13635 234 LQEI 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-558 |
1.74e-35 |
|
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: 133.09 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLH--FRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA-- 410
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 -HMAVVAQRTHLFNA-TVRENILLARPGASEKemiQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARA 486
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEIAGVP---KAEIEERVLELLelVGLEDKADAYPAQ----LSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 487 ILKNASVLILDEVTAGLDPVVGREIMQDLFQLMK--DKTSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMeVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-529 |
2.89e-35 |
|
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: 131.83 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW--ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHqsklmAHM 412
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLFN-ATVRENILLarpGASEKEMIQAARRARIHDFILT--LPEGYDTYVGEgglkLSGGQRQRVAIARAILK 489
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVAL---GLELQGVPKAEARERAEELLELvgLSGFENAYPHQ----LSGGMRQRVALARALAV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 134052199 490 NASVLILDEVTAGLDPVVgREIMQDLfqLMK-----DKTSLVISH 529
Cdd:cd03293 149 DPDVLLLDEPFSALDALT-REQLQEE--LLDiwretGKTVLLVTH 190
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
351-559 |
4.98e-35 |
|
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: 131.40 E-value: 4.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAH-MAVVAQRTHLF-NATVRE 428
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFpELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILL-ARPGASEKEmiqAARRARIHDFILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVV 507
Cdd:cd03224 95 NLLLgAYARRRAKR---KARLERVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 508 GREIMQDLFQLMKDKTSLVISHHLVG--LECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVEQNARfaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
293-565 |
5.34e-35 |
|
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: 141.24 E-value: 5.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 293 LPLTFIYLEESMSAAKRLFELAETENYSPSRKDEQFVPKG--YEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGP 370
Cdd:TIGR00957 593 LPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGegNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQ 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 371 SGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmahMAVVAQRTHLFNATVRENILLARPGASE--KEMIQAArr 448
Cdd:TIGR00957 673 VGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKyyQQVLEAC-- 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 449 ARIHDFILtLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLF---QLMKDKTSL 525
Cdd:TIGR00957 738 ALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRI 816
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 134052199 526 VISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYA 565
Cdd:TIGR00957 817 LVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-560 |
7.67e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 131.27 E-value: 7.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTL---ANLLLgffDYQRGSLQLGGREVRDYHQS--KLM 409
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLE---EPDSGTITVDGEDLTDSKKDinKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQRTHLF-NATVRENILLArP----GASEKEMIQAARR--ARIHdfiltLPEGYDTYVGEgglkLSGGQRQRVA 482
Cdd:COG1126 77 RKVGMVFQQFNLFpHLTVLENVTLA-PikvkKMSKAEAEERAMEllERVG-----LADKADAYPAQ----LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 483 IARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFarEVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-547 |
8.00e-35 |
|
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: 129.23 E-value: 8.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQS--KLMAHM 412
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLF-NATVRENILLArpgasekemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNA 491
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 492 SVLILDEVTAGLDPVVGREI---MQDLFQLMKdKTSLVISHHLVGLECM-DEILVLVEGK 547
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVralLKSLQAQLG-ITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
336-543 |
1.19e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.96 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 336 EFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHqsklmAHMAVV 415
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 416 AQRTHL---FNATVRENILLAR---------PGASEKEMIQAA-RRARIHDFIltlpegyDTYVGEgglkLSGGQRQRVA 482
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyghkglfrrLSKADKAKVDEAlERVGLSELA-------DRQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 483 IARAILKNASVLILDEVTAGLDPVVGREIMQDLFQL-MKDKTSLVISH--HLVgLECMDEILVL 543
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHdlGLV-LEYFDRVLLL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
336-552 |
1.35e-34 |
|
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: 128.71 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 336 EFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVV 415
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 416 AqrthlfnatvrenillarpgasekemiQAARRARIHDFIltlpegyDTYVGEgglkLSGGQRQRVAIARAILKNASVLI 495
Cdd:cd03214 79 P---------------------------QALELLGLAHLA-------DRPFNE----LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 496 LDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHL-VGLECMDEILVLVEGKVVEKG 552
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
334-571 |
1.88e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 139.78 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRY-SAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD----------------------YQ- 389
Cdd:PTZ00265 1165 KIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdYQg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 390 -------------------------------RGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGAS 438
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 439 EKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQL 518
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 519 MK--DKTSLVISHHLVGLECMDEILVL----VEGKVVE-KGTHSQLLE-QGGVYARMWQLS 571
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSvQDGVYKKYVKLA 1465
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-557 |
8.39e-34 |
|
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: 128.07 E-value: 8.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTL---ANLLLGFFDYQR--GSLQLGGREVR--DYHQSK 407
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLlrlLNRLNDLIPGAPdeGEVLLDGKDIYdlDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQRTHLFNATVRENILLA------RPGASEKEMI-QAARRARIHDfiltlpEGYDTYvgeGGLKLSGGQRQR 480
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVeEALRKAALWD------EVKDRL---HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLV-GLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-552 |
8.71e-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: 127.64 E-value: 8.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAH--- 411
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPErrn 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENILLarpGASEKEMIQAARRARIHD--FILTLPEGYDTYVGEgglkLSGGQRQRVAIARAIL 488
Cdd:cd03259 74 IGMVFQDYALFpHLTVAENIAF---GLKLRGVPKAEIRARVREllELVGLEGLLNRYPHE----LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 489 KNASVLILDEVTAGLDPVVGREIMQDLFQLMK--DKTSLVISHHLVGLECM-DEILVLVEGKVVEKG 552
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
335-563 |
1.42e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 129.11 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA- 410
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 --HMAVVAQ--RTHLFNATVRENILLArP---GASEKEMIQAARRARIhdfILTLPEgydTYVGEGGLKLSGGQRQRVAI 483
Cdd:TIGR04521 81 rkKVGLVFQfpEHQLFEETVYKDIAFG-PknlGLSEEEAEERVKEALE---LVGLDE---EYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQL--MKDKTSLVISHHL--VgLECMDEILVLVEGKVVEKGT------ 553
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMedV-AEYADRVIVMHKGKIVLDGTprevfs 232
|
250
....*....|
gi 134052199 554 HSQLLEQGGV 563
Cdd:TIGR04521 233 DVDELEKIGL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
330-569 |
3.07e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 135.87 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 330 PKGYEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLM 409
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQRTHLFNATVRENIllaRPGA--SEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAI 487
Cdd:PLN03232 1310 RVLSIIPQSPVLFSGTVRFNI---DPFSehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 488 LKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLE-QGGVYAR 566
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFR 1466
|
...
gi 134052199 567 MWQ 569
Cdd:PLN03232 1467 MVH 1469
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
335-548 |
8.10e-33 |
|
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: 124.95 E-value: 8.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV--RDYHQSKLMAHM 412
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLF-NATVRENILLA---RPGASEKEMIQAARRarihdfILT---LPEGYDTYVGEgglkLSGGQRQRVAIAR 485
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApikVKGMSKAEAEERALE------LLEkvgLADKADAYPAQ----LSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKV 548
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFarEVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-560 |
4.07e-32 |
|
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: 123.83 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---H 411
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLFN-ATVRENILLARPGAS----------EKEMIQAARRA--RIhdfiltlpeGYDTYVGEGGLKLSGGQR 478
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglfPKEEKQRALAAleRV---------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 479 QRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQL-MKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHS 555
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLarEYADRIVGLKDGRIVFDGPPA 230
|
....*
gi 134052199 556 QLLEQ 560
Cdd:cd03256 231 ELTDE 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
352-553 |
8.69e-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: 122.93 E-value: 8.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAH------MAVVAQRTHLF-NA 424
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-----TGLPPHeiarlgIGRTFQIPRLFpEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 TVRENILLA------------RPGASEKEMIQAARRA--RIHdfiltLPEGYDTYVGEgglkLSGGQRQRVAIARAILKN 490
Cdd:cd03219 91 TVLENVMVAaqartgsglllaRARREEREARERAEELleRVG-----LADLADRPAGE----LSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 491 ASVLILDEVTAGLDPVVgREIMQDLFQLMKDK--TSLVISHHL-VGLECMDEILVLVEGKVVEKGT 553
Cdd:cd03219 162 PKLLLLDEPAAGLNPEE-TEELAELIRELRERgiTVLLVEHDMdVVMSLADRVTVLDQGRVIAEGT 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-553 |
8.86e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.98 E-value: 8.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAH--- 411
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPPEkrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENI---LLARpGASEKEmiqaaRRARIHDfILTLP--EGY-DTYVGEgglkLSGGQRQRVAIA 484
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVafgLRMR-GVPKAE-----IRARVAE-LLELVglEGLaDRYPHQ----LSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVgREIMQD-LFQLMKD--KTSLVISHHLvgLECM---DEILVLVEGKVVEKGT 553
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKL-REEMREeLRRLQRElgITFIYVTHDQ--EEALalaDRIAVMNDGRIEQVGT 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
352-553 |
2.31e-31 |
|
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: 122.45 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAHmAVVA-------QRTHLF-N 423
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-----TGLPPH-RIARlgiartfQNPRLFpE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATVRENILLA-----------------RPGASEKEMIQAAR----RARIHDFIltlpegyDTYVGEgglkLSGGQRQRVA 482
Cdd:COG0411 94 LTVLENVLVAaharlgrgllaallrlpRARREEREARERAEelleRVGLADRA-------DEPAGN----LSYGQQRRLE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 483 IARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHH--LVglecM---DEILVLVEGKVVEKGT 553
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDmdLV----MglaDRIVVLDFGRVIAEGT 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-553 |
4.59e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.03 E-value: 4.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV-------RDyhqs 406
Cdd:COG3839 3 SLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 klmahMAVVAQRTHLF-NATVRENI---LLARpGASEKEmiqaaRRARIHDF--ILTLpEGY-DTYVGEgglkLSGGQRQ 479
Cdd:COG3839 77 -----IAMVFQSYALYpHMTVYENIafpLKLR-KVPKAE-----IDRRVREAaeLLGL-EDLlDRKPKQ----LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 480 RVAIARAILKNASVLILDEVTAGLDP---VVGREIMQDLFQLMKdKTSLVISHHLVglECM---DEILVLVEGKVVEKGT 553
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAklrVEMRAEIKRLHRRLG-TTTIYVTHDQV--EAMtlaDRIAVMNDGRIQQVGT 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-560 |
5.13e-31 |
|
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: 122.85 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI--LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD---YQRGSLQLGGREVRDYHQSKLM 409
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 A----HMAVVAQrthlfNA--------TVRENI---LLARPGASEKEmiqaaRRARIHDFI----LTLPEGY-DTYVGEg 469
Cdd:COG0444 82 KirgrEIQMIFQ-----DPmtslnpvmTVGDQIaepLRIHGGLSKAE-----ARERAIELLervgLPDPERRlDRYPHE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 470 glkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLV-ISHHL-VGLECMDEILVLVEG 546
Cdd:COG0444 151 ---LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILfITHDLgVVAEIADRVAVMYAG 227
|
250
....*....|....
gi 134052199 547 KVVEKGTHSQLLEQ 560
Cdd:COG0444 228 RIVEEGPVEELFEN 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-559 |
3.15e-30 |
|
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: 118.55 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 336 EFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAH-MAV 414
Cdd:COG0410 5 EVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLARPGASEKEMIqAARRARIHDFILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASV 493
Cdd:COG0410 83 VPEGRRIFpSLTVEENLLLGAYARRDRAEV-RADLERVYELFPRLKERRRQRAGT----LSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTS-LVISHHL-VGLECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTiLLVEQNArFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
273-543 |
3.43e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 126.68 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 273 GVYIAMLALATLSAFEAVTPLPLTFIYLEeSMSAAKRLFELAETENYSPSRKDEQFVPKGYEIEFNNLHFRY-SAKDPWI 351
Cdd:PTZ00265 322 GSVISILLGVLISMFMLTIILPNITEYMK-SLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYdTRKDVEI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLG-GREVRDYHQSKLMAHMAVVAQRTHLFNATVRENI 430
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 -------------------------------------------LLARPGAS--------------EKEMIQAARRARIHD 453
Cdd:PTZ00265 481 kyslyslkdlealsnyynedgndsqenknkrnscrakcagdlnDMSNTTDSneliemrknyqtikDSEVVDVSKKVLIHD 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 454 FILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLM--KDKTSLVISHHL 531
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
|
330
....*....|..
gi 134052199 532 VGLECMDEILVL 543
Cdd:PTZ00265 641 STIRYANTIFVL 652
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-560 |
4.59e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.02 E-value: 4.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMAHMA 413
Cdd:COG1118 2 SIEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQrtH--LF-NATVRENI---LLARPGASekemiqAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIAR 485
Cdd:COG1118 79 FVFQ--HyaLFpHMTVAENIafgLRVRPPSK------AEIRARVEELLelVQLEGLADRYPSQ----LSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISH-HLVGLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
301-569 |
7.15e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 125.62 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 301 EESMSAAKRLFELAETENYSPSRKDEQFVPKGY----EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKS 376
Cdd:PLN03130 1200 ENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWpssgSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKS 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 377 TLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENiLLARPGASEKEMIQAARRARIHDFIL 456
Cdd:PLN03130 1280 SMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-LDPFNEHNDADLWESLERAHLKDVIR 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 457 TLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLEC 536
Cdd:PLN03130 1359 RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID 1438
|
250 260 270
....*....|....*....|....*....|....
gi 134052199 537 MDEILVLVEGKVVEKGTHSQLL-EQGGVYARMWQ 569
Cdd:PLN03130 1439 CDRILVLDAGRVVEFDTPENLLsNEGSAFSKMVQ 1472
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-540 |
7.99e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.42 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyHQSKLMAHMAV 414
Cdd:COG4133 3 LEAENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNA-TVRENILLAR----PGASEKEMIQAARRARIHDFIltlpegyDTYVGegglKLSGGQRQRVAIARAILK 489
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 490 NASVLILDEVTAGLDpVVGREIMQDLFQLMKDKTSLVI--SHHLVGLECMDEI 540
Cdd:COG4133 149 PAPLWLLDEPFTALD-AAGVALLAELIAAHLARGGAVLltTHQPLELAAARVL 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-553 |
1.24e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.41 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI--LRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLlgffdyQR---GSLQLGGREVRDYHQS 406
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLL------ERptsGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 KLMA---HMAVVAQRTHLFNA-TVRENIllARP----GASEKEmiqaaRRARIHDfILTLpegydtyVGEGGLK------ 472
Cdd:COG1135 76 ELRAarrKIGMIFQHFNLLSSrTVAENV--ALPleiaGVPKAE-----IRKRVAE-LLEL-------VGLSDKAdaypsq 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 473 LSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMqdlfQLMKD------KTSLVISHhlvglE-------CmDE 539
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIL----DLLKDinrelgLTIVLITH-----EmdvvrriC-DR 210
|
250
....*....|....
gi 134052199 540 ILVLVEGKVVEKGT 553
Cdd:COG1135 211 VAVLENGRIVEQGP 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-549 |
1.37e-29 |
|
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: 115.82 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYSaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrDYHQSKLMAHMAVVAQ- 417
Cdd:cd03226 4 NISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 418 -RTHLFNATVRENILLARPGASEKEMIQAA--RRARIHDFILTLPegydtyvgeggLKLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03226 80 vDYQLFTDSVREELLLGLKELDAGNEQAETvlKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 495 ILDEVTAGLDpvvgREIMQDLFQLMKD-----KTSLVISHHL-VGLECMDEILVLVEGKVV 549
Cdd:cd03226 149 IFDEPTSGLD----YKNMERVGELIRElaaqgKAVIVITHDYeFLAKVCDRVLLLANGAIV 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
356-558 |
1.68e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.22 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 356 SFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMavVAQRTHLFN-ATVRENILLA- 433
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSM--LFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 434 RPG----ASEKEMIQA-ARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:PRK10771 97 NPGlklnAAQREKLHAiARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 509 REIMQDLFQLMKDK--TSLVISHHLV-GLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
335-560 |
1.90e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 116.63 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLM---AH 411
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENILLAR--------------PGASEKEMIQAARRARIHDFILTLPEgydtyvgegglKLSGG 476
Cdd:TIGR02315 81 IGMIFQHYNLIeRLTVLENVLHGRlgykptwrsllgrfSEEDKERALSALERVGLADKAYQRAD-----------QLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 477 QRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHL-VGLECMDEILVLVEGKVVEKGT 553
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVdLAKKYADRIVGLKAGEIVFDGA 229
|
....*..
gi 134052199 554 HSQLLEQ 560
Cdd:TIGR02315 230 PSELDDE 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
352-550 |
3.09e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.28 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVR--DYHQSkLMAHMAVVAQRTHLF-NATVRE 428
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrSPRDA-QAAGIAIIHQELNLVpNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLARPGAS-----EKEMIQAARRArIHDFILTLPEgyDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:COG1129 99 NIFLGREPRRgglidWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 504 DPvvgREImQDLFQLMKD-----KTSLVISHHlvglecMDEIL-------VLVEGKVVE 550
Cdd:COG1129 172 TE---REV-ERLFRIIRRlkaqgVAIIYISHR------LDEVFeiadrvtVLRDGRLVG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
335-561 |
3.44e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.39 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQR--THLFNATVRENILLARpgasEKEMIQAARRARIHDFILTLPEGYDtYVGEGGLKLSGGQRQRVAIARAILKNAS 492
Cdd:PRK13648 88 VFQNpdNQFVGSIVKYDVAFGL----ENHAVPYDEMHRRVSEALKQVDMLE-RADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 493 VLILDEVTAGLDPvVGREIMQDLFQLMK---DKTSLVISHHLVglECM--DEILVLVEGKVVEKGTHSQLLEQG 561
Cdd:PRK13648 163 VIILDEATSMLDP-DARQNLLDLVRKVKsehNITIISITHDLS--EAMeaDHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-558 |
5.11e-29 |
|
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: 115.57 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG-----------FFDYQRGslqlgGREVRDy 403
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvrLFGERRG-----GEDVWE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 404 hqskLMAHMAVVAQRTHLF---NATVRENIL------LARPGASEKEMIQAARRarihdfILTLpegydtyVGEGGLK-- 472
Cdd:COG1119 76 ----LRKRIGLVSPALQLRfprDETVLDVVLsgffdsIGLYREPTDEQRERARE------LLEL-------LGLAHLAdr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 473 ----LSGGQRQRVAIARAILKNASVLILDEVTAGLDPvVGREIMQDLF-QLMKD--KTSLVISHHL-VGLECMDEILVLV 544
Cdd:COG1119 139 pfgtLSQGEQRRVLIARALVKDPELLILDEPTAGLDL-GARELLLALLdKLAAEgaPTLVLVTHHVeEIPPGITHVLLLK 217
|
250
....*....|....
gi 134052199 545 EGKVVEKGTHSQLL 558
Cdd:COG1119 218 DGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-553 |
6.02e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGR----EVRDYHQS 406
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 KLMAHMAVVAQ--RTHLFNATVRENILLArP---GASEKEmiqAARRARIHDFILTLPEgydTYVGEGGLKLSGGQRQRV 481
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFG-PmnfGVSEED---AKQKAREMIELVGLPE---ELLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHlvglecM-------DEILVLVEGKVVEKG 552
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHS------MedaaryaDQIVVMHKGTVFLQG 228
|
.
gi 134052199 553 T 553
Cdd:PRK13634 229 T 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
334-552 |
1.83e-28 |
|
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: 112.26 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLhfRYSAKDPW------ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQR--GSLQLGGREVrdyHQ 405
Cdd:cd03213 3 TLSFRNL--TVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL---DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 406 SKLMAHMAVVAQRTHLF-NATVRENIllarpgasekeMIQAARRarihdfiltlpegydtyvgegglKLSGGQRQRVAIA 484
Cdd:cd03213 78 RSFRKIIGYVPQDDILHpTLTVRETL-----------MFAAKLR-----------------------GLSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLV---GLECMDEILVLVEGKVVEKG 552
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsseIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-530 |
1.98e-28 |
|
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: 112.89 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK---LMAH 411
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENILLA------RPGASEKEMIQAARRARIHDFILTLPEGydtyvgegglkLSGGQRQRVAIA 484
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHH 530
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-552 |
2.74e-28 |
|
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: 112.29 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRrLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQsKLMAHMAV 414
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVREniLLARPGASeKEMIQAARRARIHDFI--LTLPEGYDTYVGegglKLSGGQRQRVAIARAILKNA 491
Cdd:cd03264 77 LPQEFGVYpNFTVRE--FLDYIAWL-KGIPSKEVKARVDEVLelVNLGDRAKKKIG----SLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 492 SVLILDEVTAGLDP---VVGREIMQDlfqLMKDKTsLVISHHLVG-LECM-DEILVLVEGKVVEKG 552
Cdd:cd03264 150 SILIVDEPTAGLDPeerIRFRNLLSE---LGEDRI-VILSTHIVEdVESLcNQVAVLNKGKLVFEG 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-558 |
9.19e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.13 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:COG4559 2 LEAENLSVRLGGR--TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHL-FNATVRENILLAR-PGASEkemiQAARRARIHDfILTLpegydtyVGEGGLK------LSGGQRQRVAIARA 486
Cdd:COG4559 80 LPQHSSLaFPFTVEEVVALGRaPHGSS----AAQDRQIVRE-ALAL-------VGLAHLAgrsyqtLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 487 IL-------KNASVLILDEVTAGLDPVVgreiMQDLFQLMKDKTS-----LVISH--HLVGLECmDEILVLVEGKVVEKG 552
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAH----QHAVLRLARQLARrgggvVAVLHdlNLAAQYA-DRILLLHQGRLVAQG 222
|
....*.
