|
Name |
Accession |
Description |
Interval |
E-value |
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
58-705 |
2.31e-180 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 530.98 E-value: 2.31e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 58 PAERVSRILLAAGLKnIKVAQLRWERFDHRHLPALLLHNGcwqlaehGDAGVLLLTAADG--------------TVSRVA 123
Cdd:TIGR03375 33 TPELLPRAARRAGLS-ARLVKRSLDDISPLLLPAILLLKD-------GRACVLLGIDEDGkarvllpetgdgeqELSLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 124 NGELVDAVVLWLR-VERPETPAGELLKSSASQMLLRELLRDKRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYA 202
Cdd:TIGR03375 105 LEALYSGYAIFVRpQFRFDARADELISPRPKHWFWSTLKESWPLYRDVLIASLLINLLALASPLFVMNVYDRVVPNQAFE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 203 TLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHLLDLRLDKRPRSLGSLAAQMNGLETVRTFFSSTIV 282
Cdd:TIGR03375 185 TLWVLAIGVALAIVFDFVLKTLRSYFLDVAGKKADLILSAKLFERVLGLRMEARPASVGSFANQLREFESVRDFFTSATL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 283 FAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGW 362
Cdd:TIGR03375 265 TALIDLPFALLFLLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQRNAVLVESLSGLETIKALNAEG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 363 FFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGI 442
Cdd:TIGR03375 345 RFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELTMGGLIACVMLSGRALAPLGQLAGL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 443 LVQWQHVREALEMVNRLLALEGNRPEGKVLLVPETLPDRLELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGK 522
Cdd:TIGR03375 425 LTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGK 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 523 STLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIML-AGGINDARFLEVAELLGLDRVA 601
Cdd:TIGR03375 505 STLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALgAPYADDEEILRAAELAGVTEFV 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 602 ADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLL 681
Cdd:TIGR03375 585 RRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLV-THRTSLL 663
|
650 660
....*....|....*....|....
gi 2542252196 682 SLANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR03375 664 DLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
36-705 |
1.35e-168 |
|
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: 501.29 E-value: 1.35e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 36 AVPPGELEQACAaTQQEGVeqkPAERVSRILLAAGLKnIKVAQLRWERFDHRHLPALLLHNG--CWQLAEHGDAGVLLLT 113
Cdd:COG2274 30 PVSLEELREALG-VSRDGL---SLLGLLRAARRLGLR-ARGVRLDLEELAELPLPAILHWDGnhFVVLEGVDGDKVTIAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 114 AADG--TVSRVANGELVDAVVLWLRVERPETPAGEllKSSASQMLLRELLRDKRWLLEVGVATVVVNLLAVATSLFSMQV 191
Cdd:COG2274 105 PATGrrKLSLEEFAESWTGVALLLEPTPEFDKRGE--KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 192 YDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHLLDLRLDKRP-RSLGSLAAQMNGL 270
Cdd:COG2274 183 IDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFEsRSVGDLASRFRDV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 271 ETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWLAQRQLRTLARLEIQRGHERHGLLVDTIQ 350
Cdd:COG2274 263 ESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 351 GAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGG 430
Cdd:COG2274 343 GIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 431 KVIGPIAQSVGILVQWQHVREALEMVNRLLALEGNRPEGKVLLVPETLPDRLELEGVRFAYPGTPVIRLQVETLAFGPGD 510
Cdd:COG2274 423 RFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGE 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 511 RVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAG-GINDARFL 589
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEII 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 590 EVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTd 669
Cdd:COG2274 583 EAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR- 661
|
650 660 670
....*....|....*....|....*....|....*.
gi 2542252196 670 IVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG2274 662 TVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
157-705 |
1.00e-100 |
|
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: 320.54 E-value: 1.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 157 LRELLRD-KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKR 235
Cdd:COG4618 11 LRAALRAcRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 236 VDIALSQQLYEHLLDLRLdkrpRSLGSLAAQ-MNGLETVRTFFSSTIVFAMTDLPFGLMFIV----------FIAAIGGM 304
Cdd:COG4618 91 LDRRLGPRVFDAAFRAAL----RGGGGAAAQaLRDLDTLRQFLTGPGLFALFDLPWAPIFLAvlflfhpllgLLALVGAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 305 ISTVylallpvsllLGWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKL 384
Cdd:COG4618 167 VLVA----------LALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 385 ISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMVNRLLALEG 464
Cdd:COG4618 237 RAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 465 NRPEGKVLLVPETlpdRLELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGG 544
Cdd:COG4618 317 AEPERMPLPRPKG---RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 545 ADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQR 624
Cdd:COG4618 394 ADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 625 QLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
.
gi 2542252196 705 I 705
Cdd:COG4618 554 L 554
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
164-456 |
2.23e-97 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 302.43 E-value: 2.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRLDKRPRSLGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWLA 323
Cdd:cd18587 81 LFERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 324 QRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYVA 403
Cdd:cd18587 161 QKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 404 AVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMV 456
Cdd:cd18587 241 IVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
480-699 |
3.78e-95 |
|
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: 294.11 E-value: 3.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 480 DRLELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERI 559
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKGTLKNNIMLAGG-INDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPR 638
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPlADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQSHTRPtDIVLIATHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
156-705 |
1.95e-88 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 288.60 E-value: 1.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 156 LLRELLRDKRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKR 235
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 236 VDIALSQQLYEHLLDLRL---DKRPRslGSLAAQM-NGLETVRTFFSST---------------IVFAMTDLPFGLMFIV 296
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLsffDRRRT--GDLLSRLtNDVDAVEQFLAHGlpqlvrsvvtligalVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 297 FIAAIGGMIstvylallpvslllgWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMA 376
Cdd:COG1132 170 VLPLLLLVL---------------RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 377 AYSLKSKLISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMV 456
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 457 NRLLALEGNRPEGKVLLVPETLPDRLELEGVRFAYPG-TPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGL 532
Cdd:COG1132 315 FELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGdRPVLKdisLTIP-----PGETVALVGPSGSGKSTLVNLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 533 YKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLA-GGINDARFLEVAELLGLDRVAADSPRSMDTE 611
Cdd:COG1132 390 YDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 612 ISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMR 691
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIA-HRLSTIRNADRILVLD 548
|
570
....*....|....
gi 2542252196 692 RGQVIADGPPAEVI 705
Cdd:COG1132 549 DGRIVEQGTHEELL 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
160-705 |
6.56e-88 |
|
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: 286.17 E-value: 6.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 160 LLRDKRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIA 239
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 240 LSQQLYEHLLDLRLdKRPRSLGSLAaqMNGLETVRTFFSSTIVFAMTDLPFGLMFIVF---------IAAIGGMISTVyl 310
Cdd:TIGR01842 81 LNQPIFAASFSATL-RRGSGDGLQA--LRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVcfllhpwigILALGGAVVLV-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 311 allPVSLLLGWLAQRQLRTLARLEIQRGHerhgLLVDTIQGAETIQSSGSGWFFADLWRSIT-ASMAAYSLKSKLISSLT 389
Cdd:TIGR01842 156 ---GLALLNNRATKKPLKEATEASIRANN----LADSALRNAEVIEAMGMMGNLTKRWGRFHsKYLSAQSAASDRAGMLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 390 TTTTATLSTVGYVAAVVVGVLLIEaGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMVNRLLALEGNRPEG 469
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLGLGAYLAID-GEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 470 KVLLVPEtlpDRLELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWE 549
Cdd:TIGR01842 308 MPLPEPE---GHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 550 LDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGGINDAR-FLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTA 628
Cdd:TIGR01842 385 WDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEkIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
156-703 |
1.31e-68 |
|
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: 235.42 E-value: 1.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 156 LLRELLRDKRWLLEVGVATVVVNLLAVATS-LFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAK 234
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAwLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 235 RVDIALSQQLYEHLLDL--RLDKRPRSlGSLAAQM-NGLETVRTFFSS---------------TIVFAMTDLPFGLMFIV 296
Cdd:COG4988 88 RVKRRLRRRLLEKLLALgpAWLRGKST-GELATLLtEGVEALDGYFARylpqlflaalvplliLVAVFPLDWLSGLILLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 297 -------FIAAIGgmistvylallpvslllgWLAQ----RQLRTLARLEiqrgherhGLLVDTIQGAETIQSSGSGW--- 362
Cdd:COG4988 167 tapliplFMILVG------------------KGAAkasrRQWRALARLS--------GHFLDRLRGLTTLKLFGRAKaea 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 363 ----FFADLWRSIT----------------------ASMAAYSLKSklissltttttatlstvgyvaavvvgvLLieAGQ 416
Cdd:COG4988 221 eriaEASEDFRKRTmkvlrvaflssavleffaslsiALVAVYIGFR---------------------------LL--GGS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 417 LTTGGLIACTILGGKVIGPIAQsVGilVQWqHVR----EALEMVNRLLALEGNRPEGKVLLVPETLPDRLELEGVRFAYP 492
Cdd:COG4988 272 LTLFAALFVLLLAPEFFLPLRD-LG--SFY-HARangiAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 493 GTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGT 572
Cdd:COG4988 348 GGRPA-LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGT 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 573 LKNNIMLAG-GINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDT 651
Cdd:COG4988 427 IRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDA 506
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 652 ESEERVLKALQSHTRpTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:COG4988 507 ETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
275-705 |
2.48e-64 |
|
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: 223.87 E-value: 2.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 275 TFFSSTIVFAMTDLPFGLMFIVFIAAIGGMIStvylallpvslllgWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAET 354
Cdd:COG4987 142 VILAAVAFLAFFSPALALVLALGLLLAGLLLP--------------LLAARLGRRAGRRLAAARAALRARLTDLLQGAAE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 355 IQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTtGGLIACTILG----G 430
Cdd:COG4987 208 LAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAalalF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 431 KVIGPIAQSVgilVQWQHVREALEMVNRLLALEGNRPEGKVLLVPETLPDrLELEGVRFAYPGTPVIRLQVETLAFGPGD 510
Cdd:COG4987 287 EALAPLPAAA---QHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPS-LELEDVSFRYPGAGRPVLDGLSLTLPPGE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 511 RVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLA-GGINDARFL 589
Cdd:COG4987 363 RVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLArPDATDEELW 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 590 EVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPtD 669
Cdd:COG4987 443 AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-R 521
|
410 420 430
....*....|....*....|....*....|....*.
gi 2542252196 670 IVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG4987 522 TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
482-694 |
5.46e-54 |
|
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: 183.35 E-value: 5.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNImlaggindarflevaellgldrvaadsprsmdteiseggqgLSGGQRQLTAISRIFLARPRVWL 641
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 642 LDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLLSLANRLLIMRRGQ 694
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVI-AHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
165-456 |
1.05e-52 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 184.32 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 165 RWLL-EVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18566 1 RPLLpQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRLDK-RPRSLGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWL 322
Cdd:cd18566 81 AFEHLLSLPLSFfEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 323 AQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYV 402
Cdd:cd18566 161 LGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 403 AAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMV 456
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
450-690 |
3.10e-50 |
|
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: 184.03 E-value: 3.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 450 REALEMVNRLLAlEGNRPEGKVLLVPETLPDRLELEGVRFAYPGTPViRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLA 529
Cdd:TIGR02857 291 VAAAEALFAVLD-AAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 530 AGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLA-GGINDARFLEVAELLGLDRVAADSPRSM 608
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 609 DTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL----QSHTrptdiVLIATHRPRLLSLA 684
Cdd:TIGR02857 449 DTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALralaQGRT-----VLLVTHRLALAALA 523
|
....*.
gi 2542252196 685 NRLLIM 690
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
481-705 |
8.25e-48 |
|
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: 168.56 E-value: 8.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAY-PGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERI 559
Cdd:cd03254 2 EIEFENVNFSYdEKKPV--LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKGTLKNNIMLAG-GINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPR 638
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
482-695 |
2.89e-47 |
|
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: 165.08 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNImlaggindarflevaellgldrvaadsprsmdteiseggqgLSGGQRQltaisRIFLAR----- 636
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQ-----RLGLARalygn 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 637 PRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
482-705 |
5.05e-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: 166.35 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIG 560
Cdd:COG1122 1 IELENLSFSYPgGTPALD-DV-SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQ--DVHLFKGTLKNNIMLaGGIN--------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAIS 630
Cdd:COG1122 79 LVFQnpDDQLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPHE-----------LSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 631 RIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
482-695 |
1.26e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:COG4619 1 LELEGLSFRVGGKPILS-PV-SLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNIMLAGGI-----NDARFLEVAELLGLDrvaadsPRSMDTEISEggqgLSGGQRQLTAISRIFLAR 636
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLrerkfDRERALELLERLGLP------PDILDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 637 PRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLS-LANRLLIMRRGQV 695
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRaVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
481-705 |
1.46e-43 |
|
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: 157.51 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIG 560
Cdd:COG1120 1 MLEAENLSVGYGGRPVLD-DV-SLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHL-FKGTLKNNIML-------AGGINDARFLEVA----ELLGLDRVAAdspRSMDTeiseggqgLSGGQRQLTA 628
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALgryphlgLFGRPSAEDREAVeealERTGLEHLAD---RPVDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRL-LSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRtVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
482-705 |
6.28e-43 |
|
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: 155.08 E-value: 6.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNIMLAG-GINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVW 640
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 641 LLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIA-HRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
443-678 |
1.18e-42 |
|
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: 162.53 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 443 LVQWQHVREALEMVNRLLALEGNRPEGKV---LLVPETLPDrLELEGVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNG 519
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPVAEGSApaaGAVGLGKPT-LELRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 520 CGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLA-GGINDARFLEVAELLGLD 598
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLArPDATDEELWAALERVGLA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 599 RVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRP 678
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLI-THHL 530
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
482-698 |
1.54e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.66 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP--GTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVL---- 555
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 GERIGYLPQDVHLFKG-TLKNNIMLAGGIN-------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLT 627
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLLLAgvsrkerRERARELLERVGLGDRLDHRPSQ-----------LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSLANRLLIMRRGQVIAD 698
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTtIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
164-454 |
2.25e-42 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 155.45 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRLDKRPRslGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWLA 323
Cdd:cd18586 81 VFRAVLELPLESRPS--GYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 324 QRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYVA 403
Cdd:cd18586 159 HRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 404 AVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALE 454
Cdd:cd18586 239 ILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYE 289
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
482-705 |
5.25e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.53 E-value: 5.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLgER 558
Cdd:COG1131 1 IEVRGLTKRYGDKTALDgvsLTVE-----PGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKG-TLKNNIMLAGGI-------NDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAIS 630
Cdd:COG1131 75 IGYVPQEPALYPDlTVRENLRFFARLyglprkeARERIDELLELFGLTDAADRKVGT-----------LSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 631 RIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHrprLLS----LANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTH---YLEeaerLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
483-705 |
2.51e-41 |
|
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: 150.77 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTP-VIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:cd03249 2 EFKNVSFRYPSRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNIMLagGINDARFLEV---AELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPR 638
Cdd:cd03249 82 VSQEPVLFDGTIAENIRY--GKPDATDEEVeeaAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIA-HRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
482-705 |
2.00e-40 |
|
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: 148.15 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIRlqveTLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER 558
Cdd:cd03253 1 IEFENVTFAYdPGRPVLK----DVSFTipAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKGTLKNNIMLAG-GINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARP 637
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 638 RVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
483-694 |
1.65e-39 |
|
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: 144.92 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYL 562
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQ--DVHLFKGTLK-------NNIMLAGGINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIF 633
Cdd:cd03225 81 FQnpDDQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKAL-QSHTRPTDIVlIATHRP-RLLSLANRLLIMRRGQ 694
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLkKLKAEGKTII-IVTHDLdLLLELADRVIVLEDGK 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
160-705 |
1.49e-38 |
|
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: 152.59 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 160 LLRDKRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIA 239
Cdd:TIGR01193 151 ITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 240 LSQQLYEHLLDLRLDK-RPRSLGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLL 318
Cdd:TIGR01193 231 IILSYIKHLFELPMSFfSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 319 LGWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGwffADLWRSITASMAAY---SLKSKLISSLTTTTTAT 395
Cdd:TIGR01193 311 IIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSE---AERYSKIDSEFGDYlnkSFKYQKADQGQQAIKAV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 396 LSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMVNRLLALEGNRPEGKVLLVP 475
Cdd:TIGR01193 388 TKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 476 ETLPDRLELEGVRFAYP-GTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQV 554
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGyGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 LGERIGYLPQDVHLFKGTLKNNIMLAG--GINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRI 632
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSGSILENLLLGAkeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 633 FLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTdIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKT-IIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
483-694 |
2.41e-38 |
|
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: 139.69 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYL 562
Cdd:cd00267 1 EIENLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQdvhlfkgtlknnimlaggindarflevaellgldrvaadsprsmdteiseggqgLSGGQRQLTAISRIFLARPRVWLL 642
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 643 DEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLA-NRLLIMRRGQ 694
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
172-705 |
2.79e-38 |
|
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: 150.25 E-value: 2.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 172 VATVVVNLLAVATSLFSMQVYDRVVPTFAYAT---LWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHL 248
Cdd:TIGR02203 18 LAGVAMILVAATESTLAALLKPLLDDGFGGRDrsvLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 249 LDL---RLDKRPrsLGSLAAQMngletvrTFFSSTIVFAMTDlpfglMFIVFI----AAIGGMISTVYL------ALLPV 315
Cdd:TIGR02203 98 LGLpvsFFDRQP--TGTLLSRI-------TFDSEQVASAATD-----AFIVLVretlTVIGLFIVLLYYswqltlIVVVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 316 SLLLGWLAQRQLRTLARL--EIQRGHERHGLLVD-TIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTT 392
Cdd:TIGR02203 164 LPVLSILMRRVSKRLRRIskEIQNSMGQVTTVAEeTLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 393 TATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMVNRLLALEGNRPEGKVl 472
Cdd:TIGR02203 244 TQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTR- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 473 lVPETLPDRLELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP 552
Cdd:TIGR02203 323 -AIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 553 QVLGERIGYLPQDVHLFKGTLKNNIMLA--GGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAIS 630
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFNDTIANNIAYGrtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 631 RIFLARPRVWLLDEPSASLDTESEERVLKALQsHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALE-RLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
482-695 |
8.27e-38 |
|
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: 140.32 E-value: 8.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP--GTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLG--- 556
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 -ERIGYLPQDVHLFKG-TLKNNIMLA-------GGINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLT 627
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPSE-----------LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTtIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
483-699 |
1.02e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 138.72 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYL 562
Cdd:cd03214 1 EVENLSVGYGGRTVLD-DL-SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQdvhlfkgtlknnimlaggindarfleVAELLGLDRVAadsPRSMDTeiseggqgLSGGQRQLTAISRIFLARPRVWLL 642
Cdd:cd03214 79 PQ--------------------------ALELLGLAHLA---DRPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 643 DEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRL-LSLANRLLIMRRGQVIADG 699
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKtVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
482-705 |
1.62e-37 |
|
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: 140.31 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNIMLAG-GINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVW 640
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADpGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 641 LLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIA-HRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
482-704 |
2.15e-36 |
|
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: 136.91 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQveTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLgERIGY 561
Cdd:COG4555 2 IEVENLSKKYGKVPALKDV--SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKG-TLKNNIMLAGGIND-------ARFLEVAELLGLDRVAadsprsmDTEISEggqgLSGGQRQLTAISRIF 633
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGlfdeelkKRIEELIELLGLEEFL-------DRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLS-LANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
482-705 |
3.31e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 3.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGAdiwelDPQVLGERIGY 561
Cdd:COG1121 7 IELENLTVSYGGRPVLE-DV-SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGT-----------LKNNIMLAGGINDARFLEVAELlgLDRVAADSPRsmDTEISEggqgLSGGQRQltais 630
Cdd:COG1121 80 VPQRAEVDWDFpitvrdvvlmgRYGRRGLFRRPSRADREAVDEA--LERVGLEDLA--DRPIGE----LSGGQQQ----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 631 RIFLAR-----PRVWLLDEPSASLDTESEE---RVLKALQSHTRptdIVLIATHRPRLLS-LANRLLIMRRGqVIADGPP 701
Cdd:COG1121 147 RVLLARalaqdPDLLLLDEPFAGVDAATEEalyELLRELRREGK---TILVVTHDLGAVReYFDRVLLLNRG-LVAHGPP 222
|
....