gi 134052199 553 THSQLL 558
Cdd:COG4559 223 TPEEVL 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-552 |
9.43e-28 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 110.66 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMavVAQRTHLF-NATVRENILL 432
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSM--LFQENNLFaHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 433 AR-PG-----ASEKEMIQAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPV 506
Cdd:cd03298 94 GLsPGlkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 134052199 507 VGREIMQDLFQLMKDK--TSLVISHHLVGLECMDEILVLVE-GKVVEKG 552
Cdd:cd03298 163 LRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDnGRIAAQG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-558 |
1.09e-27 |
|
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: 111.62 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLArpgASEKEMIQAARRARIhDFILTL----PEGY-DTYVGEgglkLSGGQRQRVAIARAIL 488
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALV---PKLLKWPKEKIRERA-DELLALvgldPAEFaDRYPHE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 489 KNASVLILDEVTAGLDPVVgREIMQDLFQLMKD---KTSLVISHHlvglecMDE-------ILVLVEGKVVEKGTHSQLL 558
Cdd:cd03295 152 ADPPLLLMDEPFGALDPIT-RDQLQEEFKRLQQelgKTIVFVTHD------IDEafrladrIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
335-557 |
1.44e-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: 110.67 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRdYHQSKLMAHMAV 414
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNA-TVRENILL-AR-PGASEKEMIQAARRARIHdfiLTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNA 491
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyARlKGLPKSEIKEEVELLLRV---LGLTDKANKRART----LSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 492 SVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLvgLEC---MDEILVLVEGKVVEKGTHSQL 557
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSM--DEAealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
348-534 |
1.68e-27 |
|
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: 109.43 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 348 DPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMA---HMAVVAQRT--HLF 422
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLErrqRVGLVFQDPddQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 423 NATVRENILLA--RPGASEKEMiqaarRARIHDFILTLpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVT 500
Cdd:TIGR01166 83 AADVDQDVAFGplNLGLSEAEV-----ERRVREALTAV--GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....
gi 134052199 501 AGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL 534
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
333-563 |
3.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYSaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHM 412
Cdd:PRK13647 3 NIIEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQ--RTHLFNATVRENILLA----RPGASE-KEMIQAARRA-RIHDFILTLPEgydtyvgegglKLSGGQRQRVAIA 484
Cdd:PRK13647 82 GLVFQdpDDQVFSSTVWDDVAFGpvnmGLDKDEvERRVEEALKAvRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKG-----THSQL 557
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaaEWADQVIVLKEGRVLAEGdksllTDEDI 230
|
....*.
gi 134052199 558 LEQGGV 563
Cdd:PRK13647 231 VEQAGL 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
352-560 |
3.14e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.55 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQrGSLQLGGREVRDYHQSKLMA---HMAVVAQ--------RtH 420
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPlrrRMQVVFQdpfgslspR-M 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 LFNATVRENILLARPGASEKEmiqaaRRARIHDfILT----LPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLIL 496
Cdd:COG4172 380 TVGQIIAEGLRVHGPGLSAAE-----RRARVAE-ALEevglDPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 497 DEVTAGLDPVVGREIMqDLFQLMKDK---TSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:COG4172 450 DEPTSALDVSVQAQIL-DLLRDLQREhglAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-552 |
3.29e-27 |
|
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: 109.31 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRrLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLF-NATVRE 428
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLARPGASEKEMIQAARRarihdfiLTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDE-------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 134052199 509 REIMQDLFQLMKD--KTSLVISHHLVGLECM-DEILVLVEGKVVEKG 552
Cdd:cd03297 168 LQLLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
335-555 |
5.69e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLLGffdYQRGSLQLGGREVrDYHQS----- 406
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLLEM---PRSGTLNIAGNHF-DFSKTpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 --KLMAHMAVVAQRTHLF-NATVRENILLArP----GASEKEMIQAAR----RARIHDFILTLPegydtyvgeggLKLSG 475
Cdd:PRK11124 77 irELRRNVGMVFQQYNLWpHLTVQQNLIEA-PcrvlGLSKDQALARAEklleRLRLKPYADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 476 GQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGT 553
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVarKTASRVVYMENGHIVEQGD 224
|
..
gi 134052199 554 HS 555
Cdd:PRK11124 225 AS 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
356-548 |
5.75e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 108.80 E-value: 5.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 356 SFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMavVAQRTHLF-NATVRENILLA- 433
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSM--LFQENNLFaHLTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 434 RPG----ASEKE-MIQAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:TIGR01277 96 HPGlklnAEQQEkVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 134052199 509 REIMQDLFQLM--KDKTSLVISHHLVGL-ECMDEILVLVEGKV 548
Cdd:TIGR01277 165 EEMLALVKQLCseRQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-555 |
7.41e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQ-------S 406
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQkpsekaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 KLMAHMAVVAQRTHLF-NATVRENiLLARP----GASEKEMIQAAR----RARIHDFILTLPegydtyvgeggLKLSGGQ 477
Cdd:COG4161 79 LLRQKVGMVFQQYNLWpHLTVMEN-LIEAPckvlGLSKEQAREKAMkllaRLRLTDKADRFP-----------LHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 478 RQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHS 555
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFarKVASQVVYMEKGRIIEQGDAS 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-553 |
8.32e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.40 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:COG4604 2 IEIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHlFNA--TVREniLLA---------RPGASEKEMIQAArrarIHDFILTlpEGYDTYVGEgglkLSGGQRQRVAI 483
Cdd:COG4604 80 LRQENH-INSrlTVRE--LVAfgrfpyskgRLTAEDREIIDEA----IAYLDLE--DLADRYLDE----LSGGQRQRAFI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTS-LVI------SHHlvglecMDEILVLVEGKVVEKGT 553
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVvIVLhdinfaSCY------ADHIVAMKDGRVVAQGT 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
335-558 |
8.53e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.48 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:PRK13548 3 LEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHL-FNATVRENILLAR-PGASEKemiqaARRARIHDFILTLpegydtyVGEGGLK------LSGGQRQRVAIARA 486
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRaPHGLSR-----AEDDALVAAALAQ-------VDLAHLAgrdypqLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 487 IL------KNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLvGLECM--DEILVLVEGKVVEKGTHSQ 556
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDL-NLAARyaDRIVLLHQGRLVADGTPAE 227
|
..
gi 134052199 557 LL 558
Cdd:PRK13548 228 VL 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
273-567 |
9.25e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 115.84 E-value: 9.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 273 GVYIamLALATLSAFEAVTPLPLtFIYLEESMSAAKRLFELAETENYSPSRKDEQFV-------------PKGYEIEFNN 339
Cdd:PLN03232 543 GVFV--LLGGDLTPARAFTSLSL-FAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLseerilaqnpplqPGAPAISIKN 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 340 LHFRYSAK--DPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDY-QRGSLQLGGRevrdyhqsklmahMAVVA 416
Cdd:PLN03232 620 GYFSWDSKtsKP-TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGS-------------VAYVP 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 417 QRTHLFNATVRENILLARPGASEKEMIQAARRARIHDfiLTLPEGYD-TYVGEGGLKLSGGQRQRVAIARAILKNASVLI 495
Cdd:PLN03232 686 QVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 496 LDEVTAGLDPVVGREIMQDLFQL-MKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
333-553 |
1.37e-26 |
|
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: 108.20 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlmAHM 412
Cdd:cd03296 1 MSIEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLF-NATVRENI---LLARPGASEKEmiQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARA 486
Cdd:cd03296 77 GFVFQHYALFrHMTVFDNVafgLRVKPRSERPP--EAEIRAKVHELLklVQLDWLADRYPAQ----LSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 487 ILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISH-HLVGLECMDEILVLVEGKVVEKGT 553
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
351-560 |
2.21e-26 |
|
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: 108.79 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmahMAVVAQRTHLFNATVRENI 430
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLarpGASEKE-----MIQAARrarIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDP 505
Cdd:cd03291 119 IF---GVSYDEyryksVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 506 VVGREIMQD-LFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:cd03291 193 FTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-572 |
2.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.71 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV----RDYHQSK 407
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQ--RTHLFNATVRENILLarpGASEKEMIQAARRARIHDFILTLpeGYDTYVGEGG-LKLSGGQRQRVAIA 484
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIF---GPKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDL--FQLMKDKTSLVISHHLVGLEC-MDEILVLVEGKVVEKGTHSQLLEQG 561
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
|
250
....*....|.
gi 134052199 562 GvYARMWQLSV 572
Cdd:PRK13646 238 K-KLADWHIGL 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
351-550 |
2.97e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 107.13 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLFNA-T 425
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlrarHVGFVFQSFQLLPTlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 426 VRENILLARPGASEKEMIQAARRArihdfiltLPEgydtyVGEGGL------KLSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:COG4181 107 ALENVMLPLELAGRRDARARARAL--------LER-----VGLGHRldhypaQLSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 500 TAGLDPVVGREIMQDLFQLMKDK-TSLVISHHLVGL--ECmDEILVLVEGKVVE 550
Cdd:COG4181 174 TGNLDAATGEQIIDLLFELNRERgTTLVLVTHDPALaaRC-DRVLRLRAGRLVE 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
308-567 |
5.23e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.68 E-value: 5.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 308 KRLFEL--AETENYSPSRKDEQFVPKgyeIEFNNLHFRYSAK-DPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG 384
Cdd:PLN03130 589 KRLEELllAEERVLLPNPPLEPGLPA---ISIKNGYFSWDSKaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 385 FF-DYQRGSLQLGGRevrdyhqsklmahMAVVAQRTHLFNATVRENILLARPGASEK--EMIQAArrARIHDFILtLPEG 461
Cdd:PLN03130 666 ELpPRSDASVVIRGT-------------VAYVPQVSWIFNATVRDNILFGSPFDPERyeRAIDVT--ALQHDLDL-LPGG 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 462 YDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQD-LFQLMKDKTSLVISHHLVGLECMDEI 540
Cdd:PLN03130 730 DLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRI 809
|
250 260
....*....|....*....|....*..
gi 134052199 541 LVLVEGKVVEKGTHSQLLEQGGVYARM 567
Cdd:PLN03130 810 ILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-552 |
8.32e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.95 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLqLGGREVrdyhqsklmahmAVVAQRTHLFNATVRENI 430
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSI------------AYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLARPgASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGRE 510
Cdd:PTZ00243 742 LFFDE-EDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 134052199 511 IMQDLFQ-LMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKG 552
Cdd:PTZ00243 821 VVEECFLgALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
335-559 |
8.62e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.95 E-value: 8.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTlanLLLGFF---DYQRGSLQLGGREVRDYHQSKLMAH 411
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKST---LLLTFMrmvEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLFNATVRENIllaRP--GASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILK 489
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 490 NASVLIL-DEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:PTZ00243 1463 KGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
21-307 |
1.25e-25 |
|
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: 106.98 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 21 AVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIE 100
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 101 PLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFfigaAVVVPIFIRAW 180
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVF----ALLIPLSPALW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 181 GR---RSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWT 257
Cdd:cd18561 157 DRlakDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 134052199 258 ILVMAIIKVEQGELpGVYIAMLALATLSAFEAvtPLPLTFIYLEESMSAA 307
Cdd:cd18561 237 ALGVGALRVLGGQL-TLSSLLLILFLSREFFR--PLRDLGAYWHAGYQGI 283
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
352-560 |
1.71e-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: 105.80 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLF-NATV 426
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENIL--LARPGASEKEMIQAARRArIHDFILtlpEGY-DTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:cd03294 120 LENVAfgLEVQGVPRAEREERAAEA-LELVGL---EGWeHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 504 DPVVGREiMQDLF---QLMKDKTSLVISHHLVglECM---DEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:cd03294 192 DPLIRRE-MQDELlrlQAELQKTIVFITHDLD--EALrlgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
336-557 |
2.06e-25 |
|
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: 104.53 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 336 EFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAH---- 411
Cdd:TIGR03410 2 EVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-----TKLPPHerar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 --MAVVAQRTHLFNA-TVRENILL---ARPGASEKemiqaarrarIHDFILTL-PEGYDTYVGEGGLkLSGGQRQRVAIA 484
Cdd:TIGR03410 75 agIAYVPQGREIFPRlTVEENLLTglaALPRRSRK----------IPDEIYELfPVLKEMLGRRGGD-LSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQL--MKDKTSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLdFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
335-553 |
2.38e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDP---WILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLG---------GREVRD 402
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 403 YHQSK-------LMAHMAVVAQ--RTHLFNATVRENILLArPGASEKEMIQAARRARIHDFILTLPegyDTYVGEGGLKL 473
Cdd:PRK13631 102 NPYSKkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLD---DSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 474 SGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMqdlfQLMKD-----KTSLVISHHLVG-LECMDEILVLVEGK 547
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM----QLILDakannKTVFVITHTMEHvLEVADEVIVMDKGK 253
|
....*.
gi 134052199 548 VVEKGT 553
Cdd:PRK13631 254 ILKTGT 259
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
332-565 |
2.71e-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: 104.99 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 332 GYEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLAnllLGFF---DYQRGSLQLGGREVRDYHQSKL 408
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS---LAFFrmvDIFDGKIVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 409 MAHMAVVAQRTHLFNATVRENiLLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAIL 488
Cdd:cd03288 94 RSRLSIILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 489 KNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQ-GGVYA 565
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFA 250
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
335-553 |
5.51e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMA---H 411
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEvrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRT--HLFNATVRENILLArP---GASEKEMiqaarRARIHDFILTLP-EGYDTYVGEgglKLSGGQRQRVAIAR 485
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFG-PlnlGLSKEEV-----EKRVKEALKAVGmEGFENKPPH---HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGLECM--DEILVLVEGKVVEKGT 553
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyaDKVYVMSDGKIIKEGT 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
352-549 |
6.65e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFfdYQ--RGSLQLGGREVRDYHQSKLMAH---MavVAQrtH--LFNA 424
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQpdSGEILIDGKPVRIRSPRDAIALgigM--VHQ--HfmLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 -TVRENILLARPGASEKEMIQAARRARIHDFIltlpEGY------DTYVGEgglkLSGGQRQRVAIARAILKNASVLILD 497
Cdd:COG3845 95 lTVAENIVLGLEPTKGGRLDRKAARARIRELS----ERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 498 EVTAGLDPvvgREImQDLFQLMKD-----KTSLVISHHL--VgLECMDEILVLVEGKVV 549
Cdd:COG3845 167 EPTAVLTP---QEA-DELFEILRRlaaegKSIIFITHKLreV-MAIADRVTVLRRGKVV 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-550 |
7.26e-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: 108.35 E-value: 7.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 13 PHWLPMLWAVLLGFLAVGSNIGLLTtsayLISRAAQHPPVLDLMVA---IVGVRFFGIARAVFRYLERYFSHDVTFRvls 89
Cdd:COG4615 10 ESRWLLLLALLLGLLSGLANAGLIA----LINQALNATGAALARLLllfAGLLVLLLLSRLASQLLLTRLGQHAVAR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 90 nMRVWFYKAIE--PLAtsQLMHYHSGDLLSRIVSDVETLKNFYLRVlsPPLV--ALLTLGVVFFLlacfdlrmAFI-FLA 164
Cdd:COG4615 83 -LRLRLSRRILaaPLE--RLERIGAARLLAALTEDVRTISQAFVRL--PELLqsVALVLGCLAYL--------AWLsPPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 165 FFIGAAVVVP-IFIRAWGRRSGQGILGSKAQLNTCLVDGIQGMTD---LLSFDQQGRQL---EKIDKTNDNLSKLQGRLA 237
Cdd:COG4615 150 FLLTLVLLGLgVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEgfkELKLNRRRRRAffdEDLQPTAERYRDLRIRAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 238 KINGLAGSLTGLCMNLAMWTILVMA--IIKVEQGELPGVYIAMLALAT-LSAFEAVTPlpltfIYLEESMSAAK--RL-F 311
Cdd:COG4615 230 TIFALANNWGNLLFFALIGLILFLLpaLGWADPAVLSGFVLVLLFLRGpLSQLVGALP-----TLSRANVALRKieELeL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 312 ELAETENYSPSRKDEQFVPKGYEIEFNNLHFRYSAKD---PWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDY 388
Cdd:COG4615 305 ALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 389 QRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNAtvreniLLARPGASEKEMIQA-ARRARIHDfILTLpegydtyvg 467
Cdd:COG4615 385 ESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARARElLERLELDH-KVSV--------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 468 EGG----LKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISH-----HlvgleC 536
Cdd:COG4615 449 EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLPELKArgKTVIAISHddryfD-----L 523
|
570
....*....|....
gi 134052199 537 MDEILVLVEGKVVE 550
Cdd:COG4615 524 ADRVLKMDYGKLVE 537
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-310 |
8.71e-25 |
|
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: 104.55 E-value: 8.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYK 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 98 AIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFI 177
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 178 RaWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWT 257
Cdd:cd07346 161 R-RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 258 ILVMAIIKVEQGEL-PGVYIAMLALATLsAFEAVTPLPLTFIYLEESMSAAKRL 310
Cdd:cd07346 240 VLLYGGYLVLQGSLtIGELVAFLAYLGM-LFGPIQRLANLYNQLQQALASLERI 292
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
335-558 |
9.63e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 103.76 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI-------LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV--RDYHQ 405
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFrrqqfeaVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeyGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 406 -SKlmaHMAVVAQR-THLFNATVRENILLARPGASEKEMIQAARRARIHDfILT----LPEGYDTYVGEgglkLSGGQRQ 479
Cdd:COG4167 85 rCK---HIRMIFQDpNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFA-TLRlvglLPEHANFYPHM----LSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 480 RVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLvGL--ECMDEILVLVEGKVVEKGTHS 555
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLgiSYIYVSQHL-GIvkHISDKVLVMHQGEVVEYGKTA 235
|
...