gi 2542252196 702 AEVI 705
Cdd:COG1121 223 EEVL 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
482-705 |
5.63e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 143.43 E-value: 5.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNIMLAG-GINDARFLEVAELLGLDRVaADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVW 640
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKL-LEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 641 LLDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQNKTVLMI-THRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
481-689 |
1.80e-35 |
|
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: 133.37 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTPVIR-LqveTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVlGERI 559
Cdd:COG4133 2 MLEAENLSCRRGERLLFSgL---SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKG-TLKNNIMLAGGI-----NDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIF 633
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFWAALyglraDREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLI 689
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
481-701 |
9.58e-35 |
|
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: 131.85 E-value: 9.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAY-PGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERI 559
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPV-LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRV 639
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 640 WLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPP 701
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIA-HRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
499-705 |
1.66e-34 |
|
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: 131.30 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 499 LQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlGERIGYLPQDVHLFKG-TLKNNI 577
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 mlAGGIN---------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSAS 648
Cdd:cd03299 93 --AYGLKkrkvdkkeiERKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 649 LDTESEERVLKALQSHTRPTDI-VLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVtVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
482-699 |
1.93e-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: 130.72 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlqVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlGERIGY 561
Cdd:cd03259 1 LELKGLSKTYGSVRALD--DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKG-TLKNNIMLAGGIN-------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIF 633
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGLKLRgvpkaeiRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERV---LKALQSHTRPTdIVLIATHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELreeLKELQRELGIT-TIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
472-695 |
2.26e-34 |
|
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: 130.67 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 472 LLVPETLPDRLELEGVRFAYPGTP-VIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWEL 550
Cdd:cd03248 2 SLAPDHLKGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 551 DPQVLGERIGYLPQDVHLFKGTLKNNImlAGGINDARFLEVAELLglDRVAADS-----PRSMDTEISEGGQGLSGGQRQ 625
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNI--AYGLQSCSFECVKEAA--QKAHAHSfiselASGYDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL-QSHTRPTdiVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALyDWPERRT--VLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
503-647 |
6.56e-34 |
|
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: 126.99 E-value: 6.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKG-TLKNNIMLAG 581
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRLGL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 582 GIN-------DARFLEVAELLGLDRVAadsprsmDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSA 647
Cdd:pfam00005 85 LLKglskrekDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
508-699 |
2.47e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 135.74 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGlYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGG-INDA 586
Cdd:PRK11174 375 AGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 587 RFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTR 666
Cdd:PRK11174 454 QLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR 533
|
170 180 190
....*....|....*....|....*....|...
gi 2542252196 667 PTDIVLIaTHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:PRK11174 534 RQTTLMV-THQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
164-456 |
3.64e-33 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 129.54 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRLDK-RPRSLGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWL 322
Cdd:cd18588 81 LFRHLLRLPLSYfESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 323 AQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYV 402
Cdd:cd18588 161 VTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 403 AAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMV 456
Cdd:cd18588 241 AILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
482-695 |
7.01e-33 |
|
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: 124.82 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLgERIGY 561
Cdd:cd03230 1 IEVRNLSKRYGKKTALD-DI-SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKgtlknnimlaggindarFLEVAELLgldrvaadsprsmdteiseggqGLSGGQRQLTAISRIFLARPRVWL 641
Cdd:cd03230 78 LPEEPSLYE-----------------NLTVRENL----------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 642 LDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQV 695
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
482-698 |
1.02e-32 |
|
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: 126.05 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVE--TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqvlgeRI 559
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEdiSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFK-GTLKNNIML---AGGINDA----RFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISR 631
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALgleLQGVPKAeareRAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 632 IFLARPRVWLLDEPSASLDT---ESEERVLKALQSHTRPTdIVLIaTHrpRL---LSLANRLLIM--RRGQVIAD 698
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltrEQLQEELLDIWRETGKT-VLLV-TH--DIdeaVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
483-696 |
1.03e-32 |
|
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: 125.45 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgERIGYL 562
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQDV--HLFKGTLKNNIML-----AGGINDARflEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLA 635
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLglkelDAGNEQAE--TVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 636 RPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSL-ANRLLIMRRGQVI 696
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
414-694 |
1.29e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 133.39 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 414 AGQLTTGGLIACTILGGKVIGP---IAQSVGILVQWQHVrealemVNRLLALEGN-----RPEGKVLLVPETLPDRLELE 485
Cdd:COG4178 293 AGEITLGGLMQAASAFGQVQGAlswFVDNYQSLAEWRAT------VDRLAGFEEAleaadALPEAASRIETSEDGALALE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 486 GVRFAYP-GTPVIRlqVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLggadiweldPQvlGERIGYLPQ 564
Cdd:COG4178 367 DLTLRTPdGRPLLE--DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PA--GARVLFLPQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 565 DVHLFKGTLKNNI---MLAGGINDARFLEVAELLGLDRVAADsprsMDTEiSEGGQGLSGGQRQLTAISRIFLARPRVWL 641
Cdd:COG4178 434 RPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAER----LDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 642 LDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQ 694
Cdd:COG4178 509 LDEATSALDEENEAALYQLLREELPGTTVISVG-HRSTLAAFHDRVLELTGDG 560
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
164-456 |
1.84e-32 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 127.32 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRL---DKRPrsLGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLG 320
Cdd:cd18782 81 IIDHLLRLPLgffDKRP--VGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 321 WLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVG 400
Cdd:cd18782 159 FLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 401 YVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMV 456
Cdd:cd18782 239 SLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
482-705 |
4.30e-32 |
|
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: 125.20 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQV------KLGGADIWELDP 552
Cdd:COG1119 4 LELRNVTVRRGGKTILDdisWTVK-----PGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 553 qvlgeRIGYLPQDVHL-FKGTLK----------NNIMLAGGINDA---RFLEVAELLGLDRVAAdspRSMDTeiseggqg 618
Cdd:COG1119 79 -----RIGLVSPALQLrFPRDETvldvvlsgffDSIGLYREPTDEqreRARELLELLGLAHLAD---RPFGT-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQ---SHTRPTdIVLIaTHRPR-LLSLANRLLIMRRGQ 694
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDklaAEGAPT-LVLV-THHVEeIPPGITHVLLLKDGR 220
|
250
....*....|.
gi 2542252196 695 VIADGPPAEVI 705
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
482-704 |
5.24e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.78 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPV---IRLQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE 557
Cdd:COG3638 3 LELRNLSKRYPgGTPAlddVSLEIE-----RGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 ---RIGYLPQDVHLFKGT--LKNniMLAGGINDARFLEVaeLLG-------------LDRV--AADSPRSMDTeiseggq 617
Cdd:COG3638 78 lrrRIGMIFQQFNLVPRLsvLTN--VLAGRLGRTSTWRS--LLGlfppedreraleaLERVglADKAYQRADQ------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 618 gLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAT-HRPRL-LSLANRLLIMRRGQV 695
Cdd:COG3638 147 -LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQVDLaRRYADRIIGLRDGRV 225
|
....*....
gi 2542252196 696 IADGPPAEV 704
Cdd:COG3638 226 VFDGPPAEL 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
482-705 |
1.14e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.64 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPA---EGQVKLGGADIWELDPQVLGER 558
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQD--VHLFKGTLKNNI---MLAGGIN----DARFLEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQLTAI 629
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIaeaLENLGLSraeaRARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLS-LANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDLGVVAeIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
411-699 |
1.18e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 131.77 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 411 LIEAGQLTTGGLIACTI----LG------GKVIGPIAQSVGIlvqwqhVREALEMVNRLLALEGNrpegkVLLVPETLPD 480
Cdd:TIGR00958 409 LVLTGKVSSGNLVSFLLyqeqLGeavrvlSYVYSGMMQAVGA------SEKVFEYLDRKPNIPLT-----GTLAPLNLEG 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTP-VIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERI 559
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQV 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKGTLKNNImlAGGIN---DARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLAR 636
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENI--AYGLTdtpDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 637 PRVWLLDEPSASLDTESEERVLKALQSHTRPtdiVLIATHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:TIGR00958 636 PRVLILDEATSALDAECEQLLQESRSRASRT---VLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
482-704 |
7.01e-31 |
|
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: 120.75 E-value: 7.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYK-----PAEGQVKLGGADIWELDPQVLG 556
Cdd:cd03260 1 IELRDLNVYYGDKHALK-DI-SLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ER--IGYLPQDVHLFKGTLKNNIMLA---GGINDARFLE--VAELL---GLDRVAADSPrsmdteiseGGQGLSGGQRQL 626
Cdd:cd03260 79 LRrrVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDerVEEALrkaALWDEVKDRL---------HALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLDTES----EERVLKALQSHTrptdiVLIATHRPR-LLSLANRLLIMRRGQVIADGPP 701
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPIStakiEELIAELKKEYT-----IVIVTHNMQqAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 2542252196 702 AEV 704
Cdd:cd03260 225 EQI 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
482-704 |
7.11e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.44 E-value: 7.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER 558
Cdd:COG3842 6 LELENVSKRYGDVTALDdvsLSIE-----PGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLF---------------KGTLKNNImlagginDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGG 622
Cdd:COG3842 78 nVGMVFQDYALFphltvaenvafglrmRGVPKAEI-------RARVAELLELVGLEGLADRYPHQ-----------LSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 623 QRQLTAISRIFLARPRVWLLDEPSASLDTESEERV---LKALQSHTRPTdiVLIATHRPR-LLSLANRLLIMRRGQVIAD 698
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMreeLRRLQRELGIT--FIYVTHDQEeALALADRIAVMNDGRIEQV 217
|
....*.
gi 2542252196 699 GPPAEV 704
Cdd:COG3842 218 GTPEEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
481-704 |
1.76e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.26 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER-I 559
Cdd:COG3839 3 SLELENVSKSYGGVEALK-DI-DLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLF---------------KGTLKNNImlagginDARFLEVAELLGLDRVAADSPRsmdteiseggqGLSGGQR 624
Cdd:COG3839 78 AMVFQSYALYphmtvyeniafplklRKVPKAEI-------DRRVREAAELLGLEDLLDRKPK-----------QLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 625 QLTAISRIFLARPRVWLLDEPSASLD------TESEervLKALQSHTRPTdiVLIATHRPR-LLSLANRLLIMRRGQVIA 697
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrveMRAE---IKRLHRRLGTT--TIYVTHDQVeAMTLADRIAVMNDGRIQQ 214
|
....*..
gi 2542252196 698 DGPPAEV 704
Cdd:COG3839 215 VGTPEEL 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
479-698 |
3.07e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 479 PDRLELEGVRFAYP----GTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqv 554
Cdd:COG1116 5 APALELRGVSKRFPtgggGVTALD-DV-SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 lgeRIGYLPQDVHLF--KgTLKNNIMLA---GGINDARFLEVA----ELLGLDRVAADSPRSmdteiseggqgLSGGQRQ 625
Cdd:COG1116 81 ---DRGVVFQEPALLpwL-TVLDNVALGlelRGVPKAERRERArellELVGLAGFEDAYPHQ-----------LSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDTESEER---VLKALQSHTRPTdiVLIATHRPR-LLSLANRLLIMRR--GQVIAD 698
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERlqdELLRLWQETGKT--VLFVTHDVDeAVFLADRVVVLSArpGRIVEE 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
482-699 |
3.53e-30 |
|
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: 117.03 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvLGERIGY 561
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNImlaggindarflevaellgldrvaadsprsmdteisegGQGLSGGQRQLTAISRIFLARPRVWL 641
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 642 LDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWI-THHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
482-704 |
6.20e-30 |
|
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: 118.31 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER-IG 560
Cdd:cd03219 1 LEVRGLTKRFGGLVALD-DV-SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLFKG-TLKNNIMLA------GGINDARF-----------LEVAELLGLDRVAADSPRSmdteiseggqgLSGG 622
Cdd:cd03219 79 RTFQIPRLFPElTVLENVMVAaqartgSGLLLARArreereareraEELLERVGLADLADRPAGE-----------LSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 623 QRQLTAISRIFLARPRVWLLDEPSASL-DTESEE--RVLKALQSHTRPtdIVLIATHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLnPEETEElaELIRELRERGIT--VLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
....*
gi 2542252196 700 PPAEV 704
Cdd:cd03219 226 TPDEV 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
482-704 |
6.92e-30 |
|
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: 117.92 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER 558
Cdd:cd03224 1 LEVENLNAGYGKSQILFgvsLTVP-----EGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLFKG-TLKNNIMLAGGINDARflEVAEllGLDRVAADSPRSMDTEISEGGQgLSGGQRQLTAISRIFLAR 636
Cdd:cd03224 76 gIGYVPEGRRIFPElTVEENLLLGAYARRRA--KRKA--RLERVYELFPRLKERRKQLAGT-LSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 637 PRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
441-705 |
9.89e-30 |
|
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: 123.86 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 441 GILVQWQHVREALEMVNRLLALEGNRPEGKVLLVPETLPDR-LELEGVRFAYPGTPVIRLQV---ETLAFGPGDRVVVMG 516
Cdd:COG1123 219 GRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPlLEVRNLSKRYPVRGKGGVRAvddVSLTLRRGETLGLVG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 517 PNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE---RIGYLPQDVH--LFKGT---------LKNNIMLAGG 582
Cdd:COG1123 299 ESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDPYssLNPRMtvgdiiaepLRLHGLLSRA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 583 INDARFLEVAELLGLDRVAAD-SPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL 661
Cdd:COG1123 379 ERRERVAELLERVGLPPDLADrYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLL 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2542252196 662 QSHTRPTDI-VLIATHRPRL-LSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG1123 448 RDLQRELGLtYLFISHDLAVvRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
481-701 |
2.51e-29 |
|
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: 115.59 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEG--VRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVL 555
Cdd:cd03369 6 EIEVENlsVRYAPDLPPVLKnvsFKVK-----AGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 GERIGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVaellgldrvaadsprsmdTEISEGGQGLSGGQRQLTAISRIFLA 635
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 636 RPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADGPP 701
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIA-HRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
481-696 |
1.39e-28 |
|
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: 121.47 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAY-PGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLG 556
Cdd:COG5265 357 EVRFENVSFGYdPERPILKgvsFEVP-----AGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ERIGYLPQDVHLFKGTLKNNImlAGGINDARFLEV---AELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIF 633
Cdd:COG5265 432 AAIGIVPQDTVLFNDTIAYNI--AYGRPDASEEEVeaaARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRprlLSL---ANRLLIMRRGQVI 696
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA-HR---LSTivdADEILVLEAGRIV 571
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
482-699 |
5.63e-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: 111.90 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGdRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWElDPQVLGERIGY 561
Cdd:cd03264 1 LQLENLTKRYGKKRALD-GV-SLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKG----TLKNNIMLAGGIND----ARFLEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQLTAISRIF 633
Cdd:cd03264 77 LPQEFGVYPNftvrEFLDYIAWLKGIPSkevkARVDEVLELVNLGDRAKKKI-----------GSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQ--SHTRptdIVLIATH-RPRLLSLANRLLIMRRGQVIADG 699
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSelGEDR---IVILSTHiVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
482-704 |
1.11e-27 |
|
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: 112.00 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER 558
Cdd:COG0410 4 LEVENLHAGYGGIHVLHgvsLEVE-----EGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLFKG-TLKNNIMLAGGINDARfLEVAELlgLDRVAADSPRSMDTEISEGGQgLSGGQRQLTAISRIFLAR 636
Cdd:COG0410 79 gIGYVPEGRRIFPSlTVEENLLLGAYARRDR-AEVRAD--LERVYELFPRLKERRRQRAGT-LSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 637 PRVWLLDEPSASLD---TESEERVLKALQShtRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG0410 155 PKLLLLDEPSLGLApliVEEIFEIIRRLNR--EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
482-704 |
1.22e-27 |
|
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: 112.00 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE- 557
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDgvsLDVP-----RGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 --RIGYLPQDVHLFKG-TLKNNIMLA----GGINDA----RFLEVAELLGLDRVAADSPrsmdteiSEggqgLSGGQRQl 626
Cdd:COG1127 81 rrRIGMLFQGGALFDSlTVFENVAFPlrehTDLSEAeireLVLEKLELVGLPGAADKMP-------SE----LSGGMRK- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 taisRIFLAR-----PRVWLLDEPSASLD---TESEERVLKALQSHTRPTdiVLIATHR-PRLLSLANRLLIMRRGQVIA 697
Cdd:COG1127 149 ----RVALARalaldPEILLYDEPTAGLDpitSAVIDELIRELRDELGLT--SVVVTHDlDSAFAIADRVAVLADGKIIA 222
|
....*..
gi 2542252196 698 DGPPAEV 704
Cdd:COG1127 223 EGTPEEL 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
481-699 |
3.61e-27 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 116.74 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAY-PGTPV---IRLQVETLAFgpgdrVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLG 556
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVlqnINLSVPSRGF-----VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ERIGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLAR 636
Cdd:PRK10790 415 QGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 637 PRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVEADTILVLHRGQAVEQG 556
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
508-704 |
3.62e-27 |
|
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: 113.66 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRV-VVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGaDIWeLDPQ----VLGE--RIGYLPQDVHLF-----KGTLKN 575
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVL-QDSArgifLPPHrrRIGYVFQEARLFphlsvRGNLLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 NIMLAGGIND-ARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESE 654
Cdd:COG4148 101 GRKRAPRAERrISFDEVVELLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 655 ERVLKALQSHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4148 170 AEILPYLERLRDELDIpILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
508-699 |
3.81e-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: 109.69 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGAdIW-------ELDPQvlGERIGYLPQDVHLFKG-TLKNNI-- 577
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLfdsrkkiNLPPQ--QRKIGLVFQQYALFPHlNVRENLaf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 ---MLAGGINDARFLEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESE 654
Cdd:cd03297 99 glkRKRNREDRISVDELLDLLGLDHLLNRYP-----------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2542252196 655 ERVLKALQS-HTRPTDIVLIATHRP-RLLSLANRLLIMRRGQVIADG 699
Cdd:cd03297 168 LQLLPELKQiKKNLNIPVIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
482-703 |
7.44e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 108.99 E-value: 7.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP-QV--LGER 558
Cdd:COG2884 2 IRFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRrEIpyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKG-TLKNNIMLA---GGINDA----RFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAIS 630
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvTGKSRKeirrRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 631 RIFLARPRVWLLDEPSASLDTESEERVLKALQshtrptDI------VLIATHRPRLL-SLANRLLIMRRGQVIADGPPAE 703
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLE------EInrrgttVLIATHDLELVdRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
482-704 |
9.59e-27 |
|
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: 109.19 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE---R 558
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFK--GTLKNniMLAGGIND-------ARFLEVAELLG----LDRVAadsprsMDTEISEGGQGLSGGQRQ 625
Cdd:cd03256 80 IGMIFQQFNLIErlSVLEN--VLSGRLGRrstwrslFGLFPKEEKQRalaaLERVG------LLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRL-LSLANRLLIMRRGQVIADGPPAE 703
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGItVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 2542252196 704 V 704
Cdd:cd03256 232 L 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
483-699 |
1.83e-26 |
|
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: 107.62 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweLDPQVLGERIGYL 562
Cdd:cd03235 1 EVEDLTVSYGGHPVLE-DV-SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQDVHL---FKGTLKNNIMLA--------GGINDARFLEVAELlgLDRVA----ADSPrsmdteISEggqgLSGGQRQlt 627
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGlyghkglfRRLSKADKAKVDEA--LERVGlselADRQ------IGE----LSGGQQQ-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 628 aisRIFLAR-----PRVWLLDEPSASLDTESEE---RVLKALQSHTRptdIVLIATHRPRLLS-LANRLLIMRRGqVIAD 698
Cdd:cd03235 140 ---RVLLARalvqdPDLLLLDEPFAGVDPKTQEdiyELLRELRREGM---TILVVTHDLGLVLeYFDRVLLLNRT-VVAS 212
|
.
gi 2542252196 699 G 699
Cdd:cd03235 213 G 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
482-704 |
2.09e-26 |
|
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: 108.74 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP----GTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE 557
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLK-DV-SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 RIGYLPQD----VHLFKgTLKNNIMLAGGIN-----DARFLEVAELLGLDRVAADS-PRSmdteiseggqgLSGGQRQLT 627
Cdd:COG1124 80 RVQMVFQDpyasLHPRH-TVDRILAEPLRIHglpdrEERIAELLEQVGLPPSFLDRyPHQ-----------LSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLS-LANRLLIMRRGQVIADGPPAEV 704
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLtYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
482-695 |
3.40e-26 |
|
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: 106.96 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqvlGER 558
Cdd:cd03301 1 VELENVTKRFGNVTALDdlnLDIAD-----GEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLFKG-TLKNNIMLAGGIN-------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAI 629
Cdd:cd03301 73 dIAMVFQNYALYPHmTVYDNIAFGLKLRkvpkdeiDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESEERV---LKALQSHTRPTdiVLIATH-RPRLLSLANRLLIMRRGQV 695
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMraeLKRLQQRLGTT--TIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
482-705 |
4.75e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:COG4559 2 LEAENLSVRLGGRTLLD-DV-SLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLfkgtlknnimlaggindaRF-LEVAELLGLDRVAADSPRSMDTEISE--------GG------QGLSGGQRQl 626
Cdd:COG4559 80 LPQHSSL------------------AFpFTVEEVVALGRAPHGSSAAQDRQIVRealalvglAHlagrsyQTLSGGEQQ- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 taisRIFLAR------------PRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSL-ANRLLIMRRG 693
Cdd:COG4559 141 ----RVQLARvlaqlwepvdggPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQG 216
|
250
....*....|..
gi 2542252196 694 QVIADGPPAEVI 705
Cdd:COG4559 217 RLVAQGTPEEVL 228
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
164-456 |
5.84e-26 |
|
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: 108.37 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRLDKRPR-SLGSLAAQMNGLETVRTFFSSTIVFAMTD-------LPF--------GLMFIVFIAAIGGMIST 307
Cdd:cd18783 81 TFDRLLSLPIDFFERtPAGVLTKHMQQIERIRQFLTGQLFGTLLDatsllvfLPVlffysptlALVVLAFSALIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 308 VYlallpvslllgWLAQRQLRTLARLEIQRGherhGLLVDTIQGAETIQSsgsgwfFA------DLWRSITASMAAYSLK 381
Cdd:cd18783 161 FL-----------PPFRRRLQALYRAEGERQ----AFLVETVHGIRTVKS------LAleprqrREWDERVARAIRARFA 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 382 SKLISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMV 456
Cdd:cd18783 220 VGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
508-699 |
7.99e-26 |
|
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: 106.44 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQ---VLGERIGYLPQD-------VHLFKGTLKNNI 577
Cdd:cd03257 30 KGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEIQMVFQDpmsslnpRMTIGEQIAEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 MLAGGINDARFLEVAELLGLDRVaADSPRSMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV 657
Cdd:cd03257 110 RIHGKLSKKEARKEAVLLLLVGV-GLPEEVLNRYPHE----LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2542252196 658 LKALQSHTRPTDI-VLIATHRPRLLS-LANRLLIMRRGQVIADG 699
Cdd:cd03257 185 LDLLKKLQEELGLtLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
511-704 |
8.57e-26 |
|
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: 109.43 E-value: 8.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 511 RVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWE------LDPQvlGERIGYLPQDVHLF-----KGTLKNNIML 579
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLFphlsvRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 580 A-GGINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVL 658
Cdd:TIGR02142 103 ArPSERRISFERVIELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2542252196 659 KALQSHTRPTDI-VLIATHRP-RLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:TIGR02142 172 PYLERLHAEFGIpILYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
482-704 |
1.47e-25 |
|
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: 106.77 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIRLQVE--TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE- 557
Cdd:TIGR04521 1 IKLKNVSYIYqPGTPFEKKALDdvSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 --RIGYLPQ--DVHLFKGTLKNNIM-------LAGGINDARFLEVAELLGLDRVAAD-SPRSmdteiseggqgLSGGQRQ 625
Cdd:TIGR04521 81 rkKVGLVFQfpEHQLFEETVYKDIAfgpknlgLSEEEAEERVKEALELVGLDEEYLErSPFE-----------LSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS--HTRPTDIVLIaTHR-PRLLSLANRLLIMRRGQVIADGPPA 702
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILV-THSmEDVAEYADRVIVMHKGKIVLDGTPR 228
|
..
gi 2542252196 703 EV 704
Cdd:TIGR04521 229 EV 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
482-704 |
1.48e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIW-ELDPQvlgER-I 559
Cdd:COG1118 3 IEVRNISKRFGSFTLLD-DV-SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPR---ERrV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKG-TLKNNImlAGGIN---------DARFLEVAELLGLDRVAADSPrsmdteisegGQgLSGGQRQLTAI 629
Cdd:COG1118 78 GFVFQHYALFPHmTVAENI--AFGLRvrppskaeiRARVEELLELVQLEGLADRYP----------SQ-LSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTE--SE-ERVLKALQSHTRPTdiVLIATHRPRL-LSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKvrKElRRWLRRLHDELGGT--TVFVTHDQEEaLELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
482-705 |
1.60e-25 |
|
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: 105.85 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:cd03295 1 IEFENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKG-TLKNNIMLAGGIN-------DARFLEVAELLGLDrvaadsPRS-MDTEISEggqgLSGGQRQLTAISRI 632
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALVPKLLkwpkekiRERADELLALVGLD------PAEfADRYPHE----LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 633 FLARPRVWLLDEPSASLDTESEERV---LKALQSHTRPTdIVLIaTHR-PRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLqeeFKRLQQELGKT-IVFV-THDiDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
482-704 |
1.95e-25 |
|
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: 105.50 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER-IG 560
Cdd:cd03296 3 IEVRNVSKRFGDFVALD-DV-SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLFKG-TLKNNImlAGGIN-------------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQL 626
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV--AFGLRvkprserppeaeiRAKVHELLKLVQLDWLADRYPAQ-----------LSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLDTeseeRVLKALQS-----HTRPTDIVLIATH-RPRLLSLANRLLIMRRGQVIADGP 700
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDA----KVRKELRRwlrrlHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
....
gi 2542252196 701 PAEV 704
Cdd:cd03296 221 PDEV 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
482-703 |
2.50e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPvirLQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqvlGER-IG 560
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AERpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLFKG-TLKNNIMLagGIND---------ARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAIS 630
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGL--GLRPglkltaeqrAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 631 RIFL-ARPrVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQVIADGPPAE 703
Cdd:COG3840 142 RCLVrKRP-ILLLDEPFSALDPALRQEMLDLVDELCRERGLtVLMVTHDPEdAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
482-694 |
2.69e-25 |
|
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: 103.04 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVEtLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER--I 559
Cdd:cd03229 1 LELKNVSKRYGQKTVLN-DVS-LNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKG-TLKNNIMLaggindarflevaellgldrvaadsprsmdteiseggqGLSGGQRQLTAISRIFLARPR 638
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIATHRPR-LLSLANRLLIMRRGQ 694
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
459-705 |
2.77e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 459 LLALEGNRPEGKvlLVPETLPDRLELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEG 538
Cdd:PRK11176 321 ILDLEQEKDEGK--RVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 539 QVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGG--INDARFLEVAELLGLDRVAADSPRSMDTEISEGG 616
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 617 QGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVI 696
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEKADEILVVEDGEIV 557
|
....*....
gi 2542252196 697 ADGPPAEVI 705
Cdd:PRK11176 558 ERGTHAELL 566
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
482-705 |
3.02e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.08 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIW--ELDPQVLG 556
Cdd:COG1126 2 IEIENLHKSFGDLEVLKgisLDVE-----KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ERIGYLPQDVHLFKG-TLKNNIMLA----GGINDARFLEVAELLgLDRVA----ADS-PRSmdteiseggqgLSGGQRQL 626
Cdd:COG1126 77 RKVGMVFQQFNLFPHlTVLENVTLApikvKKMSKAEAEERAMEL-LERVGladkADAyPAQ-----------LSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 TAISRIfLA-RPRVWLLDEPSASLDTESEERVLKALQS--HTRPTdiVLIATH-----RprllSLANRLLIMRRGQVIAD 698
Cdd:COG1126 145 VAIARA-LAmEPKVMLFDEPTSALDPELVGEVLDVMRDlaKEGMT--MVVVTHemgfaR----EVADRVVFMDGGRIVEE 217
|
....*..
gi 2542252196 699 GPPAEVI 705
Cdd:COG1126 218 GPPEEFF 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
481-705 |
3.95e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.73 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELdPqvLGE 557
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKdvsLEVN-----QGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-P--MHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 R----IGYLPQDVHLFKG-TLKNNIM----LAGGINDARFLEVAELL---GLDRVAaDSPrsmdteisegGQGLSGGQRQ 625
Cdd:COG1137 75 RarlgIGYLPQEASIFRKlTVEDNILavleLRKLSKKEREERLEELLeefGITHLR-KSK----------AYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLD--TESEervLKALQSHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQVIADGPP 701
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDpiAVAD---IQKIIRHLKERGIgVLITDHNVReTLGICDRAYIISEGKVLAEGTP 220
|
....
gi 2542252196 702 AEVI 705
Cdd:COG1137 221 EEIL 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
482-694 |
4.13e-25 |
|
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: 103.32 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPG---TPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlgeR 558
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPR 638
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 639 VWLLDEPSASLDTESEERVL-KALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQ 694
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
453-696 |
5.51e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.38 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 453 LEMVNRLLALEGNRPEGKV---LLVPETLPDR-LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKL 528
Cdd:COG0488 283 IKALEKLEREEPPRRDKTVeirFPPPERLGKKvLELEGLSKSYGDKTLLD-DL-SLRIDRGDRIGLIGPNGAGKSTLLKL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 529 AAGLYKPAEGQVKLGgadiweldPQVlgeRIGYLPQDVHLFKgtLKNNIM--LAGGINDARFLEVAELLGL-----DRVa 601
Cdd:COG0488 361 LAGELEPDSGTVKLG--------ETV---KIGYFDQHQEELD--PDKTVLdeLRDGAPGGTEQEVRGYLGRflfsgDDA- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 602 adsprsmDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSH--TrptdiVLIATHRPR 679
Cdd:COG0488 427 -------FKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFpgT-----VLLVSHDRY 490
|
250
....*....|....*...