gi 134052199 556 QLL 558
Cdd:COG4167 236 EVF 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
352-549 |
1.48e-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: 100.20 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRdyhqsklmahmavvaqrthlfNATVREnil 431
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASPRD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 432 larpgasekemiqaARRARI---HdfiltlpegydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPvvg 508
Cdd:cd03216 72 --------------ARRAGIamvY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALTP--- 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 134052199 509 REImQDLFQLMKD-----KTSLVISHHLVglECM---DEILVLVEGKVV 549
Cdd:cd03216 116 AEV-ERLFKVIRRlraqgVAVIFISHRLD--EVFeiaDRVTVLRDGRVV 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-560 |
3.33e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGgrevrdyhqSKLmaHMAV 414
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETV--KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF--NATVRENILLARPGASEKEmiqaaRRARIHDFILTlPEGYDTYVGegglKLSGGQRQRVAIARAILKNAS 492
Cdd:COG0488 383 FDQHQEELdpDKTVLDELRDGAPGGTEQE-----VRGYLGRFLFS-GDDAFKPVG----VLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 493 VLILDEVTAGLDpVVGREIMQDLfqLMK-DKTSLVISH--HLVGLECmDEILVLVEGKVVEK-GTHSQLLEQ 560
Cdd:COG0488 453 VLLLDEPTNHLD-IETLEALEEA--LDDfPGTVLLVSHdrYFLDRVA-TRILEFEDGGVREYpGGYDDYLEK 520
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
351-552 |
4.65e-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: 100.41 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlmAHMAVVAQRTHLF-NATVREN 429
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 IL--LARPGASEKEMiqaarRARIHDF--ILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDP 505
Cdd:cd03301 93 IAfgLKLRKVPKDEI-----DERVREVaeLLQIEHLLDRKPKQ----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 506 VVGREIMQDLFQLMK--DKTSLVISHHLVglECM---DEILVLVEGKVVEKG 552
Cdd:cd03301 164 KLRVQMRAELKRLQQrlGTTTIYVTHDQV--EAMtmaDRIAVMNDGQIQQIG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
335-546 |
6.11e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 100.10 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSL----QLGGREVRDYHQSKLMA 410
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 HMAVVAQRTHLFNATVRENILLARPGASE--KEMIQAARrarIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAIL 488
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQryKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 489 KNASVLILDEVTAGLDPVVGREIMQD-LFQLMKD--KTSLVISHHLVGLECMDEILVLVEG 546
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-562 |
6.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRY-SAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQR--THLFNATVRENIL--LARPGASEKEMI----QAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIAR 485
Cdd:PRK13650 85 MVFQNpdNQFVGATVEDDVAfgLENKGIPHEEMKervnEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVIS--HHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGG 562
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISitHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
354-557 |
6.61e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.89 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---HMAVVAQ--------RThlf 422
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQdpyaslnpRM--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 423 naTVREniLLARPGASEKEMIQAARRARIHDfILTL----PEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDE 498
Cdd:COG4608 113 --TVGD--IIAEPLRIHGLASKAERRERVAE-LLELvglrPEHADRYPHE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 499 VTAGLDPVVGREI---MQDL---FQLmkdkTSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQL 557
Cdd:COG4608 184 PVSALDVSIQAQVlnlLEDLqdeLGL----TYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDEL 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
351-557 |
7.18e-24 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 106.92 E-value: 7.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmahMAVVAQRTHLFNATVRENI 430
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLarpGASEKEM--IQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:TIGR01271 508 IF---GLSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 134052199 509 REIMQD-LFQLMKDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:TIGR01271 585 KEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-515 |
9.94e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW--ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAHM 412
Cdd:COG4525 4 LTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLFN-ATVRENILLarpGASEKEMIQAARRARIHDFiLTLpegydtyVGEGGL------KLSGGQRQRVAIAR 485
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAF---GLRLRGVPKAERRARAEEL-LAL-------VGLADFarrriwQLSGGMRQRVGIAR 147
|
170 180 190
....*....|....*....|....*....|
gi 134052199 486 AILKNASVLILDEVTAGLDPVVgREIMQDL 515
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALT-REQMQEL 176
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
352-553 |
2.70e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDY---HQSKLMAHMAVVAQRTHlfnATV-- 426
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENI--LLARPGASEKEMIQAARRARIHDFILTL---PEGYDTYVGegglKLSGGQRQRVAIARAILKNASVLILDEVTA 501
Cdd:PRK11308 108 RKKVgqILEEPLLINTSLSAAERREKALAMMAKVglrPEHYDRYPH----MFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 502 GLDPVVGREI---MQDLFQLMkdKTSLV-ISHHLVGLECM-DEILVLVEGKVVEKGT 553
Cdd:PRK11308 184 ALDVSVQAQVlnlMMDLQQEL--GLSYVfISHDLSVVEHIaDEVMVMYLGRCVEKGT 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
351-560 |
3.08e-23 |
|
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: 98.46 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlmAHMAVVAQRTHLF-NATVREN 429
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFpHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 ILLarpGASEKEMIQAARRARIHDFI-LTLPEGY-DTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVV 507
Cdd:cd03300 93 IAF---GLRLKKLPKAEIKERVAEALdLVQLEGYaNRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 508 gREIMQ-DLFQLMKD--KTSLVISHHLVglECM---DEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:cd03300 166 -RKDMQlELKRLQKElgITFVFVTHDQE--EALtmsDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
101-560 |
6.27e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 103.84 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 101 PLATSQLMHyhSGDLLSRIVSDVETLKNFY-LRVLSPPLVALLTLGVVFFLlacfDLRMAFIFLAffigAAVVVPIFI-- 177
Cdd:TIGR01271 972 PMAVLNTMK--AGRILNRFTKDMAIIDDMLpLTLFDFIQLTLIVLGAIFVV----SVLQPYIFIA----AIPVAVIFIml 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 178 RAWGRRSGQGI--LGSKAQ--LNTCLVDGIQGMTDLLSFdqqGRQ--LEKIDKTNDN---------LSKLQGRLAKINgl 242
Cdd:TIGR01271 1042 RAYFLRTSQQLkqLESEARspIFSHLITSLKGLWTIRAF---GRQsyFETLFHKALNlhtanwflyLSTLRWFQMRID-- 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 243 agsltglcMNLAMWTILVMAIIKVEQGELPG-----VYIAMLALATLSAfeAVTplplTFIYLEESMSAAKRLFELAE-- 315
Cdd:TIGR01271 1117 --------IIFVFFFIAVTFIAIGTNQDGEGevgiiLTLAMNILSTLQW--AVN----SSIDVDGLMRSVSRVFKFIDlp 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 316 TENYSPSRKDEQFV----------------PKGYEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLA 379
Cdd:TIGR01271 1183 QEEPRPSGGGGKYQlstvlvienphaqkcwPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 380 NLLLGFFDYQrGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENIllaRPGA--SEKEMIQAARRARIHDFILT 457
Cdd:TIGR01271 1263 SALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQ 1338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 458 LPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTsLVISHHLVG--LE 535
Cdd:TIGR01271 1339 FPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT-VILSEHRVEalLE 1417
|
490 500
....*....|....*....|....*
gi 134052199 536 CmDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:TIGR01271 1418 C-QQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-553 |
7.03e-23 |
|
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: 97.41 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlmAHMAVVAQRTHLF-NATVRENI 430
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 -----LLARPGAS-EKEMIQAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:cd03299 93 ayglkKRKVDKKEiERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 505 PVVGREIMQDLFQLMK--DKTSLVISHHLVGLECM-DEILVLVEGKVVEKGT 553
Cdd:cd03299 162 VRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGK 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-558 |
9.18e-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: 99.79 E-value: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLF-NATVRE 428
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLARpgaseKEMIQAARRARIHDFILTLpegydtyvGEGGL------KLSGGQRQRVAIARAILKNASVLILDEVTAG 502
Cdd:COG4148 97 NLLYGR-----KRAPRAERRISFDEVVELL--------GIGHLldrrpaTLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 503 LDPVVGREIMqDLFQLMKDKTSLVI---SHHlvglecMDEIL-------VLVEGKVVEKGTHSQLL 558
Cdd:COG4148 164 LDLARKAEIL-PYLERLRDELDIPIlyvSHS------LDEVArladhvvLLEQGRVVASGPLAEVL 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-553 |
9.18e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.49 E-value: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI--LRDVSFTIPQGRRLAIVGPSGAGKSTL---ANLLlgffdyQR---GSLQLGGREVRDYHQS 406
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLircINLL------ERptsGRVLVDGQDLTALSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 KLMA---HMAVVAQRTHLFNA-TVRENILLARPGASEKEmiqAARRARIHDF--ILTLPEGYDTYVGEgglkLSGGQRQR 480
Cdd:PRK11153 76 ELRKarrQIGMIFQHFNLLSSrTVFDNVALPLELAGTPK---AEIKARVTELleLVGLSDKADRYPAQ----LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHL-VGLECMDEILVLVEGKVVEKGT 553
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMdVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-559 |
9.93e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.84 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlMAHMAV--VA 416
Cdd:cd03218 5 NLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 417 QRTHLF-NATVRENILLARPGASEKEMIQAARR-ARIHDFILTlpegydTYVGEGGLKLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03218 82 QEASIFrKLTVEENILAVLEIRGLSKKEREEKLeELLEEFHIT------HLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 495 ILDEVTAGLDPVVGREImQDLFQLMKDK-TSLVISHHLV--GLECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:cd03218 156 LLDEPFAGVDPIAVQDI-QKIIKILKDRgIGVLITDHNVreTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
335-552 |
1.03e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 96.67 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI--LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyHQSKLMA-- 410
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEPAEArr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 HMAVVAQRTHLFN-ATVRENILLArpgASEKEMIQAARRARIHDFILTLpeGYDTYVGEGGLKLSGGQRQRVAIARAILK 489
Cdd:cd03266 79 RLGFVSDSTGLYDrLTARENLEYF---AGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 490 NASVLILDEVTAGLDpVVGREIMQDLFQLMKD--KTSLVISHHLVGLECM-DEILVLVEGKVVEKG 552
Cdd:cd03266 154 DPPVLLLDEPTTGLD-VMATRALREFIRQLRAlgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-558 |
1.45e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAK-DPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQR--THLFNATVRENIL--LARPGASEKEMIQAARRA----RIHDFILTLPEgydtyvgegglKLSGGQRQRVAIAR 485
Cdd:PRK13642 85 MVFQNpdNQFVGATVEDDVAfgMENQGIPREEMIKRVDEAllavNMLDFKTREPA-----------RLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLmKDK---TSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-553 |
1.58e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.56 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFF---DYQRGSLQLGGREVRDYHQSKLMAH 411
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQR--THLFNATVRENIL--LARPGASEKEMIQAARRA----RIHDFILTLPEgydtyvgegglKLSGGQRQRVAI 483
Cdd:PRK13640 86 VGIVFQNpdNQFVGATVGDDVAfgLENRAVPRPEMIKIVRDVladvGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGLECMDEILVLVEGKVVEKGT 553
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-527 |
1.64e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.03 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLLGFFDYQR--GSLQLGGREV--RDYHQSK 407
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPGARveGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQRTHLFNATVRENILLA------RPGASEKEMIQAA-RRA--------RIHDFiltlpegydtyvgegGLK 472
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAalwdevkdRLKKS---------------ALG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 473 LSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREImQDLFQLMKDKTSLVI 527
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELILELKKDYTIVI 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
352-543 |
1.91e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 96.00 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLmahmaVVAQRTHLFN-ATVRENI 430
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLA----RPGASEKEmiqaaRRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:TIGR01184 76 ALAvdrvLPDLSKSE-----RRAIVEEHIalVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 134052199 505 PVVGREIMQDLFQLMKDK--TSLVISHHLvglecmDEILVL 543
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHrvTVLMVTHDV------DEALLL 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
334-560 |
3.06e-22 |
|
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: 96.85 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFdYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNATVRENiLLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03289 81 VIPQKVFIFSGTFRKN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVG-LECmDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAmLEC-QRFLVIEENKVRQYDSIQKLLNE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
335-560 |
5.31e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRD--YHQSKLM 409
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQ--RTHLFNATVRENILLA--RPGASEKEMIQAARRARIhdfILTLPegYDTYVGEGGLKLSGGQRQRVAIAR 485
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 486 AILKNASVLILDEVTAGLDPvVGREIMQDLFQLMKDK---TSLVISHHLVGL-ECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDP-KGRDEILNKIKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
335-552 |
6.52e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.82 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHqsKLMAHMAV 414
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLARpgasekeMIQAARRARIHDFILTLpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASV 493
Cdd:cd03268 77 LIEAPGFYpNLTARENLRLLA-------RLLGIRKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 494 LILDEVTAGLDPVVGREiMQDLFQLMKD--KTSLVISHHLVGLECM-DEILVLVEGKVVEKG 552
Cdd:cd03268 148 LILDEPTNGLDPDGIKE-LRELILSLRDqgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
335-559 |
7.00e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.77 E-value: 7.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRD----YHQSKLMA 410
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvdERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 411 HMavVAQRTHLF-NATVRENILLArP----GASEKEMIQAARRarihdfILT---LPEGYDTYVGEgglkLSGGQRQRVA 482
Cdd:PRK09493 80 GM--VFQQFYLFpHLTALENVMFG-PlrvrGASKEEAEKQARE------LLAkvgLAERAHHYPSE----LSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 483 IARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFaeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
347-552 |
8.17e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.26 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 347 KDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ---RGSLQLGGREVRDYHQSKLMAHmaVVAQRTHLFN 423
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCVAY--VRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATVRENILLARPGASEKEMIQAARRARIHDFILTlpEGYDTYVGEGGLK-LSGGQRQRVAIARAILKNASVLILDEVTAG 502
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 503 LDPVVGREIMQDLFQLMKDKTSLVISHHLVG---LECMDEILVLVEGKVVEKG 552
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
333-558 |
9.83e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYsAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLM--- 409
Cdd:PRK13636 4 YILKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AHMAVVAQR--THLFNATVRENILLA--RPGASEKEMIQAARRARIHDFILTLPEGyDTYVgegglkLSGGQRQRVAIAR 485
Cdd:PRK13636 82 ESVGMVFQDpdNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 486 AILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHH---LVGLECmDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHdidIVPLYC-DNVFVMKEGRVILQGNPKEVF 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-504 |
1.09e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 337 FNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmAHMAVVA 416
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 417 QRTHLF-NATVRENI----------------LLARPGASEKEMIQAAR-------------RARIHDFILTL---PEGYD 463
Cdd:COG0488 68 QEPPLDdDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAElqeefealggweaEARAEEILSGLgfpEEDLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 134052199 464 TYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-573 |
2.02e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.79 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK------- 407
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 --LMAHMavvaqrthlfnaTVRENIL-LAR-PGASEKEmiqAARRArihDFILT---LPEGYDTYVGEgglkLSGGQRQR 480
Cdd:COG4152 80 rgLYPKM------------KVGEQLVyLARlKGLSKAE---AKRRA---DEWLErlgLGDRANKKVEE----LSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPvVGREIMQDLFQLMKDKTSLVI--SH--HLVGLECmDEILVLVEGKVVEKGTHSQ 556
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDP-VNVELLKDVIRELAAKGTTVIfsSHqmELVEELC-DRIVIINKGRKVLSGSVDE 215
|
250
....*....|....*..
gi 134052199 557 LLEQGGvyARMWQLSVR 573
Cdd:COG4152 216 IRRQFG--RNTLRLEAD 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-552 |
2.38e-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: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK------- 407
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 --LMAHMAVVAQRTHLfnatvrenillarpgASEKEMIQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAI 483
Cdd:cd03269 79 rgLYPKMKVIDQLVYL---------------AQLKGLKKEEARRRIDEWLerLELSEYANKRVEE----LSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKG 552
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELveELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-560 |
2.98e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK---- 407
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQ--RTHLFNATVRENILLArP---GASEKEMIQAARRArihdfiLTLPEGYDTYVGEGGLKLSGGQRQRVA 482
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-PqnfGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 483 IARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVG--LECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDdvANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
352-557 |
4.59e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.15 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFF--DYQRGS--------LQLGGREVRDYHQSKlmAHMAVVAQRTHL 421
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgrtVQREGRLARDIRKSR--ANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 422 FNA-TVRENILLARPGAS--------------EKEMIQAARRArihdfiltlpeGYDTYVGEGGLKLSGGQRQRVAIARA 486
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRV-----------GMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 487 ILKNASVLILDEVTAGLDPVVGREIMQDLFQL-MKDKTSLVISHHLV--GLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVdyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-561 |
5.60e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMA 413
Cdd:PRK11231 2 TLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRtHLF--NATVRE---------NILLARPGASEKEMI-QAARRARIHDFIltlpegyDTYVGEgglkLSGGQRQRV 481
Cdd:PRK11231 80 LLPQH-HLTpeGITVRElvaygrspwLSLWGRLSAEDNARVnQAMEQTRINHLA-------DRRLTD----LSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPVVGREIMqDLFQLMKD--KTSLVISHHL--VGLECmDEILVLVEGKVVEKGTHSQL 557
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELM-RLMRELNTqgKTVVTVLHDLnqASRYC-DHLVVLANGHVMAQGTPEEV 225
|
....
gi 134052199 558 LEQG 561
Cdd:PRK11231 226 MTPG 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
335-551 |
6.70e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.46 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHqsklmAHMAV 414
Cdd:PRK11248 2 LQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFN-ATVRENIL--LARPGASEKEMIQAARRArihdFILTLPEGYDT-YVGEgglkLSGGQRQRVAIARAILKN 490
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVAfgLQLAGVEKMQRLEIAHQM----LKKVGLEGAEKrYIWQ----LSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 491 ASVLILDEVTAGLDpVVGREIMQD-LFQLMKD--KTSLVISHHLVGLECMDEILVLVE---GKVVEK 551
Cdd:PRK11248 147 PQLLLLDEPFGALD-AFTREQMQTlLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSpgpGRVVER 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-558 |
6.97e-21 |
|
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: 94.41 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQS-KLMAH---MAVVAQRTHLF-NATVRE 428
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEkrrIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLARPGASEKEmiQAARRARIHDFIltlpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:TIGR02142 95 NLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 509 REIMQDLFQLMK--DKTSLVISHHLVGLECMDEILVLVE-GKVVEKGTHSQLL 558
Cdd:TIGR02142 168 YEILPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEdGRVAAAGPIAEVW 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-552 |
7.68e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 91.63 E-value: 7.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLH--FRYSAKDPWI-----------------LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQL 395
Cdd:cd03267 1 IEVSNLSksYRVYSKEPGLigslkslfkrkyreveaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 396 GGrEVRDYHQSKLMAHMAVV-AQRTHL-FNATVRENILLARPGASEKEMIQAARRARIHDfILTLPEGYDTYVgeggLKL 473
Cdd:cd03267 81 AG-LVPWKRRKKFLRRIGVVfGQKTQLwWDLPVIDSFYLLAAIYDLPPARFKKRLDELSE-LLDLEELLDTPV----RQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 474 SGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGLE-CMDEILVLVEGKVVE 550
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEaLARRVLVIDKGRLLY 234
|
..
gi 134052199 551 KG 552
Cdd:cd03267 235 DG 236
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
334-561 |
8.88e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.67 E-value: 8.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEfnNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ--RGSLQLGGREVRDyhqsklmah 411
Cdd:COG0396 2 EIK--NLHVSVEGKE--ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILE--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVvAQRthlfnatVRENILLAR------PGASEKEMIQAARRAR------IHDFI---------LTLPEGY-DTYVGEG 469
Cdd:COG0396 69 LSP-DER-------ARAGIFLAFqypveiPGVSVSNFLRTALNARrgeelsAREFLkllkekmkeLGLDEDFlDRYVNEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 470 glkLSGGQRQRVAIARAILKNASVLILDEVTAGLD----PVVGREIMqdlfQLMKDKTS-LVISHHLVGLECM--DEILV 542
Cdd:COG0396 141 ---FSGGEKKRNEILQMLLLEPKLAILDETDSGLDidalRIVAEGVN----KLRSPDRGiLIITHYQRILDYIkpDFVHV 213
|
250 260
....*....|....*....|..
gi 134052199 543 LVEGKVVEKGTHS---QLLEQG 561
Cdd:COG0396 214 LVDGRIVKSGGKElalELEEEG 235
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-549 |
1.09e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV---RDYHQSKLMAH-----MAVVAqrthlF 422
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEYKRAKYIGRvfqdpMMGTA-----P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 423 NATVRENILLA---------RPGasekemIQAARRARIHDFILTLPEGY----DTYVGegglKLSGGQRQRVAIARAILK 489
Cdd:COG1101 96 SMTIEENLALAyrrgkrrglRRG------LTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 490 NASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLV-GLECMDEILVLVEGKVV 549
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
334-557 |
1.96e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.07 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLL--------------------GFFD 387
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtgtiewifkdeknkkktKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 388 YQRGSLQLGGREVRDYHQSK-LMAHMAVVAQ--RTHLFNATVRENILL-ARPGASEKEmiQAARRARIHDFILTLPEgyd 463
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKKIKeIRRRVGVVFQfaEYQLFEQTIEKDIIFgPVSMGVSKE--EAKKRAAKYIELVGLDE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 464 TYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHLVG-LECMDEIL 541
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNvLEWTKRTI 236
|
250
....*....|....*..
gi 134052199 542 VLVEGKVVEKG-THSQL 557
Cdd:PRK13651 237 FFKDGKIIKDGdTYDIL 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
351-552 |
2.04e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHL-FNATVREN 429
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 ILLAR-PGASEKEMIQAARRARIHDFILTLpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLD---P 505
Cdd:PRK09536 98 VEMGRtPHRSRFDTWTETDRAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 134052199 506 VVGREIMQDLFQlmKDKTSLVISH--HLVGLECmDEILVLVEGKVVEKG 552
Cdd:PRK09536 176 VRTLELVRRLVD--DGKTAVAAIHdlDLAARYC-DELVLLADGRVRAAG 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
300-530 |
2.04e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 300 LEESMSAAKRLFELAETENYSPSRkdeqfvpkgyEIEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLA 379
Cdd:COG4178 338 FEEALEAADALPEAASRIETSEDG----------ALALEDLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 380 NLLLGFFDYQRGSLQLGGREvrdyhqsklmaHMAVVAQRTHLFNATVREniLLARPGA----SEKEMIQAARRARIHDFI 455
Cdd:COG4178 407 RAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLRE--ALLYPATaeafSDAELREALEAVGLGHLA 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 456 LTLPEGYDTyvgegGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHH 530
Cdd:COG4178 474 ERLDEEADW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
334-553 |
2.28e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 334 EIEFNNLHFRYSAKDPW---ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGG----------REV 400
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 401 RDyhqskLMAHMAVVAQ--RTHLFNATVRENILLA--RPGASEKEMIQaarraRIHDFI--LTLPEgydTYVGEGGLKLS 474
Cdd:PRK13645 86 KR-----LRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK-----KVPELLklVQLPE---DYVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 475 GGQRQRVAIARAILKNASVLILDEVTAGLDPvVGREIMQDLF-QLMKD--KTSLVISHHLVG-LECMDEILVLVEGKVVE 550
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDP-KGEEDFINLFeRLNKEykKRIIMVTHNMDQvLRIADEVIVMHEGKVIS 231
|
...
gi 134052199 551 KGT 553
Cdd:PRK13645 232 IGS 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
352-548 |
2.30e-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: 88.64 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAH-MAVVA---QRTHLF-NATV 426
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVlDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENILLARPgasekemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDpv 506
Cdd:cd03215 96 AENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD-- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 134052199 507 VG--REIMQDLFQLMKD-KTSLVIS---HHLVGLeCmDEILVLVEGKV 548
Cdd:cd03215 137 VGakAEIYRLIRELADAgKAVLLISselDELLGL-C-DRILVMYEGRI 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-529 |
2.62e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.50 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmAHMAV 414
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQrthlfnatvrenillarpgasekemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*
gi 134052199 495 ILDEVTAGLDpVVGREIMQDLFQlMKDKTSLVISH 529
Cdd:cd03221 93 LLDEPTNHLD-LESIEALEEALK-EYPGTVILVSH 125
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
335-557 |
4.69e-20 |
|
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: 88.97 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyHQSKLMAHMAV 414
Cdd:cd03265 1 IEVENLVKKYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNA-TVRENILL-AR----PGASEKEmiqaaRRARIHDFIlTLPEGYDTYVGegglKLSGGQRQRVAIARAIL 488
Cdd:cd03265 78 VFQDLSVDDElTGWENLYIhARlygvPGAERRE-----RIDELLDFV-GLLEAADRLVK----TYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 489 KNASVLILDEVTAGLDPVVgREIMQDLFQLMKDK---TSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQL 557
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQT-RAHVWEYIEKLKEEfgmTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-558 |
8.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.66 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYhqSKLMAHMAV 414
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF--SKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VA-----QRTHLFNATVRENIL-----LARPGASEKEMIQAArrarihdfiltLPE-GYDTYVGEGGLKLSGGQRQRVAI 483
Cdd:PRK13644 79 VGivfqnPETQFVGRTVEEDLAfgpenLCLPPIEIRKRVDRA-----------LAEiGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISHHLVGLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
341-505 |
1.14e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.54 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 341 HFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGF----FDYQrGSLQLGGREVRDY--HQSklmaHMAV 414
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspaFSAS-GEVLLNGRRLTALpaEQR----RIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLARPGASEKemiqAARRARIHDfilTLPEgydtyVGEGGL------KLSGGQRQRVAIARAI 487
Cdd:COG4136 81 LFQDDLLFpHLSVGENLAFALPPTIGR----AQRRARVEQ---ALEE-----AGLAGFadrdpaTLSGGQRARVALLRAL 148
|
170
....*....|....*...