gi 2542252196 680 LL-SLANRLLIMRRGQVI 696
Cdd:COG0488 491 FLdRVATRILEFEDGGVR 508
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
482-704 |
6.43e-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: 103.76 E-value: 6.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER 558
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRgvsLEVP-----KGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLFKgtlknnimlaggindarFLEVAE--LLGLDrVAADSPRSMDTEISE------------GGQgLSGGQ 623
Cdd:TIGR03410 76 gIAYVPQGREIFP-----------------RLTVEEnlLTGLA-ALPRRSRKIPDEIYElfpvlkemlgrrGGD-LSGGQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 624 RQLTAISRIFLARPRVWLLDEPsasldTE--------SEERVLKALQSHTRPTdIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:TIGR03410 137 QQQLAIARALVTRPKLLLLDEP-----TEgiqpsiikDIGRVIRRLRAEGGMA-ILLVEQYLDFARELADRYYVMERGRV 210
|
....*....
gi 2542252196 696 IADGPPAEV 704
Cdd:TIGR03410 211 VASGAGDEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
482-703 |
1.00e-24 |
|
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: 102.97 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWElDPQVLGERIGY 561
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKG-TLKNNIMLAGGI-------NDARFLEVAELLGLDRVAadsprsmDTEISEggqgLSGGQ-RQL-TAISr 631
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYARLkglpkseIKEEVELLLRVLGLTDKA-------NKRART----LSGGMkRKLsLAIA- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 632 iFLARPRVWLLDEPSASLDTESEERVLKALQShTRPTDIVLIATHRPRLLS-LANRLLIMRRGQVIADGPPAE 703
Cdd:cd03263 148 -LIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEaLCDRIAIMSDGKLRCIGSPQE 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
482-703 |
1.05e-24 |
|
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: 103.28 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGV--RFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELD----PQVL 555
Cdd:COG4181 9 IELRGLtkTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 GERIGYLPQDVHLFKG-TLKNNIMLA---GGINDARFLEVAEL--LGLDRVAADSPRsmdteiseggqGLSGGQRQLTAI 629
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLPlelAGRRDARARARALLerVGLGHRLDHYPA-----------QLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRP--TDIVLIaTHRPRLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLV-THDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
462-705 |
1.22e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.45 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 462 LEGNRPegkvllvPETLPDR--LELEGVRFAY-PGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEG 538
Cdd:PLN03232 1220 IENNRP-------VSGWPSRgsIKFEDVHLRYrPGLPPV-LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 539 QVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQG 618
Cdd:PLN03232 1292 RIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIAD 698
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA-HRLNTIIDCDKILVLSSGQVLEY 1450
|
....*..
gi 2542252196 699 GPPAEVI 705
Cdd:PLN03232 1451 DSPQELL 1457
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
482-704 |
1.42e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP---QVLGer 558
Cdd:COG1129 5 LEMRGISKSFGGVKALD-GV-SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKG-TLKNNIML------AGGINDARFLEVAELLgLDRVAAD-SPrsmDTEISEggqgLSGGQRQLTAIS 630
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLgreprrGGLIDWRAMRRRAREL-LARLGLDiDP---DTPVGD----LSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 631 RIFLARPRVWLLDEPSASL-DTESEE--RVLKALQShtRPTDIVLIaTHR-PRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG1129 153 RALSRDARVLILDEPTASLtEREVERlfRIIRRLKA--QGVAIIYI-SHRlDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
482-704 |
1.76e-24 |
|
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: 102.58 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP---QVLGER 558
Cdd:cd03261 1 IELRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKG-TLKNNIML---------AGGINDaRFLEVAELLGLdRVAADsprSMDTEiseggqgLSGGQRQLTA 628
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFplrehtrlsEEEIRE-IVLEKLEAVGL-RGAED---LYPAE-------LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLD---TESEERVLKALQSHTRPTdiVLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGLT--SIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
503-704 |
2.21e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 102.81 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER-IGYLPQDVHLFKG-TLKNNIMLA 580
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 581 ------GGINDARF----------------LEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPR 638
Cdd:COG0411 104 aharlgRGLLAALLrlprarreereareraEELLERVGLADRADEPAGN-----------LSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 639 VWLLDEPSASL-DTESEE--RVLKALQSHTRPTdIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG0411 173 LLLLDEPAAGLnPEETEElaELIRRLRDERGIT-ILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
482-690 |
4.74e-24 |
|
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: 99.15 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPVIRLQveTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQV-KLGGADIWELdPQVlgeri 559
Cdd:cd03223 1 IELENLSLATPdGRVLLKDL--SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFL-PQR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQdvhlfkGTLKNNIMLAggindarflevaellgLDRVaadsprsmdteiseggqgLSGGQRQLTAISRIFLARPRV 639
Cdd:cd03223 73 PYLPL------GTLREQLIYP----------------WDDV------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 640 WLLDEPSASLDTESEERVLKALQSHTrptdIVLIA-THRPRLLSLANRLLIM 690
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELG----ITVISvGHRPSLWKFHDRVLDL 160
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
411-699 |
7.27e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 411 LIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALEMVNRLLALEGNRPEGKVLLVPETLPDRLELEGVRFA 490
Cdd:PRK13657 264 LVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 491 YPGTpviRLQVETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHL 568
Cdd:PRK13657 344 YDNS---RQGVEDVSFEakPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 FKGTLKNNIMLagGINDARFLEVAEllGLDRVAA-----DSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:PRK13657 421 FNRSIEDNIRV--GRPDATDEEMRA--AAERAQAhdfieRKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 644 EPSASLDTESEERVLKALQ--SHTRPTDIvlIAtHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:PRK13657 497 EATSALDVETEAKVKAALDelMKGRTTFI--IA-HRLSTVRNADRILVFDNGRVVESG 551
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
508-678 |
1.14e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.56 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqvlGERIGYL-PQDvhlfkgTLKNNIMLAG----- 581
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLgHRN------AMKPALTVAEnlefw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 ----GINDARFLEVAELLGLDRVAaDSPrsmdteisegGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV 657
Cdd:PRK13539 98 aaflGGEELDIAAALEAVGLAPLA-HLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|.
gi 2542252196 658 LKALQSHTRPTDIVLIATHRP 678
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIP 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
482-705 |
1.46e-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: 99.92 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER--- 558
Cdd:cd03218 1 LRAENLSKRYGKRKVVN-GV-SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH---KRarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLFKG-TLKNNIMLA-------GGINDARFLEVAELLGLDRVaADSPrsmdteisegGQGLSGGQRQLTAI 629
Cdd:cd03218 76 gIGYLPQEASIFRKlTVEENILAVleirglsKKEREEKLEELLEEFHITHL-RKSK----------ASSLSGGERRRVEI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 630 SRIFLARPRVWLLDEPSASLD--TESEervLKALQSHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDpiAVQD---IQKIIKILKDRGIgVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
482-705 |
4.02e-23 |
|
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: 98.81 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVE--TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE-- 557
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 -RIGYLPQDVHLFKG-TLKNNIMLAGGIN-------DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTA 628
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEIAgvpkaeiEERVLELLELVGLEDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLtIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
164-454 |
5.39e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 99.94 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRL---DKRPRslGSLAAQMNGLETVRTFFSSTIVFAMTDL-----PFGLMF----------IVFIAAIggMI 305
Cdd:cd18568 81 FYKHLLSLPLsffASRKV--GDIITRFQENQKIRRFLTRSALTTILDLlmvfiYLGLMFyynlqltlivLAFIPLY--VL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 306 STVylallpvslllgwLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLI 385
Cdd:cd18568 157 LTL-------------LSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 386 SSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALE 454
Cdd:cd18568 224 SIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVE 292
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
482-695 |
1.13e-22 |
|
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: 96.83 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPV---IRLQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQV--LG 556
Cdd:cd03262 1 IEIKNLHKSFGDFHVlkgIDLTVK-----KGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ERIGYLPQDVHLFKG-TLKNNIMLA----GGINDARFLEVA-ELL---GLDRVAADSPRSmdteiseggqgLSGGQRQLT 627
Cdd:cd03262 76 QKVGMVFQQFNLFPHlTVLENITLApikvKGMSKAEAEERAlELLekvGLADKADAYPAQ-----------LSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRL-LSLANRLLIMRRGQV 695
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
482-694 |
1.19e-22 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 96.55 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELD----PQvLGE 557
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAA-LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRgrqlPL-LRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 RIGYLPQDVHLFKG-TLKNNI---MLAGGINDA----RFLEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQLTAI 629
Cdd:TIGR02673 80 RIGVVFQDFRLLPDrTVYENValpLEVRGKKEReiqrRVGAALRQVGLEHKADAFP-----------EQLSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSL-ANRLLIMRRGQ 694
Cdd:TIGR02673 149 ARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRvAHRVIILDDGR 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
514-704 |
1.19e-22 |
|
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: 99.49 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGerIGYLPQDVHLFKG-TLKNNImlAGGIN-------- 584
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH--INMVFQSYALFPHmTVEENV--AFGLKmrkvprae 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 -DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV---LKA 660
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQ-----------LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqleLKT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2542252196 661 LQSHTRPTdiVLIATHRPR-LLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:TIGR01187 146 IQEQLGIT--FVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
503-699 |
1.25e-22 |
|
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: 96.08 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGL--YKPAEGQVKLGGADiweLDPQVLGERIGYLPQDVHLFKG-TLKNNIML 579
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHPTlTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 580 AggindarflevAELlgldrvaadsprsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLK 659
Cdd:cd03213 106 A-----------AKL----------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2542252196 660 ALQSHTRPTDIVLIATHRPR--LLSLANRLLIMRRGQVIADG 699
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
164-459 |
1.57e-22 |
|
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: 98.29 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLrldkrP------RSLGSLAAQMNGLETVRTFFSSTIVFAMTDLpfgLMFIV-------------FIAAIGGM 304
Cdd:cd18570 81 YFKHLLKL-----PlsffetRKTGEIISRFNDANKIREAISSTTISLFLDL---LMVIIsgiilffynwklfLITLLIIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 305 ISTVYLallpvslllgWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKL 384
Cdd:cd18570 153 LYILII----------LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGK 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 385 ISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQhvrEALEMVNRL 459
Cdd:cd18570 223 LSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQ---EAKVAADRL 294
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
482-704 |
2.26e-22 |
|
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: 96.54 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER-IG 560
Cdd:cd03300 1 IELENVSKFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRpVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLF---------------KGTLKNNImlagginDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQ 625
Cdd:cd03300 76 TVFQNYALFphltvfeniafglrlKKLPKAEI-------KERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDT---ESEERVLKALQSHTRPTdiVLIATH-RPRLLSLANRLLIMRRGQVIADGPP 701
Cdd:cd03300 138 RVAIARALVNEPKVLLLDEPLGALDLklrKDMQLELKRLQKELGIT--FVFVTHdQEEALTMSDRIAVMNKGKIQQIGTP 215
|
...
gi 2542252196 702 AEV 704
Cdd:cd03300 216 EEI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
462-705 |
3.50e-22 |
|
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: 102.72 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 462 LEGNRPegkvllvPETLPDRLELE----GVRFAyPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAE 537
Cdd:TIGR00957 1270 IQETAP-------PSGWPPRGRVEfrnyCLRYR-EDLDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAE 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 538 GQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQ 617
Cdd:TIGR00957 1341 GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 618 GLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVIA 697
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA-HRLNTIMDYTRVIVLDKGEVAE 1499
|
....*...
gi 2542252196 698 DGPPAEVI 705
Cdd:TIGR00957 1500 FGAPSNLL 1507
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
482-704 |
7.22e-22 |
|
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: 95.44 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWEL---DPQVLGER 558
Cdd:TIGR02315 2 LEVENLSKVYPNGKQA-LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHL----------------FKGTLKNNIMLAGGINDARFLEVAELLGLDRVA---ADSprsmdteiseggqgL 619
Cdd:TIGR02315 81 IGMIFQHYNLierltvlenvlhgrlgYKPTWRSLLGRFSEEDKERALSALERVGLADKAyqrADQ--------------L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 620 SGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRL-LSLANRLLIMRRGQVIA 697
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGItVIINLHQVDLaKKYADRIVGLKAGEIVF 226
|
....*..
gi 2542252196 698 DGPPAEV 704
Cdd:TIGR02315 227 DGAPSEL 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
482-698 |
1.04e-21 |
|
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: 92.49 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlgerigy 561
Cdd:cd03216 1 LELRGITKRFGGVKALD-GV-SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 lpQDVHLfkgtlknnimlaGGINDARFLevaellGLDRVAadsprsmdteiseggQgLSGGQRQLTAISRIFLARPRVWL 641
Cdd:cd03216 62 --KEVSF------------ASPRDARRA------GIAMVY---------------Q-LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 642 LDEPSASL-DTESEE--RVLKALQSHTRPtdIVLIaTHRPR-LLSLANRLLIMRRGQVIAD 698
Cdd:cd03216 106 LDEPTAALtPAEVERlfKVIRRLRAQGVA--VIFI-SHRLDeVFEIADRVTVLRDGRVVGT 163
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
482-705 |
1.13e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.22 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:PRK13548 3 LEARNLSVRLGGRTLLD-DV-SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHL-FKGTLKNNIMLAGGINDARFLEVAELLG--LDRVAADSPRSMDTeiseggQGLSGGQRQltaisRIFLAR-- 636
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAaaLAQVDLAHLAGRDY------PQLSGGEQQ-----RVQLARvl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 637 ---------PRVWLLDEPSASLDTESEERVLKALQS--HTRPTDiVLIATHRPRLLSL-ANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13548 150 aqlwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQlaHERGLA-VIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEV 228
|
.
gi 2542252196 705 I 705
Cdd:PRK13548 229 L 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
482-694 |
1.28e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 91.36 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlGERIGY 561
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQdvhlfkgtlknnimlaggindarflevaellgldrvaadsprsmdteiseggqgLSGGQRQLTAISRIFLARPRVWL 641
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 642 LDEPSASLDTESEERVLKALQSHTRptdIVLIATHRPRLLS-LANRLLIMRRGQ 694
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDqVATKIIELEDGK 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
482-705 |
1.40e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:PRK11231 3 LRTENLTVGYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQdVHLfkgtlknnimLAGGINdarfleVAELLGLDRvaadSP-----------------RSM-DTEISEGGQ----GL 619
Cdd:PRK11231 81 LPQ-HHL----------TPEGIT------VRELVAYGR----SPwlslwgrlsaednarvnQAMeQTRINHLADrrltDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 620 SGGQRQltaisRIFLA------RPRVwLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRprlLSLANR----LLI 689
Cdd:PRK11231 140 SGGQRQ-----RAFLAmvlaqdTPVV-LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD---LNQASRycdhLVV 210
|
250
....*....|....*.
gi 2542252196 690 MRRGQVIADGPPAEVI 705
Cdd:PRK11231 211 LANGHVMAQGTPEEVM 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
482-676 |
2.47e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:PRK10247 8 LQLQNVGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAAdsPRSM-DTEISEggqgLSGGQRQLTAISRIFLARPRVW 640
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFAL--PDTIlTKNIAE----LSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2542252196 641 LLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATH 676
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIaVLWVTH 196
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
487-695 |
2.54e-21 |
|
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: 94.54 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 487 VRFAYPGTPVIrlqvETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKpAEGQVKLGGADIWELDPQVLGERIGYLPQ 564
Cdd:cd03289 10 AKYTEGGNAVL----ENISFSisPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 565 DVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDE 644
Cdd:cd03289 85 KVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 645 PSASLDTESEERVLKALQsHTRPTDIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:cd03289 165 PSAHLDPITYQVIRKTLK-QAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
482-698 |
2.57e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.00 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVR--FaYPGTP--VIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE 557
Cdd:COG1101 2 LELKNLSktF-NPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 RIGYLPQDVhlFKGTLKN-----NIMLA----------GGINDAR---FLEVAELLGL---DRvaadsprsMDTEIsegG 616
Cdd:COG1101 81 YIGRVFQDP--MMGTAPSmtieeNLALAyrrgkrrglrRGLTKKRrelFRELLATLGLgleNR--------LDTKV---G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 617 QgLSGGQRQltAISRIF--LARPRVWLLDEPSASLDTESEERVLKAlqshTRptDIV-------LIATHRPR-LLSLANR 686
Cdd:COG1101 148 L-LSGGQRQ--ALSLLMatLTKPKLLLLDEHTAALDPKTAALVLEL----TE--KIVeennlttLMVTHNMEqALDYGNR 218
|
250
....*....|..
gi 2542252196 687 LLIMRRGQVIAD 698
Cdd:COG1101 219 LIMMHEGRIILD 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
503-687 |
4.35e-21 |
|
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: 91.65 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvLGERIGYLPqdvHL--FKGTL---KNNI 577
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLG---HLpgLKPELsalENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 MLAGGINDARF-----LEVAELLGLDRVAADSprsmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTE 652
Cdd:TIGR01189 96 FWAAIHGGAQRtiedaLAAVGLTGFEDLPAAQ--------------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2542252196 653 SEERVLKALQSHTRPTDIVLIATHRPRLLSLANRL 687
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQDLGLVEAREL 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
482-704 |
5.39e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.96 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPV-------IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWE--LD 551
Cdd:PRK13637 3 IKIENLTHIYmEGTPFekkaldnVNIEIED-----GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 552 PQVLGERIGYLPQ--DVHLFKGTLKNNIMLAG---GINDA----RFLEVAELLGLDR--VAADSPRSmdteiseggqgLS 620
Cdd:PRK13637 78 LSDIRKKVGLVFQypEYQLFEETIEKDIAFGPinlGLSEEeienRVKRAMNIVGLDYedYKDKSPFE-----------LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 621 GGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIATHRPRLLS-LANRLLIMRRGQVIAD 698
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNMTIILVSHSMEDVAkLADRIIVMNKGKCELQ 226
|
....*.
gi 2542252196 699 GPPAEV 704
Cdd:PRK13637 227 GTPREV 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
482-695 |
7.63e-21 |
|
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: 91.70 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWEL-DPQV--LGER 558
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrGRAIpyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLF-KGTLKNNIMLAGGINDA-------RFLEVAELLGLdrvaADSPRSMDTEiseggqgLSGGQRQLTAIS 630
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFALEVTGVppreirkRVPAALELVGL----SHKHRALPAE-------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 631 RIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQV 695
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
482-699 |
8.37e-21 |
|
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: 91.40 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPvIRLqveTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqvlGER-IG 560
Cdd:cd03298 1 VRLDKIRFSYGEQP-MHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRpVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLFKG-TLKNNIMLA-------GGINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRI 632
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlspglklTAEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 633 FLARPRVWLLDEPSASLDTESEERVLK-ALQSHTRPTDIVLIATHRPR-LLSLANRLLIMRRGQVIADG 699
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDlVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
490-690 |
8.89e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 8.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 490 AYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlGERIGYLPQDVHL- 568
Cdd:NF040873 1 GYGGRPVLH-GV-DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 --FKGTLKNNIMLA----------GGINDARFLEVA-ELLGLDRVAadsPRSMDTeiseggqgLSGGQRQLTAISRIFLA 635
Cdd:NF040873 68 dsLPLTVRDLVAMGrwarrglwrrLTRDDRAAVDDAlERVGLADLA---GRQLGE--------LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 636 RPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIM 690
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
482-704 |
1.22e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGG-----ADIWELDpqvlg 556
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVR----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ERIGYLPQDV-HLFKGT---------LKNNimlagGIND----ARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGG 622
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGAtvqddvafgLENI-----GVPReemvERVDQALRQVGMEDFLNREPHR-----------LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 623 QRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSLANRLLIMRRGQVIADGPP 701
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
...
gi 2542252196 702 AEV 704
Cdd:PRK13635 225 EEI 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
482-676 |
1.36e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.62 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKP---AEGQVKLGGADIWELDPQVl 555
Cdd:COG4136 2 LSLENLTITLGGRPLLAplsLTVA-----PGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 gERIGYLPQDVHLFKG-TLKNNIM--LAGGIN----DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTA 628
Cdd:COG4136 76 -RRIGILFQDDLLFPHlSVGENLAfaLPPTIGraqrRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATH 676
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTH 192
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
503-704 |
1.51e-20 |
|
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: 90.28 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGL--YKPAEGQVKLGGADIWELDPQvlgERIgylpqdvhlfkgtlKNNIMLA 580
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE---ERA--------------RLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 581 ggindarFLEVAELLGLdRVaADSPRSMDteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKA 660
Cdd:cd03217 83 -------FQYPPEIPGV-KN-ADFLRYVN-------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542252196 661 LQSHTRPTDIVLIATHRPRLLSL--ANRLLIMRRGQVIADGPPAEV 704
Cdd:cd03217 147 INKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSGDKELA 192
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
508-701 |
1.65e-20 |
|
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: 91.89 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGGINDAR 587
Cdd:cd03288 46 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 588 FLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRP 667
Cdd:cd03288 126 LWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD 205
|
170 180 190
....*....|....*....|....*....|....*
gi 2542252196 668 TDIVLIAtHRPRLLSLANRLLIMRRGQVIA-DGPP 701
Cdd:cd03288 206 RTVVTIA-HRVSTILDADLVLVLSRGILVEcDTPE 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
466-704 |
2.21e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 466 RPEGKVllvPETLPDRLELEGVRFAYPGTPVIrlQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGA 545
Cdd:PRK11607 7 RPQAKT---RKALTPLLEIRNLTKSFDGQHAV--DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 546 DIWELDPQvlgER-IGYLPQDVHLFKG-TLKNNIM-------LAGGINDARFLEVAELLGLDRVAADSPRSmdteisegg 616
Cdd:PRK11607 82 DLSHVPPY---QRpINMMFQSYALFPHmTVEQNIAfglkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQ--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 617 qgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV-LKALQSHTRPTDIVLIATH-RPRLLSLANRLLIMRRGQ 694
Cdd:PRK11607 150 --LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
|
250
....*....|
gi 2542252196 695 VIADGPPAEV 704
Cdd:PRK11607 228 FVQIGEPEEI 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
482-701 |
2.30e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPG--TPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLG--- 556
Cdd:PRK10535 5 LELKDIRRSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 -ERIGYLPQDVHLFKG-TLKNNI----MLAGGINDARFLEVAEL---LGL-DRVaadsprsmDTEISEggqgLSGGQRQL 626
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHlTAAQNVevpaVYAGLERKQRLLRAQELlqrLGLeDRV--------EYQPSQ----LSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLDTESEERVLKAL-----QSHTrptdiVLIATHRPRLLSLANRLLIMRRGQVIADGPP 701
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILhqlrdRGHT-----VIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
491-676 |
2.53e-20 |
|
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: 89.40 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 491 YPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIwELDPQVLGE---RIGYLPQDV- 566
Cdd:TIGR01166 1 YPGGPEV-LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLErrqRVGLVFQDPd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 567 -HLFKGTLKN-------NIMLAGGINDARFLEVAELLGLDRVaADSPRSMdteiseggqgLSGGQRQLTAISRIFLARPR 638
Cdd:TIGR01166 79 dQLFAADVDQdvafgplNLGLSEAEVERRVREALTAVGASGL-RERPTHC----------LSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATH 676
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
482-704 |
3.60e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.09 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER 558
Cdd:PRK09452 15 VELRGISKSFDGKEVISnldLTINN-----GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 -IGYLPQDVHLFKG-TLKNNimlaggindarfleVAELLGLDRVAAD--SPRSMDT----EISEGGQ----GLSGGQRQL 626
Cdd:PRK09452 87 hVNTVFQSYALFPHmTVFEN--------------VAFGLRMQKTPAAeiTPRVMEAlrmvQLEEFAQrkphQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLD------TESEervLKALQshtRPTDIVLI-ATH-RPRLLSLANRLLIMRRGQVIAD 698
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDyklrkqMQNE---LKALQ---RKLGITFVfVTHdQEEALTMSDRIVVMRDGRIEQD 226
|
....*.
gi 2542252196 699 GPPAEV 704
Cdd:PRK09452 227 GTPREI 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
503-705 |
3.75e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.15 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIweLDPQVlGERI-----GYLPQDVHLF-KGTLKNN 576
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKV-DERLirqeaGMVFQQFYLFpHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 577 IMLAG----GINDARFLEVA-ELL---GLDRVAADSPrsmdteiSEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSAS 648
Cdd:PRK09493 98 VMFGPlrvrGASKEEAEKQArELLakvGLAERAHHYP-------SE----LSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 649 LDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
460-705 |
4.11e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 95.96 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 460 LALEGNRPegkvllvPETLPD--RLELEGVRFAY-PGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPA 536
Cdd:PLN03130 1221 LVIENNRP-------PPGWPSsgSIKFEDVVLRYrPELPPV-LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 537 EGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGG 616
Cdd:PLN03130 1293 RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAG 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 617 QGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAtHRPRLLSLANRLLIMRRGQVI 696
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA-HRLNTIIDCDRILVLDAGRVV 1451
|
....*....
gi 2542252196 697 ADGPPAEVI 705
Cdd:PLN03130 1452 EFDTPENLL 1460
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
508-704 |
5.58e-20 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 89.14 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADiweldPQVLGERIGYLPQDvHLFkgTLKNNIMLAGGINDAR 587
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQR-HEF--AWDFPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 588 flevAELLGLDR---------VAADSPRSMDTEISEGGQG-LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV 657
Cdd:TIGR03771 77 ----TGHIGWLRrpcvadfaaVRDALRRVGLTELADRPVGeLSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2542252196 658 LKALQSHTRPTDIVLIATHR-PRLLSLANRLLIMrRGQVIADGPPAEV 704
Cdd:TIGR03771 153 TELFIELAGAGTAILMTTHDlAQAMATCDRVVLL-NGRVIADGTPQQL 199
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
488-699 |
6.84e-20 |
|
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: 88.96 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 488 RFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWElDPQVLGERIGYLPQDVH 567
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 568 LFKG-TLKNNIMLAGGIN-------DARFLEVAELLGldrvaadsprsMDTEISEGGQGLSGGQRQLTAISRIFLARPRV 639
Cdd:cd03266 89 LYDRlTARENLEYFAGLYglkgdelTARLEELADRLG-----------MEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 640 WLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHR-PRLLSLANRLLIMRRGQVIADG 699
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
498-703 |
1.22e-19 |
|
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: 89.00 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 498 RLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGqvklggadiwelDPQVLGERIGYLPQDVHL-FKGTLKNN 576
Cdd:cd03237 14 TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG------------DIEIELDTVSYKPQYIKAdYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 577 IM--LAGGINDARF-LEVAELLGLDRVaadsprsMDTEISEggqgLSGGQRQLTAISrIFLARP-RVWLLDEPSASLDTE 652
Cdd:cd03237 82 LSsiTKDFYTHPYFkTEIAKPLQIEQI-------LDREVPE----LSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLDVE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 653 SE---ERVLKALQSHTRPTDIV-----LIATHrprllsLANRLLIMrrgqviaDGPPAE 703
Cdd:cd03237 150 QRlmaSKVIRRFAENNEKTAFVvehdiIMIDY------LADRLIVF-------EGEPSV 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
483-704 |
1.77e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYL 562
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQ--DVHLFKGTLKNNImlAGGINDARF---------LEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQLTAISR 631
Cdd:PRK13632 89 FQnpDNQFIGATVEDDI--AFGLENKKVppkkmkdiiDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 632 IFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIA-THRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
482-704 |
2.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.98 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPV---IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIwELDPQVLGE 557
Cdd:PRK13639 2 LETRDLKYSYPdGTEAlkgINFKAEK-----GEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 ---RIGYLPQ--DVHLFKGTLKNNIMLaGGINdarflevaelLGLDRVAADSpRSMDTEISEGGQG--------LSGGQR 624
Cdd:PRK13639 76 vrkTVGIVFQnpDDQLFAPTVEEDVAF-GPLN----------LGLSKEEVEK-RVKEALKAVGMEGfenkpphhLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 625 QLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSL-ANRLLIMRRGQVIADGPPAE 703
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKE 223
|
.
gi 2542252196 704 V 704
Cdd:PRK13639 224 V 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
504-678 |
2.90e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.39 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE--RIGYLPQdvhlFKGTL--KNNIML 579
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGllYLGHAPG----IKTTLsvLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 580 AGGINDARFLEVA----ELLGLDRVAADSprsmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEE 655
Cdd:cd03231 97 WHADHSDEQVEEAlarvGLNGFEDRPVAQ--------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|...
gi 2542252196 656 RVLKALQSHTRPTDIVLIATHRP 678
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQD 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
484-653 |
3.22e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 484 LEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlGERIGYLP 563
Cdd:COG0488 1 LENLSKSFGGRPLLD-DV-SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 564 QDVHLFKG-TLKNNIM-----------------LAGGINDARFLEVAEL----------------------LGLDRVAAD 603
Cdd:COG0488 68 QEPPLDDDlTVLDTVLdgdaelraleaeleeleAKLAEPDEDLERLAELqeefealggweaearaeeilsgLGFPEEDLD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2542252196 604 SPrsmdteISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTES 653
Cdd:COG0488 148 RP------VSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
164-454 |
5.31e-19 |
|
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: 87.95 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLrldkrP------RSLGSLAAQMNGLETVRTFFSSTIVFAMTDLP-----FGLMF---------IVFIAAIGG 303
Cdd:cd18555 81 FFEHLLKL-----PysffenRSSGDLLFRANSNVYIRQILSNQVISLIIDLLllviyLIYMLyysplltliVLLLGLLIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 304 MISTvylallpvslllgwLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGS-GWFFADlWRSITASMAAYSLKS 382
Cdd:cd18555 156 LLLL--------------LTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSeKNIYKK-WENLFKKQLKAFKKK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 383 KLISSLTTTTTATLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALE 454
Cdd:cd18555 221 ERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLE 292
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
514-704 |
5.56e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.16 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYKPAEGQVKLGG-------ADIWeLDPQvlGERIGYLPQDVHLF-----KGTLKNNImlaG 581
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIC-LPPE--KRRIGYVFQDARLFphykvRGNLRYGM---A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 GINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL 661
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2542252196 662 QSHTRPTDI-VLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK11144 172 ERLAREINIpILYVSHSlDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
489-705 |
9.13e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.54 E-value: 9.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 489 FAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHL 568
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 FKGTLKNNIMLagGINDARFLEVAELLGLDRVAADS---PRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEP 645
Cdd:PRK10789 401 FSDTVANNIAL--GRPDATQQEIEHVARLASVHDDIlrlPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 646 SASLDTESEERVLKALqSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK10789 479 LSAVDGRTEHQILHNL-RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
482-695 |
1.04e-18 |
|
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: 85.30 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPV-IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER-I 559
Cdd:TIGR01277 1 LALDKVRYEYEHLPMeFDLNVAD-----GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY---QRpV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKG-TLKNNIMLagGINDA---------RFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAI 629
Cdd:TIGR01277 73 SMLFQENNLFAHlTVRQNIGL--GLHPGlklnaeqqeKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQV 695
Cdd:TIGR01277 140 ARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRtLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
486-653 |
1.18e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.18 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 486 GVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLggadiwelDPqvlGERIGYLPQD 565
Cdd:PRK11819 11 RVSKVVPPKKQI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--------AP---GIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 566 VHLFKG-TLKNNIMLA-GGINDA--RFLEVAELLG---------------------------LDR---VAADSPR--SMD 609
Cdd:PRK11819 79 PQLDPEkTVRENVEEGvAEVKAAldRFNEIYAAYAepdadfdalaaeqgelqeiidaadawdLDSqleIAMDALRcpPWD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2542252196 610 TEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTES 653
Cdd:PRK11819 159 AKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
486-696 |
1.44e-18 |
|
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: 89.61 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 486 GVRFAYPGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGgadiweldpqvLGERIGYLPQD 565
Cdd:TIGR03719 9 RVSKVVPPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-----------PGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 566 VHL-FKGTLKNNIMLA-GGINDA--RFLEVAELLG---------------------------LDR---VAADSPR--SMD 609
Cdd:TIGR03719 77 PQLdPTKTVRENVEEGvAEIKDAldRFNEISAKYAepdadfdklaaeqaelqeiidaadawdLDSqleIAMDALRcpPWD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 610 TEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHtrpTDIVLIATH-RPRLLSLANRLL 688
Cdd:TIGR03719 157 ADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY---PGTVVAVTHdRYFLDNVAGWIL 229
|
....*...
gi 2542252196 689 IMRRGQVI 696
Cdd:TIGR03719 230 ELDRGRGI 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
499-677 |
2.20e-18 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 90.35 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 499 LQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKpAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIM 578
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 579 LAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVL 658
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170
....*....|....*....
gi 2542252196 659 KALQsHTRPTDIVLIATHR 677
Cdd:TIGR01271 1394 KTLK-QSFSNCTVILSEHR 1411
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
503-678 |
2.40e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE--RIGYLPqdvhlfkG--------- 571
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQP-------Gikteltale 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 572 TLKNNIMLAGGINDARFLEVAELLGLDRVaADSPRSMdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDT 651
Cdd:PRK13538 94 NLRFYQRLHGPGDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180
....*....|....*....|....*..
gi 2542252196 652 ESEERVLKALQSHTRPTDIVLIATHRP 678
Cdd:PRK13538 163 QGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
499-695 |
2.92e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 499 LQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQ---VLGERIGYLPQDVHLF-KGTLK 574
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHHLLmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 575 NNI----MLAGGINDARFLEVAEllGLDRVAA-DSPRSMDTEiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASL 649
Cdd:PRK10908 98 DNVaiplIIAGASGDDIRRRVSA--ALDKVGLlDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2542252196 650 DTESEERVLKALQSHTRPTDIVLIATHRPRLLSLAN-RLLIMRRGQV 695
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
484-705 |
4.30e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 484 LEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLP 563
Cdd:PRK10575 14 LRNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 564 QDVHLFKGTLKNNIMLAG-----------GINDARFLEVA-ELLGLDRVAAdspRSMDTeiseggqgLSGGQRQLTAISR 631
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGrypwhgalgrfGAADREKVEEAiSLVGLKPLAH---RLVDS--------LSGGERQRAWIAM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 632 IFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAT-HRprlLSLANR----LLIMRRGQVIADGPPAEVI 705
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVlHD---INMAARycdyLVALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
482-705 |
5.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWEL---------- 550
Cdd:PRK13644 2 IRLENVSYSYPdGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsklqgirklv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 551 -------DPQVLG----ERIGYLPQDVHLFKGTLKNNIMLAggindarfleVAELlGLDRVAADSPRSmdteiseggqgL 619
Cdd:PRK13644 80 givfqnpETQFVGrtveEDLAFGPENLCLPPIEIRKRVDRA----------LAEI-GLEKYRHRSPKT-----------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 620 SGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIaTHRPRLLSLANRLLIMRRGQVIAD 698
Cdd:PRK13644 138 SGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYI-THNLEELHDADRIIVMDRGKIVLE 216
|
....*..