gi 134052199 488 LKNASVLILDEVTAGLDP 505
Cdd:COG4136 149 LAEPRALLLDEPFSKLDA 166
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
352-557 |
1.14e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.28 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRdYHQSK--LMAHMAVVAQRTHLF-NATVRE 428
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASTTaaLAAGVAIIYQELHLVpEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLAR-PGAS----EKEMIQAARRARIHdfiLTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:PRK11288 99 NLYLGQlPHKGgivnRRLLNYEAREQLEH---LGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 504 DpvvGREIMQdLFQLMKD-----KTSLVISHHlvglecMDEIL-------VLVEGKVVEkgTHSQL 557
Cdd:PRK11288 172 S---AREIEQ-LFRVIRElraegRVILYVSHR------MEEIFalcdaitVFKDGRYVA--TFDDM 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
335-552 |
1.34e-19 |
|
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: 87.20 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHfrYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ--RGSLQLGGREVRDyhqsklmahM 412
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITD---------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVvaqrthlfNATVRENILLARPGASEKEMIqaarraRIHDFIltlpegydTYVGEGglkLSGGQRQRVAIARAILKNAS 492
Cdd:cd03217 70 PP--------EERARLGIFLAFQYPPEIPGV------KNADFL--------RYVNEG---FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 493 VLILDEVTAGLDPVVGREIMQDLFQLMKDKTS-LVISHHLVGLECM--DEILVLVEGKVVEKG 552
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSvLIITHYQRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
351-557 |
1.40e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.53 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMA---HMAVVAQRTHLF-NATV 426
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHArdrKVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENILLA--------RPGASE--------KEMIQAARrarihdfiltLPEGYDTyvgegglKLSGGQRQRVAIARAILKN 490
Cdd:PRK10851 92 FDNIAFGltvlprreRPNAAAikakvtqlLEMVQLAH----------LADRYPA-------QLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 491 ASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISH-HLVGLECMDEILVLVEGKVVEKGTHSQL 557
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-559 |
1.65e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV-RDYHQSKlmAHMA 413
Cdd:PRK13537 8 IDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHAR--QRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLF-NATVRENILLArpgASEKEMIQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKN 490
Cdd:PRK13537 84 VVPQFDNLDpDFTVRENLLVF---GRYFGLSAAAARALVPPLLefAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 491 ASVLILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLLE 559
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
352-531 |
1.77e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrdyhqsklmAHMAVVAQRTHL---FNATVRE 428
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpdsLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NI---------LLARPGASEKEMIQAA-RRARIHDFIltlpegyDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDE 498
Cdd:NF040873 77 LVamgrwarrgLWRRLTRDDRAAVDDAlERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....
gi 134052199 499 VTAGLDPVVGREIMQDLFQLMKDK-TSLVISHHL 531
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGaTVVVVTHDL 179
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-310 |
1.85e-19 |
|
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: 89.02 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYK 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 98 AIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLS----PPLVALLTLGVVFFLlacfDLRMAFIFLAFFIGAAVVV 173
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTvlvrDPLTVIGLLGVLFYL----DWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 174 PIFIRAWgRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNL 253
Cdd:cd18552 157 RRIGKRL-RKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 254 AMWTILVMAIIKVEQGEL-PGVYIAMLAlATLSAFEAVTPLPLTFIYLEESMSAAKRL 310
Cdd:cd18552 236 AIALVLWYGGYQVISGELtPGEFISFIT-ALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
335-560 |
3.02e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.55 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTL---ANLLLgffDYQRGSLQLGGREVRDYHQSKLMAH 411
Cdd:COG4598 9 LEVRDLHKSFGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLLE---TPDSGEIRVGGEEIRLKPDRDGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQ----RTHL------FN----ATVRENILLArP----GASEKEMIQAARR--ARIhdfilTLPEGYDTYVGEggl 471
Cdd:COG4598 84 PADRRQlqriRTRLgmvfqsFNlwshMTVLENVIEA-PvhvlGRPKAEAIERAEAllAKV-----GLADKRDAYPAH--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 472 kLSGGQRQRVAIARAILKNASVLILDEVTAGLDPvvgrEIMQDLFQLMKD-----KTSLVISHHLvGL--ECMDEILVLV 544
Cdd:COG4598 155 -LSGGQQQRAAIARALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRDlaeegRTMLVVTHEM-GFarDVSSHVVFLH 228
|
250
....*....|....*.
gi 134052199 545 EGKVVEKGTHSQLLEQ 560
Cdd:COG4598 229 QGRIEEQGPPAEVFGN 244
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-284 |
3.39e-19 |
|
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: 88.26 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 22 VLLGFLAVGSNIGLLTTSAYLISRA-------AQHPPVLDLMVAIVGVrffGIARAVFRYLERYFSHDVTFRVLSNMRVW 94
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIidsviggGLRELLWLLALLILGV---ALLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 95 FYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVP 174
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 175 IFIR----AWGRRSGQ-GILGSKAQLNtclvdgIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGL 249
Cdd:cd18542 158 VFFKkvrpAFEEIREQeGELNTVLQEN------LTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDF 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 134052199 250 CMNLAMWTILVMAIIKVEQGEL-PGVYIAMLALATL 284
Cdd:cd18542 232 LSGLQIVLVLWVGGYLVINGEItLGELVAFISYLWM 267
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
351-559 |
3.92e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGffdYQRGSLQLGGREVRDYH--QSKLMAHMAVVAQRTHLF--NATV 426
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF---RSPKGVKGSGSVLLNGMpiDAKEMRAISAYVQQDDLFipTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENILLARPGASEKEMIQAARRARIHDFI--LTLPEGYDTYVGEGGLK--LSGGQRQRVAIARAILKNASVLILDEVTAG 502
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 503 LDPVVGREIMQDLFQL-MKDKTSLVISH----HLVGLecMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLaQKGKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-559 |
4.42e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLLGFFDYQR--GSLQLGGREV--RDYHQ 405
Cdd:PRK14267 3 FAIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEARveGEVRLFGRNIysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 406 SKLMAHMAVVAQRTHLF-NATVRENIL-------LARPGASEKEMIQ-AARRARIHDFILTLPEGYDTyvgegglKLSGG 476
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFpHLTIYDNVAigvklngLVKSKKELDERVEwALKKAALWDEVKDRLNDYPS-------NLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 477 QRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLV-GLECMDEILVLVEGKVVEKGTHS 555
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGKLIEVGPTR 233
|
....
gi 134052199 556 QLLE 559
Cdd:PRK14267 234 KVFE 237
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
351-558 |
7.34e-19 |
|
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: 86.78 E-value: 7.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---HMAVVAQRTH-LFNA-- 424
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQDSPsAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 TVRENIllARPGASEKEMIQAARRARIHDFILTL---PEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTA 501
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLDMVglrSEDADKLPRQ----LSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 502 GLDPVVGREIMQDLFQLMKD--KTSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLL 558
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
350-552 |
7.65e-19 |
|
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: 85.66 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 350 WILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAHMAvvaqrthlFN--ATVR 427
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGG--------FNpeLTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENI-LLAR-PGASEKEMiqAARRARIHDFIlTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAgldp 505
Cdd:cd03220 103 ENIyLNGRlLGLSRKEI--DEKIDEIIEFS-ELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLA---- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 506 vVG----REIMQDLFQ--LMKDKTSLVISHHLVGLE--CmDEILVLVEGKVVEKG 552
Cdd:cd03220 172 -VGdaafQEKCQRRLRelLKQGKTVILVSHDPSSIKrlC-DRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-562 |
8.51e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLhfRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyhQSKLM-AHMA 413
Cdd:PRK13536 42 IDLAGV--SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLArARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHL-FNATVRENILL----ARPGASEKE-----MIQAARrarihdfiltLPEGYDTYVGEgglkLSGGQRQRVAI 483
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVfgryFGMSTREIEavipsLLEFAR----------LESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISHHLVGLECM-DEILVLVEG-KVVEKGTHSQLLEQ 560
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGrKIAEGRPHALIDEH 263
|
..
gi 134052199 561 GG 562
Cdd:PRK13536 264 IG 265
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
351-530 |
8.83e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLlGFFDY-QRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLF-NA 424
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKpTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYHLLsHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 TVRENILL-ARPGASEKemiqAARRARIHDFILTLpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:PRK10535 102 TAAQNVEVpAVYAGLER----KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180
....*....|....*....|....*..
gi 134052199 504 DPVVGREIMQDLFQLMKDKTSLVISHH 530
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
335-558 |
9.89e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV---RDYHQSK---- 407
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 -LMAHMAVVAQRTHLF-NATVRENIL---LARPGASEKEMIQAARR--ARIHdfiLTLPEgyDTYvgegGLKLSGGQRQR 480
Cdd:PRK11264 82 qLRQHVGFVFQNFNLFpHRTVLENIIegpVIVKGEPKEEATARAREllAKVG---LAGKE--TSY----PRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFarDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-552 |
1.29e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLLGFFDYQR--GSLQLGGREVRDYHQSKLMAHMAVVAQRTH-LFNA 424
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEARvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 TVRENILLA----RPGASEKEMIQAAR----RARIHDFI---LTLPEGydtyvgegglKLSGGQRQRVAIARAILKNASV 493
Cdd:PRK14247 98 SIFENVALGlklnRLVKSKKELQERVRwaleKAQLWDEVkdrLDAPAG----------KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 494 LILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHH-LVGLECMDEILVLVEGKVVEKG 552
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFpQQAARISDYVAFLYKGQIVEWG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
335-553 |
1.35e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKlmAHMAV 414
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLA-----RPGAS-EKEMIQAARRARIHDFILTLPegydtyvgeggLKLSGGQRQRVAIARAI 487
Cdd:PRK09452 91 VFQSYALFpHMTVFENVAFGlrmqkTPAAEiTPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 488 LKNASVLILDEVTAGLDPVVgREIMQ-DLFQLMKdktSLVISHHLV------GLECMDEILVLVEGKVVEKGT 553
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKL-RKQMQnELKALQR---KLGITFVFVthdqeeALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
335-566 |
1.79e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAkDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAV 414
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRT--HLFNATVRENILLarpGASEKEMIQAARRARIHDFILTLpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNAS 492
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAF---GPINLGLDEETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 493 VLILDEVTAGLDPvvgrEIMQDLFQLMKD-----KTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHSQLLEQGGVYA 565
Cdd:PRK13652 158 VLVLDEPTAGLDP----QGVKELIDFLNDlpetyGMTVIFSTHQLDLvpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
.
gi 134052199 566 R 566
Cdd:PRK13652 234 R 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-550 |
1.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI---LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK---- 407
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQ--RTHLFNATVRENILLArP---GASEKEMIQAA----RRARIHDFILTlpegydtyvgEGGLKLSGGQR 478
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFG-PknfGFSEDEAKEKAlkwlKKVGLSEDLIS----------KSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 479 QRVAIARAILKNASVLILDEVTAGLDPvVGREimqDLFQLMKD-----KTSLVISHHLVGL-ECMDEILVLVEGKVVE 550
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDP-EGRK---EMMQLFKDyqkagHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
352-549 |
2.11e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV--RDYHQSkLMAHMAVVA---QRTHLF-NAT 425
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVriRSPRDA-IRAGIAYVPedrKGEGLVlDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 426 VRENILLARPGA-------SEKEMIQAARRArIHDFILTLPeGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDE 498
Cdd:COG1129 347 IRENITLASLDRlsrggllDRRRERALAEEY-IKRLRIKTP-SPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 499 VTAGLDpvVG--REIMQDLFQLMKDKTS-LVIS---HHLVGLeCmDEILVLVEGKVV 549
Cdd:COG1129 421 PTRGID--VGakAEIYRLIRELAAEGKAvIVISselPELLGL-S-DRILVMREGRIV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
335-557 |
3.53e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevRDYHQSKLMAH--- 411
Cdd:PRK15439 12 LCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENIL--LARPGASEKEMIQAARRARIHdfiltlpegYDTYVGEGGLKLSggQRQRVAIARAIL 488
Cdd:PRK15439 88 IYLVPQEPLLFpNLSVKENILfgLPKRQASMQKMKQLLAALGCQ---------LDLDSSAGSLEVA--DRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 489 KNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLV-ISHHLVGL-ECMDEILVLVEGKVVEKGTHSQL 557
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
311-550 |
3.81e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.72 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 311 FELAeteNYSPSRKDEQFVPKGYEIEFNNLHFRYsAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQR 390
Cdd:PRK10522 302 LALA---PYKAEFPRPQAFPDWQTLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 391 GSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENILLARPGASEK--EMIQAARRARIHDFILTLpegydtyvge 468
Cdd:PRK10522 378 GEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPANPALVEKwlERLKMAHKLELEDGRISN---------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 469 ggLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHLVGLECMDEILVLVEG 546
Cdd:PRK10522 448 --LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNG 525
|
....
gi 134052199 547 KVVE 550
Cdd:PRK10522 526 QLSE 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
335-563 |
4.06e-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: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAH-MA 413
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFN-ATVRENILLARPGASEKEMIQaaRRARIHDFiltLPEGYDTYVGEGGlKLSGGQRQRVAIARAILKNAS 492
Cdd:PRK11614 84 IVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 493 VLILDEVTAGLDPVVGREIMQDLFQLMKDKTS--LVISHHLVGLECMDEILVLVEGKVVEKGTHSQLLEQGGV 563
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
352-552 |
4.41e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENIL 431
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 432 LAR---------PGASEKEMIQAArRARIhdfilTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAG 502
Cdd:PRK15056 103 MGRyghmgwlrrAKKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 134052199 503 LDPVVGREIMQDLFQLMKD-KTSLVISHHLVGLECMDEILVLVEGKVVEKG 552
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-553 |
1.02e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRY--------------------SAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQ 394
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 395 LGGRevrdyhQSKLMAHMAVvaqrthlFN--ATVRENILL-ARP-GASEKEMiqAARRARIHDF--IltlpEGY-DTYVG 467
Cdd:COG1134 85 VNGR------VSALLELGAG-------FHpeLTGRENIYLnGRLlGLSRKEI--DEKFDEIVEFaeL----GDFiDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 468 egglKLSGGQRQRVAIARAILKNASVLILDEVTAgldpvVG--------REIMQDLFQlmKDKTSLVISHHLVGLE--Cm 537
Cdd:COG1134 146 ----TYSSGMRARLAFAVATAVDPDILLVDEVLA-----VGdaafqkkcLARIRELRE--SGRTVIFVSHSMGAVRrlC- 213
|
250
....*....|....*.
gi 134052199 538 DEILVLVEGKVVEKGT 553
Cdd:COG1134 214 DRAIWLEKGRLVMDGD 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
351-543 |
1.18e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQlggrevrdyHQSKLmaHMAVVAQRTHL---FNATVR 427
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL--RIGYVPQKLYLdttLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENILLaRPGASEKEMIQAARR---ARIHDFILTlpegydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:PRK09544 88 RFLRL-RPGTKKEDILPALKRvqaGHLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 134052199 505 pVVGREIMQDLFQLMKDKTS---LVISH--HLVgLECMDEILVL 543
Cdd:PRK09544 153 -VNGQVALYDLIDQLRRELDcavLMVSHdlHLV-MAKTDEVLCL 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-563 |
1.47e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.13 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMA---HMAVV 415
Cdd:PRK13638 6 DLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLAlrqQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 416 AQ--RTHLFNATVRENIL--LARPGASEKEMiqaARRArihDFILTLPEGyDTYVGEGGLKLSGGQRQRVAIARAILKNA 491
Cdd:PRK13638 83 FQdpEQQIFYTDIDSDIAfsLRNLGVPEAEI---TRRV---DEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 492 SVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKG------THSQLLEQGGV 563
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLiyEISDAVYVLRQGQILTHGapgevfACTEAMEQAGL 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
351-540 |
1.76e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGRevrDYHQSKLMAHMAVVAQRTHLFNA-TVREN 429
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLGHRNAMKPAlTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 ILLARP--GASEKEMIQAARRARIHDfILTLPEGYdtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDpVV 507
Cdd:PRK13539 94 LEFWAAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD-AA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 134052199 508 GREIMQDLFQLMKDKTSLVI--SHHLVGLECMDEI 540
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIaaTHIPLGLPGAREL 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
335-560 |
2.02e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.51 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPW--ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ----RGSLQLGGREVRDYHQSKL 408
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 409 MA----HMAVVAQR--THLfN------ATVRENILL---ARPGASEKEMIQAARRARIHDfiltlPEG-YDTYVGEgglk 472
Cdd:COG4172 87 RRirgnRIAMIFQEpmTSL-NplhtigKQIAEVLRLhrgLSGAAARARALELLERVGIPD-----PERrLDAYPHQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 473 LSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLV-ISH--HLVGlECMDEILVLVEGKV 548
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLlITHdlGVVR-RFADRVAVMRQGEI 235
|
250
....*....|..
gi 134052199 549 VEKGTHSQLLEQ 560
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-531 |
2.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ-----RGSLQLGGREV--RDYHQSK 407
Cdd:PRK14258 8 IKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQRTHLFNATVRENILLA------RPGASEKEMIQAA-RRARIHDFIltlpegyDTYVGEGGLKLSGGQRQR 480
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREImQDLFQ---LMKDKTSLVISHHL 531
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQslrLRSELTMVIVSHNL 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-560 |
3.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWILR---DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK---- 407
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQ--RTHLFNATVRENILLARP--GASEKEMIQAArrARIHDFILTLPEGYDtyvgEGGLKLSGGQRQRVAI 483
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQnfGIPKEKAEKIA--AEKLEMVGLADEFWE----KSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVG--LECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDdvADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
341-504 |
4.08e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 341 HFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTH 420
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 LFNATVRENILLarPGASEKemiQAARRARIHDFI--LTLPEgydTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDE 498
Cdd:PRK10247 92 LFGDTVYDNLIF--PWQIRN---QQPDPAIFLDDLerFALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
....*.
gi 134052199 499 VTAGLD 504
Cdd:PRK10247 164 ITSALD 169
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
341-572 |
4.48e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 341 HFRYSAKDPW--ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSL--------QLGGREVRDYHQSKLM- 409
Cdd:PRK10419 15 HGGLSGKHQHqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRAQRKAFRRDIQMv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 ---AHMAVVAQRThlfnatVREniLLARPGASEKEMIQAARRARIHDFILTL---PEGYDTYVGEgglkLSGGQRQRVAI 483
Cdd:PRK10419 95 fqdSISAVNPRKT------VRE--IIREPLRHLLSLDKAERLARASEMLRAVdldDSVLDKRPPQ----LSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 484 ARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMK--DKTSLVISHHLVGLE--CmDEILVLVEGKVVEKGTHSQLLE 559
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVErfC-QRVMVMDNGQIVETQPVGDKLT 241
|
250
....*....|...
gi 134052199 560 QGGVYARMWQLSV 572
Cdd:PRK10419 242 FSSPAGRVLQNAV 254
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
352-558 |
5.73e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGG-----------REVRDYHQSKLMAHMAVVAQRTH 420
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 LFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEgydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVT 500
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 501 AGLDPVVGREIMQDLFQLM--KDKTSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
333-531 |
8.92e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.60 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTL------ANLLLGFFDYQrGSLQLGGREVRDYH-- 404
Cdd:PRK14243 9 TVLRTENLNVYYG--SFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrLNDLIPGFRVE-GKVTFHGKNLYAPDvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 405 QSKLMAHMAVVAQRTHLFNATVRENILL-ARPGASEKEMIQ----AARRARIHDfiltlpEGYDTyVGEGGLKLSGGQRQ 479
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPFPKSIYDNIAYgARINGYKGDMDElverSLRQAALWD------EVKDK-LKQSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 480 RVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHL 531
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
367-560 |
9.60e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 81.39 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 367 IVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRdyHQSKLMAHMAVVAQRTHLF-NATVRENIllARPGASEKEMiQA 445
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPHLRHINMVFQSYALFpHMTVEENV--AFGLKMRKVP-RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 446 ARRARIHDFILTLPEGydTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVgREIMQDLFQLMKDK--- 522
Cdd:TIGR01187 76 EIKPRVLEALRLVQLE--EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKL-RDQMQLELKTIQEQlgi 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 134052199 523 TSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMsDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-558 |
1.08e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 331 KGYEIEFNNLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLLGFFDYQ---RGSLQLGGREVRDYH 404
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlNRLIEIYDSKikvDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 405 QSKLMAHMAVVAQRTHLF-NATVRENIL--LARPGASEKEMIQAARRARIHDFILtLPEGYDTyVGEGGLKLSGGQRQRV 481
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFpHLSIYDNIAypLKSHGIKEKREIKKIVEECLRKVGL-WKEVYDR-LNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHH-LVGLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
354-513 |
1.31e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMavVAQRTHLF-NATVRENILL 432
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINM--MFQSYALFpHMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 433 arpGASEKEMIQAARRARIHDfILTLPEGYDtYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVgREIM 512
Cdd:PRK11607 115 ---GLKQDKLPKAEIASRVNE-MLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL-RDRM 188
|
.