gi 2542252196 699 GPPAEVI 705
Cdd:PRK13644 217 GEPENVL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
509-705 |
5.55e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHL-FKGTLKNNIMLA------- 580
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGrtphrsr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 581 -GGINDARFLEVAELLGLDRVAADSPRSMDTeiseggqgLSGGQRQltaisRIFLARP-----RVWLLDEPSASLDTESE 654
Cdd:PRK09536 109 fDTWTETDRAAVERAMERTGVAQFADRPVTS--------LSGGERQ-----RVLLARAlaqatPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 655 ERVLKALQSHTRPTDIVLIATHRprlLSLANR----LLIMRRGQVIADGPPAEVI 705
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIHD---LDLAARycdeLVLLADGRVRAAGPPADVL 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
481-705 |
1.00e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTPVIrlQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER-I 559
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVV--EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKG-TLKNNIMLAggindarfLEVAELLGLDRVAADSPRSMDT-EISE----GGQGLSGGQRQLTAISRIF 633
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAV--------LQIRDDLSAEQREDRANELMEEfHIEHlrdsMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQsHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIE-HLRDSGLgVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
509-699 |
1.41e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.20 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVlgeriGYLPQdvhlfkgtlknnimlAGGINDARF 588
Cdd:cd03220 48 GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----GFNPE---------------LTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 589 leVAELLGLDRvaaDSPRSMDTEI---SEGGQ-------GLSGGQR-QLT-AISRIFlaRPRVWLLDEPSASLDTESEER 656
Cdd:cd03220 108 --NGRLLGLSR---KEIDEKIDEIiefSELGDfidlpvkTYSSGMKaRLAfAIATAL--EPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2542252196 657 VLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADG 699
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
482-704 |
1.68e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.51 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPG-TPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgER-I 559
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIK-GI-DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFK----------GtLKNNIMLAGGInDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAI 629
Cdd:PRK11650 79 AMVFQNYALYPhmsvrenmayG-LKIRGMPKAEI-EERVAEAARILELEPLLDRKPRE-----------LSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESeeRV-----LKALQSHTRPTDIVLiaTH-RPRLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKL--RVqmrleIQRLHRRLKTTSLYV--THdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
.
gi 2542252196 704 V 704
Cdd:PRK11650 222 V 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
463-695 |
1.72e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.53 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 463 EGNRPEGKVLLVPETLPDRLELEgvrfaypgtPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVkl 542
Cdd:PTZ00243 649 ATPTSERSAKTPKMKTDDFFELE---------PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 543 ggadiweldpqvLGER-IGYLPQDVHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSG 621
Cdd:PTZ00243 718 ------------WAERsIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSG 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 622 GQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV-----LKALQSHTRptdivLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVveecfLGALAGKTR-----VLATHQVHVVPRADYVVALGDGRV 859
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
504-693 |
2.05e-17 |
|
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: 82.13 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQ--VLGERIGYLPQDvhlfkgTLKNNIMLAg 581
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmVVFQNYSLLPWL------TVRENIALA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 gindarflevaellgLDRVAADSPRSMDTEISEG---------------GQgLSGGQRQLTAISRIFLARPRVWLLDEPS 646
Cdd:TIGR01184 79 ---------------VDRVLPDLSKSERRAIVEEhialvglteaadkrpGQ-LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 647 ASLDT----ESEERVLKALQSHtRPTdiVLIATHR-PRLLSLANRLLIMRRG 693
Cdd:TIGR01184 143 GALDAltrgNLQEELMQIWEEH-RVT--VLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
508-703 |
2.20e-17 |
|
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: 81.65 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWElDPQVLGERIGYLPQDVHLFKG-TLKNNIMLAGGI--- 583
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENLYIHARLygv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 584 ----NDARFLEVAELLGLDRvAADSPRSMdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLK 659
Cdd:cd03265 104 pgaeRRERIDELLDFVGLLE-AADRLVKT----------YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542252196 660 ALQSHTRPTDI-VLIATH-RPRLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:cd03265 173 YIEKLKEEFGMtILLTTHyMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
508-705 |
2.29e-17 |
|
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: 82.69 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE----RIGYLPQDVHLF--KGTLKN---NIM 578
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLphRTVLENvafGLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 579 LAG---GINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLD----T 651
Cdd:cd03294 129 VQGvprAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 652 ESEERVLKaLQSHTRPTdIVLIaTHRP-RLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:cd03294 198 EMQDELLR-LQAELQKT-IVFI-THDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
483-705 |
2.40e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYL 562
Cdd:COG4604 3 EIKNVSKRYGGKVVLD-DV-SLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQDVHL-----------F------KGTLKNNIMLAggINDA-RFLEVAELlgldrvaADspRSMDTeiseggqgLSGGQR 624
Cdd:COG4604 81 RQENHInsrltvrelvaFgrfpysKGRLTAEDREI--IDEAiAYLDLEDL-------AD--RYLDE--------LSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 625 QltaisRIFLArpRVW-------LLDEPSASLDTESEERVLKALQSHTRPTD----IVL----IATHrprllsLANRLLI 689
Cdd:COG4604 142 Q-----RAFIA--MVLaqdtdyvLLDEPLNNLDMKHSVQMMKLLRRLADELGktvvIVLhdinFASC------YADHIVA 208
|
250
....*....|....*.
gi 2542252196 690 MRRGQVIADGPPAEVI 705
Cdd:COG4604 209 MKDGRVVAQGTPEEII 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
454-690 |
2.46e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.01 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 454 EMVNRLLALEGNRpEGKvllvpeTLPD--RLELEGVRFAYPgtpvIRLQVE-----TLAFGPGDRVVVMGPNGCGKSTLL 526
Cdd:PTZ00265 360 EIINRKPLVENND-DGK------KLKDikKIQFKNVRFHYD----TRKDVEiykdlNFTLTEGKTYAFVGESGCGKSTIL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 527 KLAAGLYKPAEGQVKLGGA-DIWELDPQVLGERIGYLPQDVHLFKGTLKNNI---------------------------- 577
Cdd:PTZ00265 429 KLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgndsqenk 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 --------MLAGGIN----------------------DARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLT 627
Cdd:PTZ00265 509 nkrnscraKCAGDLNdmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRI 588
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIATHRPRLLSLANRLLIM 690
Cdd:PTZ00265 589 SIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
503-702 |
3.36e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 81.54 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAG--LYKPAEGQVKLGGADIWELDPQvlgERIG---YL----PQDV-----HL 568
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPD---ERARaglFLafqyPEEIpgvsnLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 FKGTLKNNIMLAGGINDARFLEVAELLG-----LDRVAADSPRSMDTeiseggqGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:TIGR01978 97 FLRSALNARRSARGEEPLDLLDFEKLLKeklalLDMDEEFLNRSVNE-------GFSGGEKKRNEILQMALLEPKLAILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 644 EPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSL--ANRLLIMRRGQVIADGPPA 702
Cdd:TIGR01978 170 EIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYikPDYVHVLLDGRIVKSGDVE 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
504-703 |
3.59e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.62 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADI----------------WELDPQV-LGERIGYlpqdv 566
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiqqrdicmvfqsYALFPHMsLGENVGY----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 567 hlfkgTLKnniMLaGGINDARFLEVAELLGLDRVAADSPRSMDTeiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPS 646
Cdd:PRK11432 102 -----GLK---ML-GVPKEERKQRVKEALELVDLAGFEDRYVDQ--------ISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 647 ASLDT---ESEERVLKALQSHTRPTDivLIATH-RPRLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:PRK11432 165 SNLDAnlrRSMREKIRELQQQFNITS--LYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
481-697 |
3.63e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPG--TPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGAdiweldpQVLG-- 556
Cdd:COG4525 3 MLTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-------PVTGpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 -ERiGYLPQDVHLFKG-TLKNNIMLA---GGINDARFLEVAE----LLGLDRVAADSprsmdteISEggqgLSGGQRQLT 627
Cdd:COG4525 76 aDR-GVVFQKDALLPWlNVLDNVAFGlrlRGVPKAERRARAEellaLVGLADFARRR-------IWQ----LSGGMRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEER----VLKALQSHTRPtdiVLIATHR-PRLLSLANRLLIM--RRGQVIA 697
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQmqelLLDVWQRTGKG---VFLITHSvEEALFLATRLVVMspGPGRIVE 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
503-699 |
3.69e-17 |
|
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: 81.22 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWEldpqvlgERIGYLPQDVHLF--KGTLKNNI--- 577
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-------RRKKFLRRIGVVFgqKTQLWWDLpvi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 ----MLAG--GINDARFL----EVAELLGLDRVaadsprsMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSA 647
Cdd:cd03267 114 dsfyLLAAiyDLPPARFKkrldELSELLDLEEL-------LDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 648 SLDTESEERVLKALQSHTRPTDI-VLIATHRPR-LLSLANRLLIMRRGQVIADG 699
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTtVLLTSHYMKdIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
482-701 |
4.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.09 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIG 560
Cdd:PRK13647 5 IEVEDLHFRYKdGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDV--HLFKGTLKN-------NIMLAGGINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISR 631
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 632 IFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRL-LSLANRLLIMRRGQVIADGPP 701
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
489-694 |
4.51e-17 |
|
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: 82.21 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 489 FAYPGTPV---IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlgeRIGYLPQD 565
Cdd:cd03291 45 LCLVGAPVlknINLKIEK-----GEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 566 VHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEP 645
Cdd:cd03291 107 SWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 646 SASLDTESEERVL-----KALQSHTRptdivLIATHRPRLLSLANRLLIMRRGQ 694
Cdd:cd03291 187 FGYLDVFTEKEIFescvcKLMANKTR-----ILVTSKMEHLKKADKILILHEGS 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
498-704 |
4.87e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 498 RLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYkPAEGQVKLGGADIWELDPQVLGERIGYLPQ-DVHLFkgtlknn 576
Cdd:COG4138 11 RLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQqQSPPF------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 577 IM-------------LAGGINDARFLEVAELLGLDrvaaDS-PRSMDTeiseggqgLSGGQRQLTAISRIFLarpRVW-- 640
Cdd:COG4138 83 AMpvfqylalhqpagASSEAVEQLLAQLAEALGLE----DKlSRPLTQ--------LSGGEWQRVRLAAVLL---QVWpt 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 641 --------LLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4138 148 inpegqllLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
508-699 |
4.94e-17 |
|
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: 80.34 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVlgERIGYLpQDVHLFKG--TLKNNIMLAG---G 582
Cdd:cd03268 25 KGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGAL-IEAPGFYPnlTARENLRLLArllG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 583 INDARFLEVAELLGLDRVAADSPRsmdteiseggqGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQ 662
Cdd:cd03268 102 IRKKRIDEVLDVVGLKDSAKKKVK-----------GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2542252196 663 SHTRPTDIVLIATHrprLLS----LANRLLIMRRGQVIADG 699
Cdd:cd03268 171 SLRDQGITVLISSH---LLSeiqkVADRIGIINKGKLIEEG 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
496-705 |
7.20e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 496 VIRLQVETLAFGPGDRVV---------------VMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIG 560
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVaenltveipdghftaIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDvhlfkGTLKNNIMLAGGINDARFLE--------------VAELLGLDRVAADSPRSMDTeiseggqgLSGGQRQL 626
Cdd:PRK10253 85 LLAQN-----ATTPGDITVQELVARGRYPHqplftrwrkedeeaVTKAMQATGITHLADQSVDT--------LSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRP--RLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlnQACRYASHLIALREGKIVAQGAPKEI 231
|
.
gi 2542252196 705 I 705
Cdd:PRK10253 232 V 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
482-701 |
7.94e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 7.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR-LqveTLAFGPGDRVVVMGPNGCGKSTLLKLAAGL--YKPAEGQVKLGGADIWELDPQvlgER 558
Cdd:COG0396 1 LEIKNLHVSVEGKEILKgV---NLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPD---ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 ----IGYLPQDVHLFKG-TLKNNIMLA------GGINDARFL----EVAELLGLDRVAADspRSMDTeiseggqGLSGGQ 623
Cdd:COG0396 75 aragIFLAFQYPVEIPGvSVSNFLRTAlnarrgEELSAREFLkllkEKMKELGLDEDFLD--RYVNE-------GFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 624 RQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIaTHRPRLLSL--ANRLLIMRRGQVIADGP 700
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILII-THYQRILDYikPDFVHVLVDGRIVKSGG 224
|
.
gi 2542252196 701 P 701
Cdd:COG0396 225 K 225
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
164-454 |
1.44e-16 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 81.05 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQ 243
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 244 LYEHLLDLRLDK-RPRSLGSLAAQMNGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLGWL 322
Cdd:cd18779 81 FLEHLLRLPYRFfQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 323 AQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVGYV 402
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 403 AAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALE 454
Cdd:cd18779 241 VLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLE 292
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
503-705 |
3.63e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqvlGER-IGYLPQDVHLFKG-TLKNNIMLa 580
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRpVSMLFQENNLFSHlTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 581 gGINDARFLEVAELLGLDRVAadSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKA 660
Cdd:PRK10771 95 -GLNPGLKLNAAQREKLHAIA--RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2542252196 661 LQS--HTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK10771 172 VSQvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
484-650 |
3.75e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.84 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 484 LEGVRFAYPGTPV---IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGerIG 560
Cdd:PRK11000 6 LRNVTKAYGDVVIskdINLDIHE-----GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLFKG-TLKNN----IMLAGGIN---DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRI 632
Cdd:PRK11000 79 MVFQSYALYPHlSVAENmsfgLKLAGAKKeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
|
170
....*....|....*...
gi 2542252196 633 FLARPRVWLLDEPSASLD 650
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLD 165
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
503-695 |
4.59e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE----RIGYLPQDVHLFK--GTLKNN 576
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQFHHLLPdfTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 577 IM--LAGGINDA----RFLEVAELLGLDRVAADSPrsmdteiSEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLD 650
Cdd:PRK11629 109 AMplLIGKKKPAeinsRALEMLAAVGLEHRANHRP-------SE----LSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542252196 651 TESEERVLKALQS-HTRPTDIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:PRK11629 178 ARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
489-693 |
5.99e-16 |
|
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: 82.27 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 489 FAYPGTPV---IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpqvlgeRIGYLPQD 565
Cdd:TIGR01271 434 FSLYVTPVlknISFKLEK-----GQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 566 VHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEP 645
Cdd:TIGR01271 496 SWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 646 SASLD--TESE--ERVL-KALQSHTRptdivLIATHRPRLLSLANRLLIMRRG 693
Cdd:TIGR01271 576 FTHLDvvTEKEifESCLcKLMSNKTR-----ILVTSKLEHLKKADKILLLHEG 623
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
509-693 |
7.92e-16 |
|
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: 76.99 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER----IGYLPQDVHLFKGTLKNNIMLAGGIN 584
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENITFGSPFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 DARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTE-----SEERVLK 659
Cdd:cd03290 107 KQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILK 186
|
170 180 190
....*....|....*....|....*....|....
gi 2542252196 660 ALQSHTRptdIVLIATHRPRLLSLANRLLIMRRG 693
Cdd:cd03290 187 FLQDDKR---TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
514-704 |
8.43e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYKPAEGQVKLG----GADIWELDPQV------------LGERIGYLPQ--DVHLFKGTLKN 575
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 NIM---LAGGINDARFLEVA----ELLGLDrvaadsprsmDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSAS 648
Cdd:PRK13631 137 DIMfgpVALGVKKSEAKKLAkfylNKMGLD----------DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 649 LDTESEERVLKALQSHTRPTDIVLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
482-676 |
1.20e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIweLDPQ----VLGE 557
Cdd:PRK11248 2 LQISHLYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGPGaergVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 RIGYLP-QDVhlfKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMdteiseggQGLSGGQRQLTAISRIFLAR 636
Cdd:PRK11248 78 NEGLLPwRNV---QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYI--------WQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2542252196 637 PRVWLLDEPSASLDTESEER----VLKALQSHTRPtdiVLIATH 676
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQmqtlLLKLWQETGKQ---VLLITH 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
504-704 |
1.33e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGeRIGYLP--QDVHLFKG-TLKNNIM-- 578
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-RMGVVRtfQHVRLFREmTVIENLLva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 579 ---------LAGGINDARFLEvAELLGLDRVAADSPRSMDTEIS--EGGQGLSGGQRQLtAISRIFLARPRVWLLDEPSA 647
Cdd:PRK11300 105 qhqqlktglFSGLLKTPAFRR-AESEALDRAATWLERVGLLEHAnrQAGNLAYGQQRRL-EIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 648 SLDTEsEERVLKALQSHTRP---TDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK11300 183 GLNPK-ETKELDELIAELRNehnVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
482-704 |
1.40e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVklggadIWELDPQ-------- 553
Cdd:PRK13638 2 LATSDLWFRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV------LWQGKPLdyskrgll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 554 VLGERIGYLPQD--VHLFKGTLKNNIMLAggindARFLEVAELLGLDRV-----AADSPRSMDTEIseggQGLSGGQRQL 626
Cdd:PRK13638 74 ALRQQVATVFQDpeQQIFYTDIDSDIAFS-----LRNLGVPEAEITRRVdealtLVDAQHFRHQPI----QCLSHGQKKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
482-705 |
1.44e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 81.36 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIG 560
Cdd:PTZ00243 1309 LVFEGVQMRYrEGLPLV-LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHLFKGTLKNNImlagginDArFLEVA--------ELLGL-DRVAADSpRSMDTEISEGGQGLSGGQRQLTAISR 631
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNV-------DP-FLEASsaevwaalELVGLrERVASES-EGIDSRVLEGGSNYSVGQRQLMCMAR 1458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 632 IFLARPRVW-LLDEPSAS----LDTESEERVLKALQSHTrptdIVLIAtHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PTZ00243 1459 ALLKKGSGFiLMDEATANidpaLDRQIQATVMSAFSAYT----VITIA-HRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
482-705 |
1.50e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.58 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGV--RFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE-- 557
Cdd:COG1135 2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 -RIGYLPQDVHLFKG-TLKNNIMLA---GGIN----DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTA 628
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENVALPleiAGVPkaeiRKRVAELLELVGLSDKADAYPSQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTD--IVLIaTH-----RprllSLANRLLIMRRGQVIADGPP 701
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGltIVLI-THemdvvR----RICDRVAVLENGRIVEQGPV 225
|
....
gi 2542252196 702 AEVI 705
Cdd:COG1135 226 LDVF 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
480-677 |
1.60e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 480 DRLELEGVRFAYPGTPVIRLQvetlafgpgdrvvvmGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADI------WELDPQ 553
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLK---------------GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 554 VLGERIGYLPQDvhlfkgTLKNNIMLagginDARF----LEVAELLGLDRVA--ADSPRSMdteiseggqgLSGGQRQLT 627
Cdd:PRK13540 78 FVGHRSGINPYL------TLRENCLY-----DIHFspgaVGITELCRLFSLEhlIDYPCGL----------LSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHR 677
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
511-704 |
1.71e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.54 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 511 RVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQ--DVHLFKGTLKNNIMLaGGIN---- 584
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSPTVEQDIAF-GPINlgld 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 ----DARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKA 660
Cdd:PRK13652 111 eetvAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542252196 661 LQSHTRPTDI-VLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13652 180 LNDLPETYGMtVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
482-704 |
1.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPG-TPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIG 560
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQ--DVHLFKGTLKNNImlAGGINDaRFLEVAELLGLDRVAADSPRSMDTEISEGGQgLSGGQRQLTAISRIFLARPR 638
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDV--AFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLtVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
482-704 |
1.97e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQ--------VKLGGADIWELDpq 553
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 554 vlgERIGYLPQ--DVHLFKGTLKNNImlAGGINDaRFLEVAELLGLDRVAADSPRSMDTEISEGgQGLSGGQRQLTAISR 631
Cdd:PRK13640 84 ---EKVGIVFQnpDNQFVGATVGDDV--AFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 632 IFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIA-THRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
503-696 |
2.02e-15 |
|
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: 76.16 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGL---YKPAEGQVKLGGAdiwELDPQVLGERIGYLPQDVHLFKG-----TLK 574
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGltvreTLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 575 NNIMLAGG--INDARFLEVAELLGLDRVAadsprsmDTEIseGG---QGLSGGQRQLTAISRIFLARPRVWLLDEPSASL 649
Cdd:cd03234 104 YTAILRLPrkSSDAIRKKRVEDVLLRDLA-------LTRI--GGnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2542252196 650 DTESEERVLKALQSHTRPTDIVLIATHRPR--LLSLANRLLIMRRGQVI 696
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRsdLFRLFDRILLLSSGEIV 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
503-705 |
2.10e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVlgeriGYLPQdvhLfkgTLKNNIMLAGG 582
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELGA-----GFHPE---L---TGRENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 583 IN-------DARFLEVAELLGLDRvAADSP-RSmdteiseggqgLSGGQRqltaiSRIFLA-----RPRVWLLDEPSASL 649
Cdd:COG1134 115 LLglsrkeiDEKFDEIVEFAELGD-FIDQPvKT-----------YSSGMR-----ARLAFAvatavDPDILLVDEVLAVG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 650 DTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG1134 178 DAAFQKKCLARIRELRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
509-704 |
2.79e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlGERIGYLPQDVHLFKG-TLKNNI-----ML--- 579
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDNIafgltVLprr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 580 ---AGGINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEE- 655
Cdd:PRK10851 106 erpNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKe 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 656 --RVLKALQSHTRPTDIVLiaTH-RPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK10851 175 lrRWLRQLHEELKFTSVFV--THdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
482-703 |
2.97e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAfgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPqVLGERIG- 560
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YL-PQDVHLFKG-TLKNNIM--LAGGINDARFLE--VAEL---LGLDRVAAdsprsmDTEISEggqglsggqRQLTAISR 631
Cdd:PRK15439 89 YLvPQEPLLFPNlSVKENILfgLPKRQASMQKMKqlLAALgcqLDLDSSAG------SLEVAD---------RQIVEILR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 632 IFLARPRVWLLDEPSASL---DTESEERVLKALQShtRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:PRK15439 154 GLMRDSRILILDEPTASLtpaETERLFSRIRELLA--QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
508-676 |
3.03e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.36 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVV-MGPNGCGKSTLLK-------LAAGLYkpAEGQVKLGGADIW--ELDPQVLGERIGYLPQDVHLFKGTLKNNI 577
Cdd:PRK14243 34 PKNQITAfIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYapDVDPVEVRRRIGMVFQKPNPFPKSIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 578 MLAGGINDARflevaelLGLDRVAADSPR------SMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDT 651
Cdd:PRK14243 112 AYGARINGYK-------GDMDELVERSLRqaalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180
....*....|....*....|....*
gi 2542252196 652 ESEERVLKALQSHTRPTDIVlIATH 676
Cdd:PRK14243 185 ISTLRIEELMHELKEQYTII-IVTH 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
503-705 |
3.12e-15 |
|
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: 79.99 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGAdiweldpqvlgerIGYLPQDVHLFKGTLKNNIMLAGG 582
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 583 INDARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLK--- 659
Cdd:TIGR00957 725 LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvi 804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2542252196 660 ----ALQSHTRptdivLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR00957 805 gpegVLKNKTR-----ILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
482-699 |
3.43e-15 |
|
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: 75.01 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYpgTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDpqvlGERIGY 561
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVHLFKgtlKNNIMlaggiNDARFLevAELLGLDRvaADSPRSMDT-----EISEGG----QGLSGGQRQLTAISRI 632
Cdd:cd03269 75 LPEERGLYP---KMKVI-----DQLVYL--AQLKGLKK--EEARRRIDEwlerlELSEYAnkrvEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 633 FLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLS-LANRLLIMRRGQVIADG 699
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEeLCDRVLLLNKGRAVLYG 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
432-702 |
3.50e-15 |
|
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: 79.07 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 432 VIGPIAQSVGILVQWQHVREALEMVNRL-LALEGNRPEGKVLLVPETLPD--RLELEGVRFAYP---GTPVIRLQVETLA 505
Cdd:COG4615 275 LRGPLSQLVGALPTLSRANVALRKIEELeLALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPgedGDEGFTLGPIDLT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 506 FGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFkgtlKNNIMLAGGIND 585
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADP 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 586 ARFLEVAELLGLDR-VAADSPRSMDTEiseggqgLSGGQRQ----LTAisrifLA--RPrVWLLDEPSASLDTESEER-- 656
Cdd:COG4615 431 ARARELLERLELDHkVSVEDGRFSTTD-------LSQGQRKrlalLVA-----LLedRP-ILVFDEWAADQDPEFRRVfy 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 657 -----VLKAlQSHTrptdiVLIATHRPRLLSLANRLLIMRRGQVIADGPPA 702
Cdd:COG4615 498 tellpELKA-RGKT-----VIAISHDDRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
432-698 |
4.03e-15 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 78.85 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 432 VIGPIAQSVGIL-------VQWQHVREALEMVNRLLA-LEGNRPEGKVLLVPETLPDRLELEGVRFAYP---GTPVIRLQ 500
Cdd:TIGR01194 280 IKGPLEMLVSALpilaqaqIACQRLADFGERFNEPEPeLELSDADNVLLLAHDKSVDSIELKDVHMNPKapeGSEGFALG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 501 VETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLA 580
Cdd:TIGR01194 360 PIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYRDLFSAIFADFHLFDDLIGPDEGEH 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 581 GGINDA-RFLEVAELlgldrvaADSPRSMDTEISEgGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTeSEERVL- 658
Cdd:TIGR01194 440 ASLDNAqQYLQRLEI-------ADKVKIEDGGFST-TTALSTGQQKRLALICAWLEDRPILLFDEWAADQDP-AFKRFFy 510
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2542252196 659 -KALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIAD 698
Cdd:TIGR01194 511 eELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCIVKD 551
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
479-704 |
4.26e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 479 PDRLELEGVRFAYPGtpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQV---L 555
Cdd:COG3845 3 PPALELRGITKRFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 GerIGYLPQDVHLFKG-TLKNNIMLA-----GGIND-----ARFLEVAELLGL----DRVAADsprsmdteiseggqgLS 620
Cdd:COG3845 81 G--IGMVHQHFMLVPNlTVAENIVLGleptkGGRLDrkaarARIRELSERYGLdvdpDAKVED---------------LS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 621 GGQRQLTAISRIFLARPRVWLLDEPSASL-DTESEE--RVLKAL--QSHTrptdIVLIaTHRPR-LLSLANRLLIMRRGQ 694
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLtPQEADElfEILRRLaaEGKS----IIFI-THKLReVMAIADRVTVLRRGK 218
|
250
....*....|
gi 2542252196 695 VIADGPPAEV 704
Cdd:COG3845 219 VVGTVDTAET 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
503-703 |
8.09e-15 |
|
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: 75.23 E-value: 8.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQ-----------VLGERIGYL-PQDV--HL 568
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafrrdvqlVFQDSPSAVnPRMTvrQI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 FKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADS-PRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSA 647
Cdd:TIGR02769 111 IGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKlPRQ-----------LSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 648 SLDTESEERVLKALQSHTRPTDIV-LIATHRPRLL-SLANRLLIMRRGQVIADGPPAE 703
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQ 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
482-704 |
8.50e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.64 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIRLQVETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIwelDPQV---- 554
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKGLDNISFEleEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI---TPETgnkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 ---LGERIGYLPQ--DVHLFKGTLKNNIMLAG---GINDARFLEVA----ELLGL-DRVAADSPRSmdteiseggqgLSG 621
Cdd:PRK13641 80 lkkLRKKVSLVFQfpEAQLFENTVLKDVEFGPknfGFSEDEAKEKAlkwlKKVGLsEDLISKSPFE-----------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 622 GQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLS-LANRLLIMRRGQVIADGP 700
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHAS 228
|
....
gi 2542252196 701 PAEV 704
Cdd:PRK13641 229 PKEI 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
509-676 |
8.67e-15 |
|
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: 77.90 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGqvklggadiwELDPQVlgeRIGYLPQDV-HLFKGTLKNNIM--LAGGIND 585
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDEDL---KISYKPQYIsPDYDGTVEEFLRsaNTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 586 ARF-LEVAELLGLDRVaadsprsMDTEISEggqgLSGGQRQLTAISrIFLARP-RVWLLDEPSASLDteSEERVL--KAL 661
Cdd:COG1245 433 SYYkTEIIKPLGLEKL-------LDKNVKD----LSGGELQRVAIA-ACLSRDaDLYLLDEPSAHLD--VEQRLAvaKAI 498
|
170
....*....|....*.
gi 2542252196 662 QSHTRPTDI-VLIATH 676
Cdd:COG1245 499 RRFAENRGKtAMVVDH 514
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
503-704 |
1.13e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP-------------QVLGERIGYLPQDVHLF 569
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 570 KG-TLKNNIMLAG----GINDARFLEVAELLgLDRVAadsprsmdteISEGGQG-----LSGGQRQLTAISRIFLARPRV 639
Cdd:PRK10619 105 SHmTVLENVMEAPiqvlGLSKQEARERAVKY-LAKVG----------IDERAQGkypvhLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 640 WLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
504-704 |
1.62e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADI---WELDPQ-----VLGERIGYLPQDVHLF--KGTL 573
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQLRQHVGFVFQNFNLFphRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 574 KNNI----MLAGGINDARFLEVAELL---GLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPS 646
Cdd:PRK11264 104 ENIIegpvIVKGEPKEEATARARELLakvGLAGKETSYPRR-----------LSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 647 ASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
482-695 |
1.73e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR-LQVETLAfgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDpqvlgERIG 560
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNqLDLHIPA---GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-----EDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 561 YLPQDVHL--FKGTLKN-NIMLAGGINDARfLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARP 637
Cdd:PRK11247 85 LMFQDARLlpWKKVIDNvGLGLKGQWRDAA-LQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 638 RVWLLDEPSASLDT----ESEERVLKALQSHTRptdIVLIATHR-PRLLSLANRLLIMRRGQV 695
Cdd:PRK11247 153 GLLLLDEPLGALDAltriEMQDLIESLWQQHGF---TVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
482-699 |
3.53e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGG------ADIWELDPQVL 555
Cdd:COG4161 3 IQLKNINCFYGSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 GERIGYLPQDVHLFKG-TLKNNIMLAG----GIN--DARF--LEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQL 626
Cdd:COG4161 81 RQKVGMVFQQYNLWPHlTVMENLIEAPckvlGLSkeQAREkaMKLLARLRLTDKADRFP-----------LHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 627 TAISRIFLARPRVWLLDEPSASLDTESEERVLKALQ--SHTRPTDIvlIATHRPRLL-SLANRLLIMRRGQVIADG 699
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRelSQTGITQV--IVTHEVEFArKVASQVVYMEKGRIIEQG 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
482-704 |
3.78e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.52 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIRLQVE--TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIW----ELDPQV 554
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRALYdvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 LGERIGYLPQ--DVHLFKGTLKNNIMLaGGIN------DARFL--EVAELLGLDR-VAADSPRSmdteiseggqgLSGGQ 623
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICF-GPMNfgvseeDAKQKarEMIELVGLPEeLLARSPFE-----------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 624 RQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL-QSHTRPTDIVLIATHR-PRLLSLANRLLIMRRGQVIADGPP 701
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFyKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVFLQGTP 230
|
...