gi 134052199 513 Q 513
Cdd:PRK11607 189 Q 189
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
352-558 |
1.34e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQrGSLQLGGREVRDYHQSKLMAHMAVVAQR-THLFNATVRENI 430
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLARPG-----ASEKEMIQAARRARIHDFiLTLPEGydtyvgegglKLSGGQRQRVAIARAILK-------NASVLILDE 498
Cdd:COG4138 91 ALHQPAgasseAVEQLLAQLAEALGLEDK-LSRPLT----------QLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 499 VTAGLDpvVGREIMQD--LFQLMKDKTSLVISHHLVGLECM--DEILVLVEGKVVEKGTHSQLL 558
Cdd:COG4138 160 PMNSLD--VAQQAALDrlLRELCQQGITVVMSSHDLNHTLRhaDRVWLLKQGKLVASGETAEVM 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-528 |
1.41e-16 |
|
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: 77.58 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREvrdyhqsklmaHMAV 414
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLFNATVREniLLARPGASEkemiqaarrarihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVL 494
Cdd:cd03223 69 LPQRPYLPLGTLRE--QLIYPWDDV---------------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....
gi 134052199 495 ILDEVTAGLDPvvgrEIMQDLFQLMKDKTSLVIS 528
Cdd:cd03223 114 FLDEATSALDE----ESEDRLYQLLKELGITVIS 143
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
18-279 |
1.64e-16 |
|
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: 80.12 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIglltTSAYLISRA-----AQHPPVLDLMVAIVGVrFFG--IARAVFRYLERYFSHDVTFRVLSN 90
Cdd:cd18544 1 FILALLLLLLATALEL----LGPLLIKRAiddyiVPGQGDLQGLLLLALL-YLGllLLSFLLQYLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 91 MRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAA 170
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 171 VVVPIFiRAWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLC 250
Cdd:cd18544 156 LATYLF-RKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELL 234
|
250 260 270
....*....|....*....|....*....|
gi 134052199 251 MNLAMWTILVMAIIKVEQGELP-GVYIAML 279
Cdd:cd18544 235 SSLALALVLWYGGGQVLSGAVTlGVLYAFI 264
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
351-531 |
1.84e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYH---QSKLMAH-MAVVAQRTHL---FN 423
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATvrENIllARPgasekEMIQAARRARIHDFILTLPE--GYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTA 501
Cdd:PRK11629 104 AL--ENV--AMP-----LLIGKKKPAEINSRALEMLAavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|..
gi 134052199 502 GLDPVVGREIMQDLFQL-MKDKTS-LVISHHL 531
Cdd:PRK11629 175 NLDARNADSIFQLLGELnRLQGTAfLVVTHDL 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
339-559 |
1.92e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDY--HQSklmAHMAV-- 414
Cdd:COG1137 8 NLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKR---ARLGIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 415 VAQRTHLF-NATVRENILLARpgasekEMIQ---AARRARIHDFI--LTLPEGYDTYvgegGLKLSGGQRQRVAIARAIL 488
Cdd:COG1137 83 LPQEASIFrKLTVEDNILAVL------ELRKlskKEREERLEELLeeFGITHLRKSK----AYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 489 KNASVLILDEVTAGLDPVVGREImQDLFQLMKDK-TSLVISHHLVglecmDEIL-------VLVEGKVVEKGTHSQLLE 559
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADI-QKIIRHLKERgIGVLITDHNV-----RETLgicdrayIISEGKVLAEGTPEEILN 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
339-558 |
2.06e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVR------------DYHQS 406
Cdd:PRK10619 10 DLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 407 KLM-AHMAVVAQRTHLFN-ATVRENILLArP----GASEKEmiqAARRArihdfILTLPE-GYDTYV-GEGGLKLSGGQR 478
Cdd:PRK10619 88 RLLrTRLTMVFQHFNLWShMTVLENVMEA-PiqvlGLSKQE---ARERA-----VKYLAKvGIDERAqGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 479 QRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHL-VGLECMDEILVLVEGKVVEKGTHSQ 556
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMgFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
..
gi 134052199 557 LL 558
Cdd:PRK10619 239 LF 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-556 |
2.10e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 82.62 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ--RGSLQLGGREVrdyhQSKLMAHMAVVAQRTHLF-NATVR 427
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENI----LLARPGASEKEMIQAARRARIHDFILTLPEgyDTYVGEGGLK-LSGGQRQRVAIARAILKNASVLILDEVTAG 502
Cdd:PLN03211 159 ETLvfcsLLRLPKSLTKQEKILVAESVISELGLTKCE--NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 503 LDPVVGREIMQDLFQLMKDKTSLVISHHLVG---LECMDEILVLVEGKVVEKGTHSQ 556
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPSsrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
351-560 |
2.54e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.53 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRdyHQSKLMAHMAVVAQRTHLF-NATVREN 429
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 I-----LLARPGASEKEMIQAArrarihdfiLTLP--EGY-DTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTA 501
Cdd:PRK11432 99 VgyglkMLGVPKEERKQRVKEA---------LELVdlAGFeDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 502 GLDPVVGREIMQDLFQLMK--DKTSLVISH-HLVGLECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-559 |
3.58e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQL------------------- 395
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 396 -------GGR---EVRDY------HQSKLMAHMAVVAQRTHLF--NATVRENILLARP--GASEKEMIQAARrarihDFI 455
Cdd:TIGR03269 79 gepcpvcGGTlepEEVDFwnlsdkLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEeiGYEGKEAVGRAV-----DLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 456 LTLPEGYD-TYVGEgglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK-TSLVISHHL-- 531
Cdd:TIGR03269 154 EMVQLSHRiTHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWpe 230
|
250 260
....*....|....*....|....*...
gi 134052199 532 VGLECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-558 |
3.70e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.98 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD----YQ-RGSLQLGGREVRDYHQS-KLMAHM 412
Cdd:PRK14271 26 NLTLGFAGKT--VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgYRySGDVLLGGRSIFNYRDVlEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRTHLFNATVRENILL---ARPGASEKEMiQAARRARIHDfiLTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILK 489
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAgvrAHKLVPRKEF-RGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 490 NASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLV-GLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-531 |
5.17e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwiLRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ-----RGSLQLGGREV--RDYHQSK 407
Cdd:PRK14239 6 LQVSDLSVYYNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQRTHLFNATVRENIL--LARPGASEKEMIQAA-----RRARIHDfiltlpEGYDtYVGEGGLKLSGGQRQR 480
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVygLRLKGIKDKQVLDEAvekslKGASIWD------EVKD-RLHDSALGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 134052199 481 VAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHL 531
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
352-558 |
6.51e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVR--DYHQSKLMAHMAVVAQRTHLfNATVREN 429
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDPSTSL-NPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 ILLARPGASEKEMIQAARRARIHDFILT---LPEGYDTYVGegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPV 506
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLRQvglLPDHASYYPH----MLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 507 VGREIMQDLFQLMKDK--TSLVISHHLVGLECM-DEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK15112 184 MRSQLINLMLELQEKQgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
339-557 |
1.06e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGG-------REV---RDYHQSKL 408
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVielSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 409 M----AHMAVVAQR--THL-----FNATVRENILLARPGASEKEMIQAAR---RARIhdfiltlPEGyDTYVGEGGLKLS 474
Cdd:PRK10261 99 RhvrgADMAMIFQEpmTSLnpvftVGEQIAESIRLHQGASREEAMVEAKRmldQVRI-------PEA-QTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 475 GGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLV--ISHHL-VGLECMDEILVLVEGKVVEK 551
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMgVVAEIADRVLVMYQGEAVET 250
|
....*.
gi 134052199 552 GTHSQL 557
Cdd:PRK10261 251 GSVEQI 256
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
335-560 |
1.33e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKD----PWILRDVSFTIPQGRRLAIVGPSGAGKSTLA---NLLLgffdyqrgsLQLGGREVRDYHQSK 407
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmNALL---------IPSEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 LMAHMAVVAQRTHL-FN-------ATVRENILLARP---GASEKEMiqaarRARIHDFILTLpeGYDTYVGEGGLKLSGG 476
Cdd:PRK13633 76 DEENLWDIRNKAGMvFQnpdnqivATIVEEDVAFGPenlGIPPEEI-----RERVDESLKKV--GMYEYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 477 QRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGLECMDEILVLVEGKVVEKGTH 554
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
....*.
gi 134052199 555 SQLLEQ 560
Cdd:PRK13633 229 KEIFKE 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
352-548 |
2.29e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYH-QSKLMAHMAVVAQ-RTH---LFNATV 426
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEdRKRdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENILLARPGASEKEMIQ---AARRARIHDFILTL----PeGYDTYVGegglKLSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:PRK10762 348 KENMSLTALRYFSRAGGSlkhADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 134052199 500 TAGLDPVVGREIMQDLFQLMKDKTS--LVISHHLVGLECMDEILVLVEGKV 548
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSiiLVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-552 |
3.79e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQrGSLQLGGREVRDYHQSKLMA---HMAVVAQRThlfNATV- 426
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLLPvrhRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 -RENIL-LARPG--ASEKEMIQAARRARIHDFILTL---PEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:PRK15134 377 pRLNVLqIIEEGlrVHQPTLSAAQREQQVIAVMEEVgldPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 500 TAGLDPVVGREIMQDLFQLMKDK--TSLVISH--HLVGLECmDEILVLVEGKVVEKG 552
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHqlAYLFISHdlHVVRALC-HQVIVLRQGEVVEQG 508
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-565 |
6.54e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLF-NATVRE 428
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekrRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NIllaRPGASEKemiqaarrarihdfiltLPEGYDTYVGEGGLK---------LSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:PRK11144 96 NL---RYGMAKS-----------------MVAQFDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 500 TAGLDPVVGREIMQDLFQLMKD-KTSLV-ISHHLvglecmDEILVLVEgkvvekgtHSQLLEQGGVYA 565
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREiNIPILyVSHSL------DEILRLAD--------RVVVLEQGKVKA 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
351-558 |
1.08e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.25 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQR-THLFNATVREN 429
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 I---------LLARPGASEKEMIQAARRArihdfiltlpEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVT 500
Cdd:PRK10253 102 VargryphqpLFTRWRKEDEEAVTKAMQA----------TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 501 AGLDPVVGREIMQDLFQLMKDKT-SLVISHHLVGLEC--MDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGyTLAAVLHDLNQACryASHLIALREGKIVAQGAPKEIV 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
354-553 |
1.31e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.15 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ---RGSLQLGGREV---RDYHQSKLMA-HMAVVAQ--RTHLfNA 424
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlPEKELNKLRAeQISMIFQdpMTSL-NP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 TVR-----ENILLARPGASEKE-------MIQAAR----RARI----HDFiltlpegydtyvgegglklSGGQRQRVAIA 484
Cdd:PRK09473 113 YMRvgeqlMEVLMLHKGMSKAEafeesvrMLDAVKmpeaRKRMkmypHEF-------------------SGGMRQRVMIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLV-ISHHL--VGLECmDEILVLVEGKVVEKGT 553
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLgvVAGIC-DKVLVMYAGRTMEYGN 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-548 |
1.55e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 320 SPSRkdeqfVPKGYEIEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLqLGGR- 398
Cdd:PRK11247 3 NTAR-----LNQGTPLLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 399 ---EVRDyhQSKLMAHMAVVaqrthLFNATVRENILLARPGASEKEMIQA------ARRArihdfiltlpegydtyvGEG 469
Cdd:PRK11247 75 plaEARE--DTRLMFQDARL-----LPWKKVIDNVGLGLKGQWRDAALQAlaavglADRA-----------------NEW 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 470 GLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREiMQDLFQLMKDK---TSLVISHHLVGLECM-DEILVLVE 545
Cdd:PRK11247 131 PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE-MQDLIESLWQQhgfTVLLVTHDVSEAVAMaDRVLLIEE 209
|
...
gi 134052199 546 GKV 548
Cdd:PRK11247 210 GKI 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-553 |
2.80e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 355 VSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDyHQSKLMAHMAVVA--QRTHLFNA-TVRENIL 431
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPGHQIARMGVVRtfQHVRLFREmTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 432 LAR---------------PGASEKEMIQAARRARIHDFIltlpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLIL 496
Cdd:PRK11300 103 VAQhqqlktglfsgllktPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 497 DEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISH--HLVgLECMDEILVLVEGKVVEKGT 553
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHdmKLV-MGISDRIYVVNQGTPLANGT 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
351-552 |
2.83e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMavVAQRTHLF-NATVREN 429
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM--VFQSYALYpHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 430 ----ILLARPGASE--KEMIQAARrarihdfILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:PRK11000 96 msfgLKLAGAKKEEinQRVNQVAE-------VLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 504 DPVVGREIMQDLFQLMK--DKTSLVISHHLVglECM---DEILVLVEGKVVEKG 552
Cdd:PRK11000 165 DAALRVQMRIEISRLHKrlGRTMIYVTHDQV--EAMtlaDKIVVLDAGRVAQVG 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-564 |
3.69e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNL--HFRYSAKDPWI-----------------LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQL 395
Cdd:COG4586 2 IEVENLskTYRVYEKEPGLkgalkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 396 GGRE-VRDyhQSKLMAHMAVV-AQRTHLF-NATVRENILLarpgasEKEM--IQAAR-RARIHDF--ILTLPEGYDTYVg 467
Cdd:COG4586 82 LGYVpFKR--RKEFARRIGVVfGQRSQLWwDLPAIDSFRL------LKAIyrIPDAEyKKRLDELveLLDLGELLDTPV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 468 eggLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGLE--CmDEILVL 543
Cdd:COG4586 153 ---RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEalC-DRVIVI 228
|
250 260
....*....|....*....|.
gi 134052199 544 VEGKVVEKGTHSQLLEQGGVY 564
Cdd:COG4586 229 DHGRIIYDGSLEELKERFGPY 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
317-560 |
4.18e-14 |
|
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: 74.84 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 317 ENYSPSRKDEQFVPKGYEIEFNNLHFRYSAKDPWILR---DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSL 393
Cdd:TIGR03269 262 EGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 394 Q-LGGREVRDYHQSKLMA------HMAVVAQRTHLF-NATVRENILLARPGASEKEMiqAARRArihdfILTLPE-GYDT 464
Cdd:TIGR03269 342 NvRVGDEWVDMTKPGPDGrgrakrYIGILHQEYDLYpHRTVLDNLTEAIGLELPDEL--ARMKA-----VITLKMvGFDE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 465 YVGEGGL-----KLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHL-VGLEC 536
Cdd:TIGR03269 415 EKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMdFVLDV 494
|
250 260
....*....|....*....|....
gi 134052199 537 MDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
351-549 |
5.03e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.14 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLL---LGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFNATVR 427
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 EnillarpgasekeMIQAARRARIHDFILtlpegydtyvgegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVV 507
Cdd:cd03233 102 E-------------TLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 134052199 508 GREIMQDLfQLMKDKTSLVIshhLVGL--------ECMDEILVLVEGKVV 549
Cdd:cd03233 154 ALEILKCI-RTMADVLKTTT---FVSLyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
355-560 |
9.65e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 355 VSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQrGSLQLGGREVRDYHQSKLMAHMAVVAQR-THLFNATVRENILLA 433
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 434 RP-----GASEKEMIQAARRARIHDFiLTLPEGydtyvgegglKLSGGQRQRVAIARAILK-------NASVLILDEVTA 501
Cdd:PRK03695 94 QPdktrtEAVASALNEVAEALGLDDK-LGRSVN----------QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 502 GLDpvVGREIMQD--LFQLMKDKTSLVISHHLVG--LECMDEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:PRK03695 163 SLD--VAQQAALDrlLSELCQQGIAVVMSSHDLNhtLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
355-557 |
1.86e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.70 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 355 VSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDY----QRGSLQLGGREVRDYHQS---KLM-AHMAVVAQ--RTHLFNA 424
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvMAEKLEFNGQDLQRISEKerrNLVgAEVAMIFQdpMTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 -TVRENILLA---RPGASEKEmiqaaRRARIHDfILTL-----PEG-YDTYVGEgglkLSGGQRQRVAIARAILKNASVL 494
Cdd:PRK11022 106 yTVGFQIMEAikvHQGGNKKT-----RRQRAID-LLNQvgipdPASrLDVYPHQ----LSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 495 ILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISHHLVGL--ECMDEILVLVEGKVVEKGTHSQL 557
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALvaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
42-287 |
2.32e-13 |
|
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: 70.64 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 42 LISRAAQHPPVLDLMVAIVGVRFfgiARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIVS 121
Cdd:cd18778 29 VTIGSKSLGLLLGLALLLLGAYL---LRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 122 DVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFI------FLAFFIG--AAVVVPIFiRAWGRRSGqgilgska 193
Cdd:cd18778 106 DVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtlipipFLALGAWlySKKVRPRY-RKVREALG-------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 194 QLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAmwTILVMAIikveqgelpG 273
Cdd:cd18778 177 ELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG--TVLVLGF---------G 245
|
250
....*....|....*..
gi 134052199 274 VYIAM---LALATLSAF 287
Cdd:cd18778 246 GRLVLageLTIGDLVAF 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
352-552 |
2.85e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMAHM--AVVAQRTHLFNA-TVRE 428
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAAQLgiGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLAR---------PGASEKEMIQaarRARIHDFILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:PRK09700 100 NLYIGRhltkkvcgvNIIDWREMRV---RAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 500 TAGLdpvVGREIMQdLF----QLMKDKTSLV-ISHHLVGL-ECMDEILVLVEGKVVEKG 552
Cdd:PRK09700 173 TSSL---TNKEVDY-LFlimnQLRKEGTAIVyISHKLAEIrRICDRYTVMKDGSSVCSG 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-559 |
3.97e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---HMAVVAQRTHLF---NATVR 427
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPYASldpRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENIL--LARPGASEKEMiQAARRARIHDFILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDP 505
Cdd:PRK10261 422 DSIMepLRVHGLLPGKA-AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 134052199 506 VVGREIMQDLFQLMKDK--TSLVISHHLVGLECMD-EILVLVEGKVVEKGTHSQLLE 559
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFgiAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-284 |
4.58e-13 |
|
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: 69.59 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 22 VLLGFLAVGSNIGLLTTSaYLISRAAQH------PPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWF 95
Cdd:pfam00664 2 ILAILLAILSGAISPAFP-LVLGRILDVllpdgdPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 96 YKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFY---LRVLSPPLVALLTLGVVFFLlacFDLRMAFIFLAFFIgAAVV 172
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLgekLGLLFQSLATIVGGIIVMFY---YGWKLTLVLLAVLP-LYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 173 VPIFIRAWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMN 252
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|...
gi 134052199 253 LAMWTILVMAIIKVEQGEL-PGVYIAMLALATL 284
Cdd:pfam00664 237 LSYALALWFGAYLVISGELsVGDLVAFLSLFAQ 269
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
355-553 |
4.82e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 355 VSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMAHMAVVAQRTHLFN-ATVRENILL- 432
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFy 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 433 ARPGASEKEMIQAARRARIHDfiltlpEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIM 512
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 134052199 513 QDLFQLMKDKTSLVISHHLVGLECM-DEILVLVEGKVVEKGT 553
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-504 |
4.95e-13 |
|
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: 68.29 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 355 VSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGR---EVRDYHQSKL--MAHMAVVAQRThlfnaTVREN 429
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldFQRDSIARGLlyLGHAPGIKTTL-----SVLEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 430 ILLARPGASEKEMIQAARRARIHDFiLTLPEGYdtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
338-558 |
6.40e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 338 NNLHFRYSAKdpWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGR--EVRDyhqsklMAHMAvV 415
Cdd:PRK11701 10 RGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRD------LYALS-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 416 AQRTHLFN---ATVRENILLA-RPGAS------EKEMIQAAR-------------------RARIHDfiltLPEGYdtyv 466
Cdd:PRK11701 81 AERRRLLRtewGFVHQHPRDGlRMQVSaggnigERLMAVGARhygdiratagdwlerveidAARIDD----LPTTF---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 467 gegglklSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHLVGLECM--DEILVL 543
Cdd:PRK11701 153 -------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLlaHRLLVM 225
|
250
....*....|....*
gi 134052199 544 VEGKVVEKGTHSQLL 558
Cdd:PRK11701 226 KQGRVVESGLTDQVL 240
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-284 |
6.70e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 69.46 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGsnIGLLttSAYL--------ISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLS 89
Cdd:cd18563 1 LILGFLLMLLGTA--LGLV--PPYLtkiliddvLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 90 NMRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTL---GVVFFLLacfDLRMAFIFL--A 164
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIigiGVVLFSL---NWKLALLVLipV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 165 FFIGAAVVV------PIFIRAWGRRSgqgilgskaQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAK 238
Cdd:cd18563 154 PLVVWGSYFfwkkirRLFHRQWRRWS---------RLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 134052199 239 INGLAGSLTGLCMNLAMWTILVMAIIKVEQGELP-GVYIAMLALATL 284
Cdd:cd18563 225 LWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTlGTLVAFLSYLGM 271
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
24-271 |
7.11e-13 |
|
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: 69.43 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 24 LGFLAVGSNIGLLttSAYLISR------AAQHPPVLDLMVAIVGVRFfgIARAVFRYLERYFSHDVTFRVLSNMRVWFYK 97
Cdd:cd18576 2 LILLLLSSAIGLV--FPLLAGQlidaalGGGDTASLNQIALLLLGLF--LLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 98 AIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLA---FFIGAAVVVP 174
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLAtvpVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 175 IFIRAWGRRSgQGILgskAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLA 254
Cdd:cd18576 158 RRIRKLSKKV-QDEL---AEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250
....*....|....*..
gi 134052199 255 MWTILVMAIIKVEQGEL 271
Cdd:cd18576 234 IVAVLWYGGRLVLAGEL 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
312-529 |
8.67e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 312 ELAETENYSPSRKDEQFVPKGYE-----IEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFF 386
Cdd:TIGR03719 295 ELLSQEFQKRNETAEIYIPPGPRlgdkvIEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 387 DYQRGSLQLGGrevrdyhqsklMAHMAVVAQ-RTHL-FNATVRENIllarPGASEKEMI---QAARRARIHDFILTlpeG 461
Cdd:TIGR03719 373 QPDSGTIEIGE-----------TVKLAYVDQsRDALdPNKTVWEEI----SGGLDIIKLgkrEIPSRAYVGRFNFK---G 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 462 YD--TYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPvvgrEIMQDLFQLMKD--KTSLVISH 529
Cdd:TIGR03719 435 SDqqKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNfaGCAVVISH 498
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
335-562 |
8.92e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHfrYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ--RGSLQLGGREVRDYHQSklmahm 412
Cdd:CHL00131 8 LEIKNLH--ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPE------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 avvaQRTHLfnatvreNILLAR------PGASEKEMIQAARRARiHDFiLTLPE-----------------GYDT----- 464
Cdd:CHL00131 80 ----ERAHL-------GIFLAFqypieiPGVSNADFLRLAYNSK-RKF-QGLPEldplefleiineklklvGMDPsflsr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 465 YVGEGglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLV-ISHHLVGLECM--DEIL 541
Cdd:CHL00131 147 NVNEG---FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHYQRLLDYIkpDYVH 223
|
250 260
....*....|....*....|...
gi 134052199 542 VLVEGKVVEKGTHS--QLLEQGG 562
Cdd:CHL00131 224 VMQNGKIIKTGDAElaKELEKKG 246
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-287 |
1.01e-12 |
|
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: 69.00 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIG--LLTTSayLISRAAQHPPVLDLMVAIVGVRFFG-IARAVFRYLERYFSHDVTFRV------- 87
Cdd:cd18551 1 LILALLLSLLGTAASLAqpLLVKN--LIDALSAGGSSGGLLALLVALFLLQaVLSALSSYLLGRTGERVVLDLrrrlwrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 88 LSNMRVWFYKaieplatsqlmHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFI-FLAFF 166
Cdd:cd18551 79 LLRLPVSFFD-----------RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVtLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 167 IGAAVVVPIFIRAwgRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSL 246
Cdd:cd18551 148 LAFLIILPLGRRI--RKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 134052199 247 TGLCMNLAMWTILVMAIIKVEQGELPgvyiamlaLATLSAF 287
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALT--------VGTLVAF 258
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
351-550 |
1.23e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGR---EVRDYHQSKLMA-HMAVVAQRTHL---FN 423
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEEARAKLRAkHVGFVFQSFMLiptLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 AtvRENILLAR--PGASEKEMIQAARRarihdfiLTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTA 501
Cdd:PRK10584 105 A--LENVELPAllRGESSRQSRNGAKA-------LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 502 GLDPVVGREIMQDLFQLMKD-KTSLVISHHLVGL--ECmDEILVLVEGKVVE 550
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLaaRC-DRRLRLVNGQLQE 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
333-529 |
1.74e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 333 YEIEfnNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGR-EVR--DYHQSKLM 409
Cdd:PRK11147 320 FEME--NVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAyfDQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 AhmavvaqrthlfNATVRENIllarpgASEKEMIQAARRAR-----IHDFiLTLPEGYDTYVGegglKLSGGQRQRVAIA 484
Cdd:PRK11147 396 P------------EKTVMDNL------AEGKQEVMVNGRPRhvlgyLQDF-LFHPKRAMTPVK----ALSGGERNRLLLA 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 134052199 485 RAILKNASVLILDEVTAGLDpVVGREIMQDL---FQlmkdKTSLVISH 529
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLD-VETLELLEELldsYQ----GTVLLVSH 495
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
352-549 |
1.85e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKL----MAH-------MAVVAqrth 420
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlgVAYipedrlgRGLVP---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 lfNATVRENILL---ARPGASEKEMIqaaRRARIHDFILTLPEGYD-------TYVGegglKLSGGQRQRVAIARAILKN 490
Cdd:COG3845 350 --DMSVAENLILgryRRPPFSRGGFL---DRKAIRAFAEELIEEFDvrtpgpdTPAR----SLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 491 ASVLILDEVTAGLDpvVG------REIMQdlfqlMKD--KTSLVISHHLvglecmDEIL-------VLVEGKVV 549
Cdd:COG3845 421 PKLLIAAQPTRGLD--VGaiefihQRLLE-----LRDagAAVLLISEDL------DEILalsdriaVMYEGRIV 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-530 |
2.27e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 339 NLHFRYsaKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMAHMAVVAQR 418
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 419 THLF-NATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYdtyvgegglkLSGGQRQRVAIARAILKNASVLILD 497
Cdd:PRK13540 83 SGINpYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|...
gi 134052199 498 EVTAGLDPVVGREIMQDLFQLMKDKTSLVISHH 530
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
352-540 |
3.21e-12 |
|
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: 66.30 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSL------------QLGGREVRDYHQSKL----------- 408
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaQASPREILALRRRTIgyvsqflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 409 -MAHMAVVAQRthlfnatvreniLLARpGASEKEMIQAARR--ARihdfiLTLPEgydtyvgegglKL--------SGGQ 477
Cdd:COG4778 107 rVSALDVVAEP------------LLER-GVDREEARARAREllAR-----LNLPE-----------RLwdlppatfSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 478 RQRVAIARAILKNASVLILDEVTAGLDPvVGREIMQDLFQLMKDK-TSLV-ISHHlvgLECMDEI 540
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDA-ANRAVVVELIEEAKARgTAIIgIFHD---EEVREAV 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
335-557 |
3.36e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNL--HFRYSAKDPWI---------LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDY 403
Cdd:PRK15079 9 LEVADLkvHFDIKDGKQWFwqppktlkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 404 HQSKLMA---HMAVVAQRThLFNATVRENI--LLARP-GASEKEMIQAARRARIHDFILT---LPEGYDTYVGEgglkLS 474
Cdd:PRK15079 89 KDDEWRAvrsDIQMIFQDP-LASLNPRMTIgeIIAEPlRTYHPKLSRQEVKDRVKAMMLKvglLPNLINRYPHE----FS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 475 GGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLV-ISHHL-VGLECMDEILVLVEGKVVEK 551
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIfIAHDLaVVKHISDRVLVMYLGHAVEL 243
|
....*.
gi 134052199 552 GTHSQL 557
Cdd:PRK15079 244 GTYDEV 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
342-558 |
3.69e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 342 FRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD-----YQRGSLQLGGREVRDYHQSKLMA----HM 412
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQTLRGvrgnKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 AVVAQRT-------HLFNATVRENILL---ARPGASEKEMI---------QAARRarIHDFiltlPEgydtyvgegglKL 473
Cdd:PRK15134 95 AMIFQEPmvslnplHTLEKQLYEVLSLhrgMRREAARGEILncldrvgirQAAKR--LTDY----PH-----------QL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 474 SGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMK--DKTSLVISHHL-VGLECMDEILVLVEGKVVE 550
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLsIVRKLADRVAVMQNGRCVE 237
|
....*...
gi 134052199 551 KGTHSQLL 558
Cdd:PRK15134 238 QNRAATLF 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
335-557 |
4.03e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA---H 411
Cdd:PRK11831 8 VDMRGVSFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 412 MAVVAQRTHLF-NATVRENIllARPGASEKEMIQAArrarIHDFILTLPEGydtyVGEGGL------KLSGGQRQRVAIA 484
Cdd:PRK11831 86 MSMLFQSGALFtDMNVFDNV--AYPLREHTQLPAPL----LHSTVMMKLEA----VGLRGAaklmpsELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 485 RAILKNASVLILDEVTAGLDPVVgreiMQDLFQLMKD------KTSLVISHHLVG-LECMDEILVLVEGKVVEKGTHSQL 557
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPIT----MGVLVKLISElnsalgVTCVVVSHDVPEvLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
351-530 |
4.22e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLanlllgffdyqrgslqlgGREVRDYHQSKLMAHMAVVAQRTHLFNATVRENI 430
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTL------------------LRLLAGALKGTPVAGCVDVPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLARPGASEKEMIQAARRARIHDFILTLPEgydtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGRE 510
Cdd:COG2401 107 GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|...
gi 134052199 511 I---MQDLFQLMKdKTSLVISHH 530
Cdd:COG2401 175 VarnLQKLARRAG-ITLVVATHH 196
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
21-280 |
4.62e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 67.11 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 21 AVLLGFLAVGSNIGLLTTSAYLISRA------AQHPPVLDLMVAIVGVrfFGIARAVFRYLERYFSHDVTFRVLSNMRVW 94
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAideyipNGDLSGLLIIALLFLA--LNLVNWVASRLRIYLMAKVGQRILYDLRQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 95 FYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFylrvLSPPLVALLT-----LGVVFFLLAcFDLRMAFIFLAfFIGA 169
Cdd:cd18545 79 LFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDL----LSNGLINLIPdlltlVGIVIIMFS-LNVRLALVTLA-VLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 170 AVVVPIFIRAWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGL 249
Cdd:cd18545 153 LVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVEL 232
|
250 260 270
....*....|....*....|....*....|..
gi 134052199 250 CMNLAMWTILVMAIIKVEQGEL-PGVYIAMLA 280
Cdd:cd18545 233 ISALGTALVYWYGGKLVLGGAItVGVLVAFIG 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-553 |
4.67e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV-------RDyhqsk 407
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadRD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 408 lmahMAVVAQRTHLF-NATVRENI---LLAR--PGASEKEMIQAARRarihdfILTLpegydtyvgeGGL------KLSG 475
Cdd:PRK11650 78 ----IAMVFQNYALYpHMSVRENMaygLKIRgmPKAEIEERVAEAAR------ILEL----------EPLldrkprELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 476 GQRQRVAIARAILKNASVLILDEVTAGLDP---VVGR-EImQDLFQLMKdKTSLVISHHLVglECM---DEILVLVEGKV 548
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrVQMRlEI-QRLHRRLK-TTSLYVTHDQV--EAMtlaDRVVVMNGGVA 213
|
....*
gi 134052199 549 VEKGT 553
Cdd:PRK11650 214 EQIGT 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
351-505 |
6.51e-12 |
|
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: 64.69 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGR---EVRD-YHQSKL-MAHMAVVAQRThlfnaT 425
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaEQRDePHENILyLGHLPGLKPEL-----S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 426 VRENI-LLARPGASEKEMIQAARRARIHDFILTLPEGYdtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:TIGR01189 90 ALENLhFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
.
gi 134052199 505 P 505
Cdd:TIGR01189 160 K 160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
335-530 |
6.89e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG-----------FFDYQRGSlqlgGREVRDY 403
Cdd:PRK10938 261 IVLNNGVVSYN--DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 404 HQsklmaHMAVVAQRTHL---FNATVRENILlarPGASEKEMI-QAA--RRARIHDFILTLPeGYDTYVGEGGLK-LSGG 476
Cdd:PRK10938 335 KK-----HIGYVSSSLHLdyrVSTSVRNVIL---SGFFDSIGIyQAVsdRQQKLAQQWLDIL-GIDKRTADAPFHsLSWG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 477 QRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLV-ISHH 530
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfVSHH 461
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
348-552 |
9.52e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 348 DPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFdyQRGSLQLGGREVRD---YHQSKLMA-HMAVVAQR----- 418
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL--PAGVRQTAGRVLLDgkpVAPCALRGrKIATIMQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 419 --THLFNATVRENiLLARPGASEKEMIQAARRARIHDFILTLPEGYdtyvgegGLKLSGGQRQRVAIARAILKNASVLIL 496
Cdd:PRK10418 93 npLHTMHTHARET-CLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 497 DEVTAGLDPVVGREIMQDLFQLMKDKTS--LVISHHL-VGLECMDEILVLVEGKVVEKG 552
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMgVVARLADDVAVMSHGRIVEQG 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
330-548 |
1.07e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.58 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 330 PKGYEIEFNNLHFRYSAkDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLqlggrevrdYHQSKLm 409
Cdd:PLN03073 504 PGPPIISFSDASFGYPG-GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKV- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 410 aHMAVVAQRtHLFNATVRENILL----ARPGASEKEMiqaarRARIHDFILTlpegydtyvGEGGLK----LSGGQRQRV 481
Cdd:PLN03073 573 -RMAVFSQH-HVDGLDLSSNPLLymmrCFPGVPEQKL-----RAHLGSFGVT---------GNLALQpmytLSGGQKSRV 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPVVGREIMQDL--FQlmkdKTSLVISH--HLVGlECMDEILVLVEGKV 548
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLvlFQ----GGVLMVSHdeHLIS-GSVDELWVVSEGKV 702
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
352-534 |
1.22e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSK---LMAHMAVVAQRTHLF-NATVR 427
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 EN--ILLARPGASEKEMIQAARRARIHDFILTLPEGYDtyvgeggLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDP 505
Cdd:PRK10908 98 DNvaIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFP-------IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*....
gi 134052199 506 VVGREIMQDLFQLMKDKTSLVISHHLVGL 534
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGL 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
362-561 |
2.37e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 362 GRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV-----RDYHQsklmAHMAVVAQRTHLF-NATVRENILLARP 435
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQE----AGIGIIHQELNLIpQLTIAENIFLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 436 GASE------KEMIQAARR--ARihdfiLTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTaglDPVV 507
Cdd:PRK10762 106 FVNRfgridwKKMYAEADKllAR-----LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT---DALT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 508 GREiMQDLFQLMKDKTS-----LVISHHLVGL-ECMDEILVLVEGKVVEKGTHSQLLEQG 561
Cdd:PRK10762 174 DTE-TESLFRVIRELKSqgrgiVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-556 |
2.84e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 325 DEQFVPKGYEIEFNNLHfrySAKDPWIlRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYH 404
Cdd:PRK10982 241 DKENKPGEVILEVRNLT---SLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 405 QSKLMAH-MAVVAQR---THLF-NATVRENILLA-------RPGASEKEMIQAARRARIHDFILTLPeGYDTYVGEgglk 472
Cdd:PRK10982 317 ANEAINHgFALVTEErrsTGIYaYLDIGFNSLISnirnyknKVGLLDNSRMKSDTQWVIDSMRVKTP-GHRTQIGS---- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 473 LSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISH---HLVGLecMDEILVLVEGKV 548
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSempELLGI--TDRILVMSNGLV 469
|
250
....*....|.
gi 134052199 549 ---VEKGTHSQ 556
Cdd:PRK10982 470 agiVDTKTTTQ 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
352-547 |
3.11e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYqrGSLQ---------LGGREVRDYHQsklmAHMAVVAQRTHLF 422
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH--GTYEgeiifegeeLQASNIRDTER----AGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 423 -NATVRENILLARPGASEKEMIQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEV 499
Cdd:PRK13549 95 kELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqLKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 500 TAGL---DPVVGREIMQDLFQlmKDKTSLVISHHLVGLECM-DEILVLVEGK 547
Cdd:PRK13549 171 TASLtesETAVLLDIIRDLKA--HGIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
352-505 |
3.40e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQ-LGG--REVRdyHQSKLMAHMAVVAQ---RTHLFNAT 425
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGdmADAR--HRRAVCPRIAYMPQglgKNLYPTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 426 VRENI-LLARP-GASEKEmiqaaRRARIHDfiLTLPEGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:NF033858 95 VFENLdFFGRLfGQDAAE-----RRRRIDE--LLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
..
gi 134052199 504 DP 505
Cdd:NF033858 168 DP 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-553 |
3.65e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ--------RGSLQLGGREVRDYHQSKLMAHMAVVAQRTH-L 421
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 422 FNATVRENILLARPGASEKEMIQAARRARIHDFILTLPeGYDTYVGEGGLKLSGGQRQRVAIARAILK---------NAS 492
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 493 VLILDEVTAGLDPVVGREIMQDLFQLMKD--KTSLVISHHL-VGLECMDEILVLVEGKVVEKGT 553
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPnLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-558 |
4.39e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrdyhqSKLMAH------MAVVAQRTHLFNA 424
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-----SLLPLHararrgIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 425 -TVRENILLARpgASEKEMIQAARRARIHDFiltLPEGYDTYVGEG-GLKLSGGQRQRVAIARAILKNASVLILDEVTAG 502
Cdd:PRK10895 93 lSVYDNLMAVL--QIRDDLSAEQREDRANEL---MEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 503 LDPVVGREIMQDLFQLMKDKTSLVISHHLV--GLECMDEILVLVEGKVVEKGTHSQLL 558
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVreTLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
354-548 |
1.01e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD--YQrGSLQLGGREVRDYHQSKLMAH-MAVVAQ--RTH--LFNATV 426
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWE-GEIFIDGKPVKIRNPQQAIAQgIAMVPEdrKRDgiVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENILLA-----------RPGASEKEMIQAARRARIHDFILTLPEGydtyvgegglKLSGGQRQRVAIARAILKNASVLI 495
Cdd:PRK13549 359 GKNITLAaldrftggsriDDAAELKTILESIQRLKVKTASPELAIA----------RLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 496 LDEVTAGLDpvVGR--EIMQDLFQLMKDKTSL-VISHHL---VGLEcmDEILVLVEGKV 548
Cdd:PRK13549 429 LDEPTRGID--VGAkyEIYKLINQLVQQGVAIiVISSELpevLGLS--DRVLVMHEGKL 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
351-552 |
1.05e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD-YQRGslqLGGREVRDYH-QSKLMAH----MAVVAQR-THLFN 423
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgFHIG---VEGVITYDGItPEEIKKHyrgdVVYNAETdVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATVRENILLA--------RP-GASEKEmiqaaRRARIHDFILT---LPEGYDTYVGEGGLK-LSGGQRQRVAIARAILKN 490
Cdd:TIGR00956 153 LTVGETLDFAarcktpqnRPdGVSREE-----YAKHIADVYMAtygLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 491 ASVLILDEVTAGLDPVVGREIMQDLfqlmkdKTSLVISHH--LVGL--------ECMDEILVLVEGKVVEKG 552
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRAL------KTSANILDTtpLVAIyqcsqdayELFDKVIVLYEGYQIYFG 293
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
354-548 |
1.17e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ-RGSLQLGGREVRDYHQSKLMAH-MAVVAQ--RTH--LFNATVR 427
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgIAMVPEdrKRHgiVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENILLA-----------RPGASEKEMIQAARRARIHDFILTLPEGydtyvgegglKLSGGQRQRVAIARAILKNASVLIL 496
Cdd:TIGR02633 358 KNITLSvlksfcfkmriDAAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 497 DEVTAGLDPVVGREIMQDLFQLMKDKTSL-VISHHL---VGLEcmDEILVLVEGKV 548
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELaevLGLS--DRVLVIGEGKL 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-547 |
1.27e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 359 IPQ-GRRLAIVGPSGAGKSTLANLLLG-----------------FFDYQRGSlqlggrEVRDYHQsKLMAHMAVVAQRTH 420
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdeVLKRFRGT------ELQNYFK-KLYNGEIKVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 -------LFNATVREniLLARpgASEKEMiqaarrarihdfiltlpegYDTYVGEGGLK---------LSGGQRQRVAIA 484
Cdd:PRK13409 168 yvdlipkVFKGKVRE--LLKK--VDERGK-------------------LDEVVERLGLEnildrdiseLSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 485 RAILKNASVLILDEVTAGLDpVVGREIMQDLFQ-LMKDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD-IRQRLNVARLIReLAEGKYVLVVEHDLAVLDYLADNVHIAYGE 287
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
352-550 |
1.73e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDY--QRGSLQLGGREV--RDYHQSKlmaHMAVV------AQRTHL 421
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCrfKDIRDSE---ALGIViihqelALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 422 fnaTVRENILL----ARPGA-SEKEMIQAARR--ARIhdfilTLPEGYDTYVGEGGLklsgGQRQRVAIARAILKNASVL 494
Cdd:NF040905 94 ---SIAENIFLgnerAKRGViDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 495 ILDEVTAGLDpvvgREIMQDLFQLM---KDK--TSLVISHHL--VgLECMDEILVLVEGKVVE 550
Cdd:NF040905 162 ILDEPTAALN----EEDSAALLDLLlelKAQgiTSIIISHKLneI-RRVADSITVLRDGRTIE 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
354-529 |
2.50e-10 |
|
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: 63.23 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYqrgslqLGGREVRDYHQSklmahMAVVAQRTHLFNATVRENIL-- 431
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV------YGGRLTKPAKGK-----LFYVPQRPYMTLGTLRDQIIyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 432 -----LARPGASEKEMIQAARRARIHDfILTLPEGYDTyVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPv 506
Cdd:TIGR00954 539 dssedMKRRGLSDKDLEQILDNVQLTH-ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV- 615
|
170 180
....*....|....*....|....*
gi 134052199 507 vgrEIMQDLFQLMKDK--TSLVISH 529
Cdd:TIGR00954 616 ---DVEGYMYRLCREFgiTLFSVSH 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
344-505 |
2.83e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 344 YSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQRTHLFN 423
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATVRENILLARPGASEKEMIQAARRarihdfILTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:PRK13543 99 TLENLHFLCGLHGRRAKQMPGSALA------IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
..
gi 134052199 504 DP 505
Cdd:PRK13543 169 DL 170
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
18-287 |
3.82e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 61.27 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIglltTSAYLISRAAQHppVLDLMVAIVGVRFFGIAR------------AVFRYLERYFSHDVTF 85
Cdd:cd18547 1 LILVIILAIISTLLSV----LGPYLLGKAIDL--IIEGLGGGGGVDFSGLLRilllllglyllsALFSYLQNRLMARVSQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 86 RVLSNMRVWFYKAIE--PLAtsqlmhY---HS-GDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMA 159
Cdd:cd18547 75 RTVYDLRKDLFEKLQrlPLS------YfdtHShGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 160 FIFLAfFIGAAVVVPIFIrawGRRSG------QGILGskaQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKlQ 233
Cdd:cd18547 149 LIVLV-TVPLSLLVTKFI---AKRSQkyfrkqQKALG---ELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYK-A 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 234 GRLAK-INGLAGSLTGLCMNLAMWTILVMAIIKVEQGelpgvyiaMLALATLSAF 287
Cdd:cd18547 221 SFKAQfYSGLLMPIMNFINNLGYVLVAVVGGLLVING--------ALTVGVIQAF 267
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
335-561 |
5.34e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFrySAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ--RGSLQLGGREVRDYHQSKLMAhm 412
Cdd:PRK09580 2 LSIKDLHV--SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRAG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 413 avvaqrthlfnatvrENILLAR------PGASEKEMIQ----AARRAR---------IHDFI------LTLPEGYDT-YV 466
Cdd:PRK09580 78 ---------------EGIFMAFqypveiPGVSNQFFLQtalnAVRSYRgqepldrfdFQDLMeekialLKMPEDLLTrSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 467 GEGglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVI-SHHLVGLECM--DEILVL 543
Cdd:PRK09580 143 NVG---FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIvTHYQRILDYIkpDYVHVL 219
|
250 260
....*....|....*....|.
gi 134052199 544 VEGKVVEKGTHS---QLLEQG 561
Cdd:PRK09580 220 YQGRIVKSGDFTlvkQLEEQG 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
315-550 |
5.84e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 315 ETENYSPSRKDEQFVPKGYEI-EFNNLhfrySAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSL 393
Cdd:PRK09700 245 ELQNRFNAMKENVSNLAHETVfEVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 394 QLGGREVRDYHQ----SKLMAHMAVVAQRTHLF-NATVRENILLARP-------GA----SEKEMIQAARRARihDFILT 457
Cdd:PRK09700 321 RLNGKDISPRSPldavKKGMAYITESRRDNGFFpNFSIAQNMAISRSlkdggykGAmglfHEVDEQRTAENQR--ELLAL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 458 LPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKD-KTSLVISHHLVG-LE 535
Cdd:PRK09700 399 KCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEiIT 474
|
250
....*....|....*
gi 134052199 536 CMDEILVLVEGKVVE 550
Cdd:PRK09700 475 VCDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
21-231 |
7.09e-10 |
|
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: 60.12 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 21 AVLLGFLAVGSNIGLLTTSAYLISRAA-QHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAI 99
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 100 EPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLsPPLVA-----LLTLGVVFFLlacfDLRMAFIFLAffigAAVVVP 174
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYL-PQLVLaaivpLLILVAVFPL----DWVSALILLV----TAPLIP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 175 IFirawgrrsgQGILGSKAQ------------LNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSK 231
Cdd:cd18584 152 LF---------MILIGKAAQaasrrqwaalsrLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRR 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-547 |
7.74e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 358 TIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSKLMAHmavvaqrthlFNATVREniLLarpga 437
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKAD----------YEGTVRD--LL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 438 SEKEMIQAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDP----VVGREI 511
Cdd:cd03237 83 SSITKDFYTHPYFKTEIAkpLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 134052199 512 MQdlFQLMKDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:cd03237 159 RR--FAENNEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-547 |
8.72e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.34 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 359 IPQ-GRRLAIVGPSGAGKSTLANLL-------LGFFD----------YQRGSlqlggrEVRDYHQsKLMAHMAVVAQRTH 420
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILsgelkpnLGDYDeepswdevlkRFRGT------ELQDYFK-KLANGEIKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 421 -------LFNATVREniLLARpgasekemiqAARRARIHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNA 491
Cdd:COG1245 168 yvdlipkVFKGTVRE--LLEK----------VDERGKLDELAekLGLENILDRDISE----LSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 492 SVLILDEVTAGLDpVVGR----EIMQDLFQlmKDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:COG1245 232 DFYFFDEPSSYLD-IYQRlnvaRLIRELAE--EGKYVLVVEHDLAILDYLADYVHILYGE 288
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
23-280 |
1.21e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 59.73 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 23 LLGFLAVGSNIGLLTTSAYLISRA-----AQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYK 97
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAidaltAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 98 AIEPLATSQLMHYHSGDLLSRIVSDVETLKNFylrvLSPPLV----ALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVV 173
Cdd:cd18541 82 HLLTLSPSFYQKNRTGDLMARATNDLNAVRMA----LGPGILylvdALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 174 PIFIRAWGRRSGQgILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNL 253
Cdd:cd18541 158 YRLGKKIHKRFRK-VQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGL 236
|
250 260 270
....*....|....*....|....*....|....
gi 134052199 254 AMWTILVMAIIKVEQGEL-PG------VYIAMLA 280
Cdd:cd18541 237 SFLIVLWYGGRLVIRGTItLGdlvafnSYLGMLI 270
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-529 |
1.30e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 358 TIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLggrEVRdyhqsklmahMAVVAQR-THLFNATVRENILLARPG 436
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLK----------ISYKPQYiSPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 437 ASEKEMIQA--ARRARIHDFiltlpegYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDP----VVGRE 510
Cdd:COG1245 429 DFGSSYYKTeiIKPLGLEKL-------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKA 497
|
170
....*....|....*....
gi 134052199 511 IMQdlFQLMKDKTSLVISH 529
Cdd:COG1245 498 IRR--FAENRGKTAMVVDH 514
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
353-534 |
1.33e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 353 RDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVR----DYHQSKL-MAHMAVVaqRTHLfnaTVR 427
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYHQDLLyLGHQPGI--KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENIL----LARPgASEKEMIQAARRARIHDFiLTLPEGYdtyvgegglkLSGGQRQRVAIARAILKNASVLILDE-VTAg 502
Cdd:PRK13538 93 ENLRfyqrLHGP-GDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEpFTA- 159
|
170 180 190
....*....|....*....|....*....|....
gi 134052199 503 LDpVVGREIMQDLFQLMKDKTSLVI--SHHLVGL 534
Cdd:PRK13538 160 ID-KQGVARLEALLAQHAEQGGMVIltTHQDLPV 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
338-559 |
1.35e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 338 NNLHFRYSAKDpwILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMAHMAVVAQ 417
Cdd:PRK10575 15 RNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 418 RthLFNA---TVRENILLAR-PGASEKEMIQAARRARIHDFIltlpegydTYVGEGGL------KLSGGQRQRVAIARAI 487
Cdd:PRK10575 93 Q--LPAAegmTVRELVAIGRyPWHGALGRFGAADREKVEEAI--------SLVGLKPLahrlvdSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134052199 488 LKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVIS--HHL-VGLECMDEILVLVEGKVVEKGTHSQLLE 559
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDInMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-547 |
1.68e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 358 TIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLggrEVR-----DYHQSKlmahmavvaqrthlFNATVREniLL 432
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELKisykpQYIKPD--------------YDGTVED--LL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 433 AR-PGASEKEMIQaarrariHDFI--LTLPEGYDTYVGEgglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDP---- 505
Cdd:PRK13409 422 RSiTDDLGSSYYK-------SEIIkpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrl 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 134052199 506 VVGREIMQdlFQLMKDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:PRK13409 491 AVAKAIRR--IAEEREATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-559 |
1.69e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQ---RGSLQLGGREVRDYHQSKLMAHMAvvAQRTHLFNATVR 427
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYIS--QNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENI--------------LLARPGASEKE----------------MIQAARRARIHDF---ILTLPEGYDTYVGEGGLK-L 473
Cdd:PLN03140 258 ETLdfsarcqgvgtrydLLSELARREKDagifpeaevdlfmkatAMEGVKSSLITDYtlkILGLDICKDTIVGDEMIRgI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 474 SGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLV----GLECMDEILVLVEGKVV 549
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQIV 417
|
250
....*....|
gi 134052199 550 EKGTHSQLLE 559
Cdd:PLN03140 418 YQGPRDHILE 427
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
312-504 |
2.21e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 312 ELAETENYSPSRKDEQFVPKGYE-----IEFNNLHFRYSakDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFF 386
Cdd:PRK11819 297 ELLSEEYQKRNETNEIFIPPGPRlgdkvIEAENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 387 DYQRGSLQLGGrevrdyhqsklMAHMAVVAQ-RTHLF-NATVRENIllarpgASEKEMIQAARR---ARihdfiltlpeg 461
Cdd:PRK11819 375 QPDSGTIKIGE-----------TVKLAYVDQsRDALDpNKTVWEEI------SGGLDIIKVGNReipSR----------- 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 462 ydTYVGEGGLK----------LSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:PRK11819 427 --AYVGRFNFKggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
352-549 |
2.68e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFF---DYQrGSLQLGGREVRDYHQSKL-MAHMAVVAQRTHLF-NATV 426
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWD-GEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENILLAR----PGA--SEKEMIQAA----RRARIHDFILTLPegydtyVGEGGlklsGGQRQRVAIARAILKNASVLIL 496
Cdd:TIGR02633 96 AENIFLGNeitlPGGrmAYNAMYLRAknllRELQLDADNVTRP------VGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 497 DEVTAGLDPvVGREIMQDLFQLMKDK--TSLVISHHLVGLECM-DEILVLVEGKVV 549
Cdd:TIGR02633 166 DEPSSSLTE-KETEILLDIIRDLKAHgvACVYISHKLNEVKAVcDTICVIRDGQHV 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-549 |
3.07e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG--FFDYQRGSLQLGGREVRDYHQSKLMAH-MAVVAQ-RTHL---FN 423
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDVSTVSDAIDAgLAYVTEdRKGYglnLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATVRENILLAR-PGASEKEMIQAARRARIhdfiltlPEGYDTY-------VGEGGLKLSGGQRQRVAIARAILKNASVLI 495
Cdd:NF040905 355 DDIKRNITLANlGKVSRRGVIDENEEIKV-------AEEYRKKmniktpsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 134052199 496 LDEVTAGLDpvVGR--EIMQDLFQLMKD-KTSLVISHHLVGLECM-DEILVLVEGKVV 549
Cdd:NF040905 428 LDEPTRGID--VGAkyEIYTIINELAAEgKGVIVISSELPELLGMcDRIYVMNEGRIT 483
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
112-310 |
4.00e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 57.84 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 112 SGDLLSRIvSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWgRRSGQGILGS 191
Cdd:cd18570 98 TGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPF-KKKNREVMES 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 192 KAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGEL 271
Cdd:cd18570 176 NAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 134052199 272 -PGvyiAMLALATLSAF--EAVTPLPLTFIYLEESMSAAKRL 310
Cdd:cd18570 256 sLG---QLIAFNALLGYflGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
55-271 |
6.47e-09 |
|
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: 57.41 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 55 LMVAIVGVrFFGIARAvfrylerYFSHDVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVL 134
Cdd:cd18548 46 LLLALLGL-IAGILAG-------YFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 135 SPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWGRRSgqgilgSKAQ-----LNTCLVDGIQGMTDL 209
Cdd:cd18548 118 RMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLF------KKVQkkldrLNRVVRENLTGIRVI 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 210 LSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGEL 271
Cdd:cd18548 192 RAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSL 253
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
18-279 |
7.76e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 57.11 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIGLLTTSAYLISRAAQH--PPVLDLMVAI-VGVrffGIARAVFRYLERYFSHDVTFRVLSNMRVW 94
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAgdLGVLLLAAAAyLAV---VLAGWVAQRAQTRLTGRTGERLLYDLRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 95 FYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVP 174
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 175 IFIRAWG---RRSGQGIlgskAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCM 251
Cdd:cd18546 158 WFRRRSSrayRRARERI----AAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLG 233
|
250 260
....*....|....*....|....*....
gi 134052199 252 NLAMWTILVMAIIKVEQGEL-PGVYIAML 279
Cdd:cd18546 234 NLATAAVLLVGAWRVAAGTLtVGVLVAFL 262
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
471-556 |
1.04e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 471 LKLSGGQRQRVAIARAILKNASVLILDEVTAGLDP----VVGREIMQdlFQLMKDKTSLVISHHLVGLECMDEILVLVEG 546
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRR--LSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
90
....*....|
gi 134052199 547 KVVEKGTHSQ 556
Cdd:cd03222 148 EPGVYGIASQ 157
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
18-180 |
1.06e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 56.72 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 18 MLWAVLLGFLAVGSNIG--LLTtsAYLISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWF 95
Cdd:cd18543 1 LILALLAALLATLAGLAipLLT--RRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 96 YKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNFyLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLaffigaAVVVPI 175
Cdd:cd18543 79 FAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF-LAFGPFLLGNLLTLVVGLVVMLVLSPPLALVAL------ASLPPL 151
|
....*
gi 134052199 176 FIRAW 180
Cdd:cd18543 152 VLVAR 156
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
318-558 |
1.12e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 318 NYSPSRKDEQFVPKGYE---IEFNNLHF--RYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD---YQ 389
Cdd:TIGR00956 740 DESDDVNDEKDMEKESGediFHWRNLTYevKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvIT 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 390 RGSLQLGGREvRDYHQSKLMAHmaVVAQRTHLFNATVRENI----LLARPGA---SEK-EMIQAARRarihdfILTLPEG 461
Cdd:TIGR00956 820 GGDRLVNGRP-LDSSFQRSIGY--VQQQDLHLPTSTVRESLrfsaYLRQPKSvskSEKmEYVEEVIK------LLEMESY 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 462 YDTYVGEGGLKLSGGQRQRVAIA-RAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHH---LVGLECM 537
Cdd:TIGR00956 891 ADAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsAILFEEF 970
|
250 260
....*....|....*....|....*
gi 134052199 538 DEILVLVEG-KVV---EKGTHSQLL 558
Cdd:TIGR00956 971 DRLLLLQKGgQTVyfgDLGENSHTI 995
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
354-562 |
1.20e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV--RDYHQSKLMAHMAvvaQRTHLFNA-TVRENI 430
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRVGYMS---QAFSLYGElTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LL-AR----PGASEKEMI-QAARRARIHDFILTLPEGydtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:NF033858 361 ELhARlfhlPAAEIAARVaEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134052199 505 PVVgreimQDLF-QLM-----KDKTSLVISHHLV--GLECmDEILVLVEGKVVEKGTHSQLLEQGG 562
Cdd:NF033858 430 PVA-----RDMFwRLLielsrEDGVTIFISTHFMneAERC-DRISLMHAGRVLASDTPAALVAARG 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
351-504 |
1.23e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.64 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGF-FDYQ--------------------------RGSLQLGGREVRDY 403
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNgearpqpgikvgylpqepqldptktvRENVEEGVAEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 404 hQSKLMAHMAVVAQRTHLFNAtvreniLLARPGASEkEMIQAA------RRARIHDFILTLPEGyDTYVGegglKLSGGQ 477
Cdd:TIGR03719 100 -LDRFNEISAKYAEPDADFDK------LAAEQAELQ-EIIDAAdawdldSQLEIAMDALRCPPW-DADVT----KLSGGE 166
|
170 180
....*....|....*....|....*..
gi 134052199 478 RQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
353-548 |
1.69e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 353 RDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYHQSKLMA----HMAVVAQRTHLF-NATVR 427
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvYLPEDRQSSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 428 ENI---LLARPGASEKEMIQAARRARIHDFILTLPEGYDTYVGegglKLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:PRK15439 360 WNVcalTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 134052199 505 pVVGReimQDLFQLMKDKTS-----LVISHHLVGLECM-DEILVLVEGKV 548
Cdd:PRK15439 436 -VSAR---NDIYQLIRSIAAqnvavLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
351-549 |
2.27e-08 |
|
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: 54.17 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFD--YQRGSLQLGGREVRDYHQsKLMAHmaVVAQRTHLFNATVRE 428
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ-RSTGY--VEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLArpgasekemiqAARRArihdfiltlpegydtyvgegglkLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:cd03232 99 ALRFS-----------ALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 134052199 509 REIMQDLFQLMKDKTSLVISHH---LVGLECMDEILVLVE-GKVV 549
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIHqpsASIFEKFDRLLLLKRgGKTV 189
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-533 |
2.72e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 361 QGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSlqlggrevrdyhqsklmahmavvaqrthlfnatvrenILLARPGASEK 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG-------------------------------------VIYIDGEDILE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 441 EMIQAARrarihdfiltlpegyDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMK 520
Cdd:smart00382 44 EVLDQLL---------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170
....*....|...
gi 134052199 521 DKTSLVISHHLVG 533
Cdd:smart00382 109 LLLKSEKNLTVIL 121
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
352-549 |
6.17e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREVrDYHQSK--LMAHMAVVAQRTHLF-NATVRE 428
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKeaLENGISMVHQELNLVlQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 429 NILLAR-----PGASEKEMIQAARraRIHDFIltlpeGYDTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGL 503
Cdd:PRK10982 93 NMWLGRyptkgMFVDQDKMYRDTK--AIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 504 DPvvgREImQDLFQL---MKDKTS--LVISHHLVGL-ECMDEILVLVEGKVV 549
Cdd:PRK10982 166 TE---KEV-NHLFTIirkLKERGCgiVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-280 |
8.49e-08 |
|
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: 54.06 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 17 PMLWAVLLGFLAVGSNIGLLTTSAylisraaqhppvldlmVAIVGVrffGIARAVFRYLERYFSHDVTFRVLSNMRVWFY 96
Cdd:cd18564 34 PLPGLLGLAPLLGPDPLALLLLAA----------------AALVGI---ALLRGLASYAGTYLTALVGQRVVLDLRRDLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 97 KAIEPLAtsqlMHYH----SGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLA---FFIGA 169
Cdd:cd18564 95 AHLQRLS----LSFHdrrrTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAvapLLLLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 170 AVVVPIFIRAWGR--RSGQGILGSKAQlntclvDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLT 247
Cdd:cd18564 171 ARRFSRRIKEASReqRRREGALASVAQ------ESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVV 244
|
250 260 270
....*....|....*....|....*....|....*..
gi 134052199 248 GLCMNLAMWTILVMAIIKVEQGEL-PG---VYIAMLA 280
Cdd:cd18564 245 DVLVAVGTALVLWFGAWLVLAGRLtPGdllVFLAYLK 281
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
355-560 |
1.19e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 355 VSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV-----RDYHQSKLM------AHMAVVAQrthlfn 423
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirspRDAIRAGIMlcpedrKAEGIIPV------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 ATVRENI-LLARPGASEKEM-IQAARRARIHD-FILTL----PEGyDTYVGegglKLSGGQRQRVAIARAILKNASVLIL 496
Cdd:PRK11288 346 HSVADNInISARRHHLRAGClINNRWEAENADrFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 497 DEVTAGLDpvVG--REIMQDLFQLMKDK-TSLVISHHLVglECM---DEILVLVEGKVVEKGTHSQLLEQ 560
Cdd:PRK11288 421 DEPTRGID--VGakHEIYNVIYELAAQGvAVLFVSSDLP--EVLgvaDRIVVMREGRIAGELAREQATER 486
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
55-310 |
1.58e-07 |
|
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: 53.19 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 55 LMVAIVGVRF--FGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSQLMHYHSGDLLSRIVSDVETLKNF--- 129
Cdd:cd18554 43 KLFTIIGIMFfiFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFitt 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 130 -YLRVLSPPLVALLTLGVVFFLlacfDLRMAFIFLAFFIGAAVVVPIFIRAWgRRSGQGILGSKAQLNTCLVDGIQGMTD 208
Cdd:cd18554 123 gLMNIWLDMITIIIAICIMLVL----NPKLTFVSLVIFPFYILAVKYFFGRL-RKLTKERSQALAEVQGFLHERIQGMSV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 209 LLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGElpgvyiamLALATLSAFe 288
Cdd:cd18554 198 IKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGN--------LTVGTLVAF- 268
|
250 260
....*....|....*....|..
gi 134052199 289 avtplpltFIYLEESMSAAKRL 310
Cdd:cd18554 269 --------VGYMERMYSPLRRL 282
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
351-529 |
4.94e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG-------------------------------FFDYQRGSLQLGGRE 399
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdpprnvegtVYDFVAEGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 400 VRDYHQsklMAHMAVVAQRTHLFNATVRENILLARPGASEKEmiqaarrARIHDFILTLPEGYDTYVGEgglkLSGGQRQ 479
Cdd:PRK11147 98 LKRYHD---ISHLVETDPSEKNLNELAKLQEQLDHHNLWQLE-------NRINEVLAQLGLDPDAALSS----LSGGWLR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 134052199 480 RVAIARAILKNASVLILDEVTAGLDPvvgrEIMQDLFQLMKD-KTSLV-ISH 529
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTfQGSIIfISH 211
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
64-310 |
6.32e-07 |
|
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: 51.41 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 64 FFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIeplaTSQLM----HYHSGDLLSRIVSDVETLKNFYLRVLSPPLV 139
Cdd:cd18557 44 AIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL----LRQEIaffdKHKTGELTSRLSSDTSVLQSAVTDNLSQLLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 140 ALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRaWGRRSGQGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQL 219
Cdd:cd18557 120 NILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR-YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 220 EKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGELPGVYIAMLALATLSAFEAVTPLPLTFIY 299
Cdd:cd18557 199 RRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLAD 278
|
250
....*....|.
gi 134052199 300 LEESMSAAKRL 310
Cdd:cd18557 279 IMKALGASERV 289
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
354-529 |
1.06e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 354 DVSFtiPQGRRLAIVGPSGAGKSTLANLLLgffdyqrgsLQLGGRevrdyhqsklmahmavvaqrthlFNATVRENILLA 433
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILDAIG---------LALGGA-----------------------QSATRRRSGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 434 RPgasekemIQAARRArihDFILTLPegydtyvgegglKLSGGQRQRVAIArAILKNASV-----LILDEVTAGLDPVVG 508
Cdd:cd03227 61 GC-------IVAAVSA---ELIFTRL------------QLSGGEKELSALA-LILALASLkprplYILDEIDRGLDPRDG 117
|
170 180
....*....|....*....|..
gi 134052199 509 REIMQDLF-QLMKDKTSLVISH 529
Cdd:cd03227 118 QALAEAILeHLVKGAQVIVITH 139
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
22-225 |
1.33e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. 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). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 50.23 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 22 VLLGFLAVGSNIGLLTTSAYLISRAAQHPPVLDLMVAIVGVRFFGIA-RAVFRYLERYFSHDVTFRVLSNMRVWFYKAIE 100
Cdd:cd18781 2 VLLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIvRFICTRLASRASYRASADVKKTLREKIYDKLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 101 PLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLspP-----LVALLTLgvvFFLLACFDLRMAFIFLAFfigaAVVVPI 175
Cdd:cd18781 82 RLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYL--PqffysMLAPLTL---FVVLAPINWKAALVLLIC----VPLIPI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 134052199 176 FIRAWGRRSGQgIL----GSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKT 225
Cdd:cd18781 153 SIIAVQKIAKK-LLskywGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEE 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
467-562 |
1.85e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 467 GEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLV--GLECMDEILVLV 544
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMeeAEQLAHELTVID 218
|
90
....*....|....*...
gi 134052199 545 EGKVVEKGTHSQLLEQGG 562
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
56-271 |
2.26e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 49.76 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 56 MVAIVGVRFFG--IARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSqlmhYH----SGDLLSRIVSDVETLKNF 129
Cdd:cd18549 40 LILIIGAILLAlyILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFS----FFdnnkTGQLMSRITNDLFDISEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 130 YLRVLSPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWGRRSGQgILGSKAQLNTCLVDGIQGMTDL 209
Cdd:cd18549 116 AHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRR-VREKIGEINAQLEDSLSGIRVV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 210 LSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGEL 271
Cdd:cd18549 195 KAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEI 256
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
351-546 |
2.48e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG--FFDYQRGSLQLGGREVRdyhqSKLMAHMAVVAQRT--HLFNATV 426
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGFPKK----QETFARISGYCEQNdiHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENIL----LARPGASEKEmiqaaRRARIHDFILTLPEG---YDTYVGEGGLK-LSGGQRQRVAIARAILKNASVLILDE 498
Cdd:PLN03140 971 RESLIysafLRLPKEVSKE-----EKMMFVDEVMELVELdnlKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 134052199 499 VTAGLDPVVGREIMQDLFQLMKDKTSLVISHHLVGL---ECMDEILVLVEG 546
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdifEAFDELLLMKRG 1096
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-504 |
2.66e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 351 ILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGF-FDYQrgslqlgGrEVRdyhqskLMAHMAV--VAQRTHL-FNATV 426
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEFE-------G-EAR------PAPGIKVgyLPQEPQLdPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 427 RENI---------LLAR----------PGASEKEMiqAARRARIHDFI------------------LTLPEGyDTYVGeg 469
Cdd:PRK11819 88 RENVeegvaevkaALDRfneiyaayaePDADFDAL--AAEQGELQEIIdaadawdldsqleiamdaLRCPPW-DAKVT-- 162
|
170 180 190
....*....|....*....|....*....|....*
gi 134052199 470 glKLSGGQRQRVAIARAILKNASVLILDEVTAGLD 504
Cdd:PRK11819 163 --KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-547 |
4.83e-06 |
|
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: 48.13 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 362 GRRLAIVGPSGAGKSTLANLL-------LGFFD----------YQRGSlqlggrEVRDYHQSKLMAHMAVV--AQRTHLF 422
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILagklkpnLGKFDdppdwdeildEFRGS------ELQNYFTKLLEGDVKVIvkPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 423 NATVRENILLARPGASEKEMIqaarrarihdfiltlpegyDTYVGEGGLK---------LSGGQRQRVAIARAILKNASV 493
Cdd:cd03236 100 PKAVKGKVGELLKKKDERGKL-------------------DELVDQLELRhvldrnidqLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134052199 494 LILDEVTAGLD-------PVVGREIMQDlfqlmkDKTSLVISHHLVGLECMDEILVLVEGK 547
Cdd:cd03236 161 YFFDEPSSYLDikqrlnaARLIRELAED------DNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
362-530 |
5.05e-06 |
|
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: 49.63 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 362 GRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREV----RDYHQS-----KLMAHMAVVAQRTHLFnatvreniLL 432
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSDVHQNmgycpQFDAIDDLLTGREHLY--------LY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 433 ARPGASEKEMIQAARRARIHDFILTLpegydtYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIM 512
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSL------YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170
....*....|....*...
gi 134052199 513 QDLFQLMKDKTSLVISHH 530
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSH 2128
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
352-529 |
8.70e-06 |
|
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: 47.25 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLAnlllgfFD--YQRGSLQ------------LGGREVRDYHQSKLMAHMAVVAQ 417
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA------FDtiYAEGQRRyveslsayarqfLGQMDKPDVDSIEGLSPAIAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 418 RTHLFN-----ATVRE-----NILLARPGAsekemiqaarRARIhDFILTLPEGYDTYVGEGGlKLSGGQRQRVAIARAI 487
Cdd:cd03270 85 KTTSRNprstvGTVTEiydylRLLFARVGI----------RERL-GFLVDVGLGYLTLSRSAP-TLSGGEAQRIRLATQI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 134052199 488 LKN-ASVL-ILDEVTAGLDPVVGREIMqDLFQLMKDK--TSLVISH 529
Cdd:cd03270 153 GSGlTGVLyVLDEPSIGLHPRDNDRLI-ETLKRLRDLgnTVLVVEH 197
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
335-558 |
1.25e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 335 IEFNNLHFRYSAKDPWI--LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLG--------------FFDYQRgsLQLGGR 398
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrFDDIDL--LRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 399 EVRdyhqsKLMAH-MAVVAQRTHLF---NATVRENILLARPGASEK------------EMIQAARRARIHDfiltlpegY 462
Cdd:PRK15093 82 ERR-----KLVGHnVSMIFQEPQSCldpSERVGRQLMQNIPGWTYKgrwwqrfgwrkrRAIELLHRVGIKD--------H 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 463 DTYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLMKDK--TSLVISHHLVGL-ECMDE 539
Cdd:PRK15093 149 KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADK 228
|
250
....*....|....*....
gi 134052199 540 ILVLVEGKVVEKGTHSQLL 558
Cdd:PRK15093 229 INVLYCGQTVETAPSKELV 247
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
352-541 |
1.96e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLgffdyqrgslqlggrevrdYHQSKLmahmavvaqrthlfnatvRENIL 431
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------YASGKA------------------RLISF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 432 LARPGASEKEMIQAARrarihdFILTLPEGYDTyVGEGGLKLSGGQRQRVAIARAILKNA--SVLILDEVTAGLDPvvgr 509
Cdd:cd03238 54 LPKFSRNKLIFIDQLQ------FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQ---- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 134052199 510 eimQDLFQLMK--------DKTSLVISHHLVGLECMDEIL 541
Cdd:cd03238 123 ---QDINQLLEvikglidlGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
366-530 |
2.62e-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: 45.29 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 366 AIVGPSGAGKSTLAN-LLLGFFdyqrGSLQLGgrevrdyhqSKLMAHMAVVAQRThlfnaTVRENILLARPGASEKEMIq 444
Cdd:cd03240 26 LIVGQNGAGKTTIIEaLKYALT----GELPPN---------SKGGAHDPKLIREG-----EVRAQVKLAFENANGKKYT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 445 AARRARIHDFILTLPEG-YDTYVGEGGLKLSGGQRQ------RVAIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQ 517
Cdd:cd03240 87 ITRSLAILENVIFCHQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIE 166
|
170
....*....|....*.
gi 134052199 518 LMKDKTS---LVISHH 530
Cdd:cd03240 167 ERKSQKNfqlIVITHD 182
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
352-531 |
5.33e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGREvrdyhqsklmahmAVVAQRTHLFNA-TVRENI 430
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------ALIAISSGLNGQlTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 431 LLarpgaseKEMIQAARRARIHDFILTLPEGYD--TYVGEGGLKLSGGQRQRVAIARAILKNASVLILDEVTAGLDPVVG 508
Cdd:PRK13545 107 EL-------KGLMMGLTKEKIKEIIPEIIEFADigKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180
....*....|....*....|....
gi 134052199 509 REIMQDLFQLM-KDKTSLVISHHL 531
Cdd:PRK13545 180 KKCLDKMNEFKeQGKTIFFISHSL 203
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
361-384 |
9.86e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.92 E-value: 9.86e-05
10 20
....*....|....*....|....
gi 134052199 361 QGRRLAIVGPSGAGKSTLANLLLG 384
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLG 217
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
361-384 |
1.51e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.16 E-value: 1.51e-04
10 20
....*....|....*....|....
gi 134052199 361 QGRRLAIVGPSGAGKSTLANLLLG 384
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-310 |
2.25e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 43.23 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 65 FGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKAIeplaTSQLMHYH----SGDLLSRIVSDVETLKNfylrVLSPPLVA 140
Cdd:cd18577 56 LGIGSFVLSYIQTACWTITGERQARRIRKRYLKAL----LRQDIAWFdkngAGELTSRLTSDTNLIQD----GIGEKLGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 141 LLTLGVVFFllACFDL------RMAFIFLAFFIGAAVVVPIFIRAWGRRSGQgILGSKAQLNTCLVDGIQGMTDLLSFDQ 214
Cdd:cd18577 128 LIQSLSTFI--AGFIIafiyswKLTLVLLATLPLIAIVGGIMGKLLSKYTKK-EQEAYAKAGSIAEEALSSIRTVKAFGG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 215 QGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGELPG--VYIAMLALATLS-AFEAVT 291
Cdd:cd18577 205 EEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPgdVLTVFFAVLIGAfSLGQIA 284
|
250
....*....|....*....
gi 134052199 292 PLpltFIYLEESMSAAKRL 310
Cdd:cd18577 285 PN---LQAFAKARAAAAKI 300
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
352-553 |
2.44e-04 |
|
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: 42.99 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRgsLQLGGREVRDYHQSKLMAH---MAVVAQ----RTHLFN- 423
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARR--LHLKKEQPGNHDRIEGLEHidkVIVIDQspigRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 424 AT-------VRE-----------------------NIllarpgASEKEM-IQAARR-----ARIHDFILTLPE---GYDT 464
Cdd:cd03271 89 ATytgvfdeIRElfcevckgkrynretlevrykgkSI------ADVLDMtVEEALEffeniPKIARKLQTLCDvglGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 465 yVGEGGLKLSGGQRQRVAIARAILKNAS---VLILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISHHLVGLECMDEI 540
Cdd:cd03271 163 -LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWI 241
|
250
....*....|....*....
gi 134052199 541 LVL------VEGKVVEKGT 553
Cdd:cd03271 242 IDLgpeggdGGGQVVASGT 260
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
329-531 |
3.50e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 329 VPKGYEIEFNN-------LHFRYSAKDPWILRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQRGSLQLGGrEVr 401
Cdd:PRK13546 10 VTKEYRIYRTNkermkdaLIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EV- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 402 dyhqSKLMAHMAVVAQRTHLFNATVRENILLARPGASEKEMIQAARRARIHDFILTLPEGYdtyvgegglklSGGQRQRV 481
Cdd:PRK13546 88 ----SVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 134052199 482 AIARAILKNASVLILDEVTAGLDPVVGREIMQDLFQLM-KDKTSLVISHHL 531
Cdd:PRK13546 153 GFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNL 203
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
111-301 |
3.86e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.50 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 111 HSGDLLSRIVSdvetlkNFYLR-VLSPPLVAL----LTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWGRRSg 185
Cdd:cd18555 97 SSGDLLFRANS------NVYIRqILSNQVISLiidlLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLN- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 186 QGILGSKAQLNTCLVDGIQGMTDLLSFDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIK 265
Cdd:cd18555 170 QEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 134052199 266 VEQGELP-GVYIAMLALAT------LSAFEAVTPLPLTFIYLE 301
Cdd:cd18555 250 VINGELTlGELIAFSSLAGsfltpiVSLINSYNQFILLKSYLE 292
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
348-523 |
4.09e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 43.01 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 348 DPWILRDVSFTipqgrrlAIVGPSGAGKSTLANLLLG----------FFDYQRGS----LQLGGRevrdyhqsklmaHMA 413
Cdd:COG3451 197 DFHDGLDNGNT-------LILGPSGSGKSFLLKLLLLqllrygarivIFDPGGSYeilvRALGGT------------YID 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 414 VVAQRTHLFNatvreniLLARPGASEKemiqaarRARIHDFILTLpegydtyVGEGGLKLSggQRQRVAIARAILKNASV 493
Cdd:COG3451 258 LSPGSPTGLN-------PFDLEDTEEK-------RDFLLELLELL-------LGREGEPLT--PEERAAIDRAVRALYRR 314
|
170 180 190
....*....|....*....|....*....|
gi 134052199 494 LildevtagldPVVGREIMQDLFQLMKDKT 523
Cdd:COG3451 315 A----------DPEERTTLSDLYELLKEQP 334
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
453-530 |
5.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 453 DFILT-----LPEGYDTyvgegglkLSGGQRQ------RVAIARAILKNASVLILDEVTAGLDPvVGREIMQDLFQL-MK 520
Cdd:PRK01156 785 DFNITvsrggMVEGIDS--------LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDE-DRRTNLKDIIEYsLK 855
|
90
....*....|....
gi 134052199 521 DKTS----LVISHH 530
Cdd:PRK01156 856 DSSDipqvIMISHH 869
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
332-384 |
6.95e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.60 E-value: 6.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 134052199 332 GYEIEFnnlhfrYSAKDPWILRDVSFTIpQGRRLAIVGPSGAGKSTLANLLLG 384
Cdd:pfam03193 83 GYPVLF------VSAKTGEGIEALKELL-KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-281 |
8.90e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 41.70 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 21 AVLLGFLAVGSNIGLLTTSAY--LISRAAQHPPVLDLMVAIVGVRFFGIARAVFRYLERYFSHDVTFRVLSNMRVWFYKA 98
Cdd:cd18550 2 ALVLLLILLSALLGLLPPLLLreIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 99 IEPLATSQLMHYHSGDLLSRIVSDVETLKNFYLRVLSPPLVALLTLGVVFFLLACFDLRMAFIflaffigAAVVVPIFIR 178
Cdd:cd18550 82 LQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALL-------SLVLLPLFVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 179 AWgRRSGQ-------GILGSKAQLNTCLVD--GIQGMtdLLS--FDQQGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLT 247
Cdd:cd18550 155 PT-RRVGRrrrkltrEQQEKLAELNSIMQEtlSVSGA--LLVklFGREDDEAARFARRSRELRDLGVRQALAGRWFFAAL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 134052199 248 GLCMNLAMWTILVMAIIKVEQGEL-PGVYIAMLAL 281
Cdd:cd18550 232 GLFTAIGPALVYWVGGLLVIGGGLtIGTLVAFTAL 266
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
297-394 |
9.06e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 297 FIYLEESmsaaKRLFELA-ETENYSpsrkdeqfvpKGYEIEFnnlhfrysakdpwILRDVSFTIPQGRRLAIVGPSGAGK 375
Cdd:PRK15064 306 FIRFEQD----KKLHRNAlEVENLT----------KGFDNGP-------------LFKNLNLLLEAGERLAIIGENGVGK 358
|
90
....*....|....*....
gi 134052199 376 STLANLLLGFFDYQRGSLQ 394
Cdd:PRK15064 359 TTLLRTLVGELEPDSGTVK 377
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
352-557 |
1.00e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 352 LRDVSFTIPQGRRLAIVGPSGAGKSTLANLLLGFFDYQR---GSLQLG-GREVRDY-HQSKLMahmaVVAQ----RT--- 419
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRlngAKTVPGrYTSIEGLeHLDKVI----HIDQspigRTprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 420 -------------HLFNATVRENILLARP---------GASEK---------EM------------IQAARRAR------ 450
Cdd:TIGR00630 700 npatytgvfdeirELFAETPEAKVRGYTPgrfsfnvkgGRCEAcqgdgvikiEMhflpdvyvpcevCKGKRYNRetlevk 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 451 -----IHDFI-LTLPEGYDTY---------------VGEGGLK-------LSGGQRQRVAIARAILKNA---SVLILDEV 499
Cdd:TIGR00630 780 ykgknIADVLdMTVEEAYEFFeavpsisrklqtlcdVGLGYIRlgqpattLSGGEAQRIKLAKELSKRStgrTLYILDEP 859
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134052199 500 TAGLDpvvgreiMQDLFQLM--------KDKTSLVISHHLVGLECMDEILVLVE------GKVVEKGTHSQL 557
Cdd:TIGR00630 860 TTGLH-------FDDIKKLLevlqrlvdKGNTVVVIEHNLDVIKTADYIIDLGPeggdggGTVVASGTPEEV 924
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
358-404 |
1.15e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.42 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 134052199 358 TIPQGRRLAIV--GPSGAGKSTLANLLLGFFDYQRGSLQLGGREVRDYH 404
Cdd:pfam06414 5 TTSQERPKAILlgGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELH 53
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
473-529 |
1.68e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134052199 473 LSGGQRQRVAIAR--AILK-NASVL-ILDEVTAGLDPV-VGREImqDLFQLMKDKTS-LVISH 529
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFKvKPAPFcILDEVDAPLDDAnVERFA--NLLKEFSKNTQfIVITH 1150
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
55-280 |
4.93e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 39.04 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 55 LMVAIVGVRFFGiarAVFRYLERYFSHDVTFRVLSNMRVWFYKAIEPLATSQlMHYHSGDLLSRIVSDVETLKNFYLRVL 134
Cdd:cd18783 44 LTIGVVIALLFE---GILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDF-FERTPAGVLTKHMQQIERIRQFLTGQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134052199 135 SPPLVALLTLGVVFFLLACFDLRMAFIFLAFFIGAAVVVPIFIRAWGRRSGQgILGSKAQLNTCLVDGIQGMTDLLSFDQ 214
Cdd:cd18783 120 FGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQA-LYRAEGERQAFLVETVHGIRTVKSLAL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134052199 215 QGRQLEKIDKTNDNLSKLQGRLAKINGLAGSLTGLCMNLAMWTILVMAIIKVEQGELP-GVYIA--MLA 280
Cdd:cd18783 199 EPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTvGALIAfnMLA 267
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
473-530 |
5.54e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.21 E-value: 5.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134052199 473 LSGGQRQRVAIAR--AIL--KNASVLILDEVTAGLDPV-VGReiMQDLFQLMKDKTS-LVISHH 530
Cdd:cd03278 114 LSGGEKALTALALlfAIFrvRPSPFCVLDEVDAALDDAnVER--FARLLKEFSKETQfIVITHR 175
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
361-384 |
7.73e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 37.47 E-value: 7.73e-03
10 20
....*....|....*....|....
gi 134052199 361 QGRRLAIVGPSGAGKSTLANLLLG 384
Cdd:cd04164 2 EGIKVVIAGKPNVGKSSLLNALAG 25
|
|
| |