gi 2542252196 702 AEV 704
Cdd:PRK13634 231 REI 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
482-705 |
4.13e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirlqVETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLgERI 559
Cdd:PRK13537 8 IDFRNVEKRYGDKLV----VDGLSFHvqRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHLFKG-TLKNNIMLAG---GINDARFLE-VAELLGLDRVAADSprsmDTEISEggqgLSGGQRQLTAISRIFL 634
Cdd:PRK13537 83 GVVPQFDNLDPDfTVRENLLVFGryfGLSAAAARAlVPPLLEFAKLENKA----DAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 635 ARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATH-RPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHfMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
503-704 |
4.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGG----ADIWEL-DPQVLGERIGYLPQ--DVHLFKGTLKN 575
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkEVKRLRKEIGLVFQfpEYQLFQETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 NIMLA----GGINDARFLEVAELLGLDRVAADSPRSMDTEiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDT 651
Cdd:PRK13645 111 DIAFGpvnlGENKQEAYKKVPELLKLVQLPEDYVKRSPFE-------LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 652 ESEERVLKALQ--SHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13645 184 KGEEDFINLFErlNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
508-703 |
4.97e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPA---EGQVKLGGADIwelDPQVLGERIGYLPQDvHLFKGTL--KNNIM---- 578
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQD-DLFIPTLtvREHLMfqah 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 579 ------LAGGINDARFLEVAELLGLDRVAadsprsmDTEISEGGQ--GLSGGQRQLTAISRIFLARPRVWLLDEPSASLD 650
Cdd:TIGR00955 126 lrmprrVTKKEKRERVDEVLQALGLRKCA-------NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 651 TESEERVLKALQSHTRPTDIVLIATHRP--RLLSLANRLLIMRRGQVIADGPPAE 703
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPssELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
509-660 |
6.21e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKlggadiWELdpqvlgeRIGYLPQDV-HLFKGTLKNNIMLAGGINDAR 587
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PEL-------KISYKPQYIkPDYDGTVEDLLRSITDDLGSS 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 588 FL--EVAELLGLDRVaadsprsMDTEISEggqgLSGGQRQLTAISrIFLARP-RVWLLDEPSASLDteSEERVLKA 660
Cdd:PRK13409 432 YYksEIIKPLQLERL-------LDKNVKD----LSGGELQRVAIA-ACLSRDaDLYLLDEPSAHLD--VEQRLAVA 493
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
482-705 |
6.42e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.71 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirlqVETLAF--GPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIwELDPQVLGERI 559
Cdd:PRK13536 42 IDLAGVSKSYGDKAV----VNGLSFtvASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-PARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVHL-FKGTLKNNIMLAG---GINdARFLE--VAELLGLDRVAadspRSMDTEISEggqgLSGGQRQLTAISRIF 633
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLVFGryfGMS-TREIEavIPSLLEFARLE----SKADARVSD----LSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATH-RPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
480-704 |
6.73e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 480 DRLELEGVRFAYPGTPVIRlqVETLAFGPGDRVVVMGPNGCGKSTLLKL---AAGLYKPA--EGQVKLGGADIWELDPQV 554
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLD--GVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 LGERIGYLPQdvhlfkgtLKNNIMlaggiNDARFLEVAELLGLDRVAaDSPRSMDTEISEG-----------------GQ 617
Cdd:PRK14247 80 LRRRVQMVFQ--------IPNPIP-----NLSIFENVALGLKLNRLV-KSKKELQERVRWAlekaqlwdevkdrldapAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 618 GLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIA 697
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 2542252196 698 DGPPAEV 704
Cdd:PRK14247 226 WGPTREV 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
475-683 |
7.75e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 475 PETLPDRLELEGVRFAYPGTPVirlqvetlaFGP-------GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadi 547
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPV---------FGPldfhvdaGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 548 welDPQVLGERIGYLPQDVHLfkGTLKNNImlaGGINDARFLevAELLGldRVAADSPRSMDTEISEGG------QGLSG 621
Cdd:PRK13543 73 ---KTATRGDRSRFMAYLGHL--PGLKADL---STLENLHFL--CGLHG--RRAKQMPGSALAIVGLAGyedtlvRQLSA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 622 GQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATH--------RPRLLSL 683
Cdd:PRK13543 141 GQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHgayaappvRTRMLTL 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
499-695 |
1.05e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.96 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 499 LQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQvlgERIGYLPQDVhlfkGTLKNNIM 578
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE---ARAKLRAKHV----GFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 579 LAGGINDarfLEVAELLGL-----DRVAADSPRSMDTEISEGGQ------GLSGGQRQLTAISRIFLARPRVWLLDEPSA 647
Cdd:PRK10584 99 LIPTLNA---LENVELPALlrgesSRQSRNGAKALLEQLGLGKRldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2542252196 648 SLDTESEERVLKALQSHTRPTDIVLI-ATHRPRLLSLANRLLIMRRGQV 695
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLIlVTHDLQLAARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
482-704 |
1.06e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.46 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPV-------IRLQVETlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQ 553
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFasralfdIDLEVKK-----GSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 554 V----LGERIGYLPQ--DVHLFKGTLKNNIMLAG---GINDARFLEVA----ELLGLDR-VAADSPRSmdteiseggqgL 619
Cdd:PRK13643 77 KeikpVRKKVGVVFQfpESQLFEETVLKDVAFGPqnfGIPKEKAEKIAaeklEMVGLADeFWEKSPFE-----------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 620 SGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATH-RPRLLSLANRLLIMRRGQVIAD 698
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISC 225
|
....*.
gi 2542252196 699 GPPAEV 704
Cdd:PRK13643 226 GTPSDV 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
482-704 |
1.40e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYP-GTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGA--DIWELDPQVLGER 558
Cdd:PRK13636 6 LKVEELNYNYSdGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVhlfkgtlKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMD-TEIS----EGGQGLSGGQRQLTAISRIF 633
Cdd:PRK13636 84 VGMVFQDP-------DNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKrTGIEhlkdKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSL-ANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLtIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
503-704 |
1.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGAD------IWEL-----------DPQVLG----ERIGY 561
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenLWDIrnkagmvfqnpDNQIVAtiveEDVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDVhlfkGTLKNNIMlaggindARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWL 641
Cdd:PRK13633 110 GPENL----GIPPEEIR-------ERVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 642 LDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGItIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
498-704 |
2.34e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 498 RLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYkPAEGQVKLGGADIWELDPQVLGERIGYLPQDVH---------- 567
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTppfampvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 568 --LFKGTLKNNIMLAGGINdarflEVAELLGLDrvaaDS-PRSMdteiseggQGLSGGQRQLTAISRIFLarpRVW---- 640
Cdd:PRK03695 90 ltLHQPDKTRTEAVASALN-----EVAEALGLD----DKlGRSV--------NQLSGGEWQRVRLAAVVL---QVWpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 641 ------LLDEPSASLDTESE---ERVLKALQSHTRPtdiVLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK03695 150 pagqllLLDEPMNSLDVAQQaalDRLLSELCQQGIA---VVMSSHDlNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-704 |
2.41e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYKPAEG-----QVKLGGADIWEL-DPQVLGERIGYLPQDVHLFKGTLKNNImLAG------ 581
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNV-LAGvrahkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 -------GINDARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESE 654
Cdd:PRK14271 131 vprkefrGVAQARLTEVGLWDAVKDRLSDSPFR-----------LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2542252196 655 ERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK14271 200 EKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
513-699 |
2.63e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 513 VVMGPNGCGKSTLLKLAAG--LYKPAEGQVKLGGADIWELDPQvlgERigylpqdVHLfkgtlknNIMLA-------GGI 583
Cdd:CHL00131 37 AIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE---ER-------AHL-------GIFLAfqypieiPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 584 NDARFLEVA-----ELLGLDRVaadSPRSMDTEISEG---------------GQGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:CHL00131 100 SNADFLRLAynskrKFQGLPEL---DPLEFLEIINEKlklvgmdpsflsrnvNEGFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 644 EPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLS--LANRLLIMRRGQVIADG 699
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDyiKPDYVHVMQNGKIIKTG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
509-696 |
3.01e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADI--WElDPQVLGERIGYLPQDVHLF-KGTLKNNIMLAGGIND 585
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdWQ-TAKIMREAVAIVPEGRRVFsRMTVEENLAMGGFFAE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 586 ARFLEVAellgLDRVAADSPRSMDTEISEGGQgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-H 664
Cdd:PRK11614 110 RDQFQER----IKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQlR 184
|
170 180 190
....*....|....*....|....*....|..
gi 2542252196 665 TRPTDIVLIATHRPRLLSLANRLLIMRRGQVI 696
Cdd:PRK11614 185 EQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-704 |
3.64e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.08 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGA------DIWELDPQVLGERIGYLPQDVHLFKG-TLKNNI---MLAGGI 583
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHlSIYDNIaypLKSHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 584 NDARflEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS 663
Cdd:PRK14246 121 KEKR--EIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2542252196 664 HTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK14246 199 LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
503-650 |
4.40e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVklggadiwELDPQVlgeRIGYLPQDVHL---FKGTLKNNIML 579
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKL---RIGYVPQKLYLdttLPLTVNRFLRL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 580 AGGINDARFLEVaellgLDRVAA----DSPRsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLD 650
Cdd:PRK09544 93 RPGTKKEDILPA-----LKRVQAghliDAPM----------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
483-704 |
4.99e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGV--RFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE--- 557
Cdd:PRK11153 3 ELKNIskVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 RIGYLPQDVHLFKG-TLKNNIMLA---GGIN----DARFLEVAELLGL----DRVAADsprsmdteiseggqgLSGGQRQ 625
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVALPlelAGTPkaeiKARVTELLELVGLsdkaDRYPAQ---------------LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTD--IVLIaTHRPRLL-SLANRLLIMRRGQVIADGPPA 702
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGltIVLI-THEMDVVkRICDRVAVIDAGRLVEQGTVS 226
|
..
gi 2542252196 703 EV 704
Cdd:PRK11153 227 EV 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
495-704 |
5.62e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 495 PVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGER-IGYLPQDV------- 566
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELsvidelt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 567 ---HLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVaaDSPRSMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:PRK09700 97 vleNLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRV--GLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 644 EPSASLdTESEERVLKALQSHTRP--TDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK09700 171 EPTSSL-TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
475-676 |
5.73e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.30 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 475 PETLPDRLELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLK-------LAAGLYkpAEGQVKLGGADI 547
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALK-DI-NLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 548 W--ELDPQVLGERIGYLPQDVHLFKGTLKNNImLAG----GINDARFLE--VAELL---GL-----DRVaaDSPrsmdte 611
Cdd:COG1117 81 YdpDVDVVELRRRVGMVFQKPNPFPKSIYDNV-AYGlrlhGIKSKSELDeiVEESLrkaALwdevkDRL--KKS------ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 612 isegGQGLSGGQRQLTAISRIfLA-RPRVWLLDEPSASLDTESEERV------LKalQSHTrptdiVLIATH 676
Cdd:COG1117 152 ----ALGLSGGQQQRLCIARA-LAvEPEVLLMDEPTSALDPISTAKIeelileLK--KDYT-----IVIVTH 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
494-693 |
6.26e-13 |
|
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: 72.09 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 494 TPVIRLQVETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGL--------YKPAEGqvklggadiweldpqvlgeRIGYLP 563
Cdd:TIGR00954 461 TPNGDVLIESLSFEvpSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKG-------------------KLFYVP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 564 QDVHLFKGTLKNNI--------MLAGGINDARFLEVAELLGLDRVAAdspRSMDTE-ISEGGQGLSGGQRQLTAISRIFL 634
Cdd:TIGR00954 522 QRPYMTLGTLRDQIiypdssedMKRRGLSDKDLEQILDNVQLTHILE---REGGWSaVQDWMDVLSGGEKQRIAMARLFY 598
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 635 ARPRVWLLDEPSASLDTESEERvlkaLQSHTRPTDIVLIA-THRPRLLSLANRLLIM-RRG 693
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEGY----MYRLCREFGITLFSvSHRKSLWKYHEYLLYMdGRG 655
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
170-454 |
6.94e-13 |
|
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: 69.89 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 170 VGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHLL 249
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 250 DLRLDKRPR-SLGSLAAQMNG-LETVRTFFSSTIVFAMTDLpfglmfIVFIAAIGGMIST-------------VYLALLp 314
Cdd:cd07346 84 RLSLSFFDRnRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDV------LTLIGALVILFYLnwkltlvallllpLYVLIL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 315 vslllgWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTA 394
Cdd:cd07346 157 ------RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 395 TLSTVGYVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPIAQSVGILVQWQHVREALE 454
Cdd:cd07346 231 LLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
503-705 |
8.33e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.83 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE----RIGYLPQDVHLfkgtLKNNIM 578
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFAL----MPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 579 LAggiNDARFLEVAELLGLDR--VAADSPRSMDTEISEGG--QGLSGGQRQLTAISRIFLARPRVWLLDEPSASLD---- 650
Cdd:PRK10070 124 LD---NTAFGMELAGINAEERreKALDALRQVGLENYAHSypDELSGGMRQRVGLARALAINPDILLMDEAFSALDplir 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 651 TESEERVLKALQSHTRptDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK10070 201 TEMQDELVKLQAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
503-703 |
1.06e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDpqvlGERIGYLPQDVHL-FKGT--------- 572
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN----RAQRKAFRRDIQMvFQDSisavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 573 --------LKNNIMLAGGINDARFLEVAELLGLDRVAADS-PrsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:PRK10419 108 vreiirepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKrP-----------PQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 644 EPSASLD---TESEERVLKALQsHTRPTDIVLIaTHRPRLLS-LANRLLIMRRGQVIADGPPAE 703
Cdd:PRK10419 177 EAVSNLDlvlQAGVIRLLKKLQ-QQFGTACLFI-THDLRLVErFCQRVMVMDNGQIVETQPVGD 238
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
516-704 |
1.14e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 516 GPNGCGKSTLLKLAAGLYKPAEGQVKLGGAdiwELDPQVLgERIGYLPQDVHLFKgtlKNNIMlaggiNDARFLevAELL 595
Cdd:COG4152 34 GPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDR-RRIGYLPEERGLYP---KMKVG-----EQLVYL--ARLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 596 GLDRvaADSPRSMDT-----EISEGG----QGLSGGQRQ----LTAIsrifLARPRVWLLDEPSASLDTESEERVLKALQ 662
Cdd:COG4152 100 GLSK--AEAKRRADEwlerlGLGDRAnkkvEELSKGNQQkvqlIAAL----LHDPELLILDEPFSGLDPVNVELLKDVIR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542252196 663 SHTRPTDIVLIATHRprlLS----LANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4152 174 ELAAKGTTVIFSSHQ---MElveeLCDRIVIINKGRKVLSGSVDEI 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
503-699 |
1.43e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGG------ADIWELDPQVLGERIGYLPQDVHLFKG-TLKN 575
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHlTVQQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 NIMLAG----GIND----ARFLEVAELLGLDRVAADSPrsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSA 647
Cdd:PRK11124 102 NLIEAPcrvlGLSKdqalARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 648 SLDTESEERVLKALQ--SHTRPTDIvlIATHRPRLL-SLANRLLIMRRGQVIADG 699
Cdd:PRK11124 171 ALDPEITAQIVSIIRelAETGITQV--IVTHEVEVArKTASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
504-704 |
1.61e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.65 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIW------ELDPqvLGERIGYLPQ--DVHLFKGTL-- 573
Cdd:PRK13646 28 TEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRP--VRKRIGMVFQfpESQLFEDTVer 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 574 ------KNNIMLAGGINDARFLEVAELlGLDR-VAADSPRSMdteiseggqglSGGQRQLTAISRIFLARPRVWLLDEPS 646
Cdd:PRK13646 106 eiifgpKNFKMNLDEVKNYAHRLLMDL-GFSRdVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 647 ASLDTESEERV---LKALQSHTRPTdIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13646 174 AGLDPQSKRQVmrlLKSLQTDENKT-IILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
482-697 |
1.69e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGtpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiwelDPQV------- 554
Cdd:PRK11288 5 LSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEMRfasttaa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 LGERIGYLPQDVHLF-KGTLKNNIML-----AGGINDARFLEVAELLGLDRVAAD-SPrsmDTEISEggqgLSGGQRQLT 627
Cdd:PRK11288 77 LAAGVAIIYQELHLVpEMTVAENLYLgqlphKGGIVNRRLLNYEAREQLEHLGVDiDP---DTPLKY----LSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 628 AISRIFLARPRVWLLDEPSASL---DTESEERVLKALQSHTRptdIVLIATHR-PRLLSLANRLLIMRRGQVIA 697
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGR---VILYVSHRmEEIFALCDAITVFKDGRYVA 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
503-705 |
1.83e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAG-LYKPAE-------GQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLK 574
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAFSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 575 NNIMLAGGINDARflEVAELLGLDRVAADSPRSM---DTEISEGGQGLSGGQRQLTAISRIF---------LARPRVWLL 642
Cdd:PRK13547 101 REIVLLGRYPHAR--RAGALTHRDGEIAWQALALagaTALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 643 DEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLSL-ANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK13547 179 DEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
482-696 |
2.11e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.31 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKlggadiWeldpqvlGE- 557
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKnlnLLLE-----AGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------W-------SEn 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 -RIGYLPQD-VHLFKgtlknnimlaggiNDarfLEVAELLGLDRVAAD---SPRSM-------DTEISEGGQGLSGGQRQ 625
Cdd:PRK15064 382 aNIGYYAQDhAYDFE-------------ND---LTLFDWMSQWRQEGDdeqAVRGTlgrllfsQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 626 LTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHtrPTDIVLIATHRPRLLSLANRLLIMRRGQVI 696
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-704 |
2.15e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.56 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYK-----PAEGQVKLGGADIW--ELDPQVLGERIGYLPQDVHLFKG-TLKNNIMLAGGIND 585
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYspDVDPIEVRREVGMVFQYPNPFPHlTIYDNVAIGVKLNG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 586 --ARFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS 663
Cdd:PRK14267 115 lvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2542252196 664 HTRPTDIVLIaTHRPRLLS-LANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK14267 195 LKKEYTIVLV-THSPAQAArVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
503-705 |
3.78e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQV----------KLGGADIWELDPQVLG--------------ER 558
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLVIQktrfkkikkikeirRR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQ--DVHLFKGTLKNNIM---LAGGINDARFLEVA----ELLGLDRVAAD-SPRsmdteiseggqGLSGGQRQLTA 628
Cdd:PRK13651 107 VGVVFQfaEYQLFEQTIEKDIIfgpVSMGVSKEEAKKRAakyiELVGLDESYLQrSPF-----------ELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 629 ISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHR-PRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
515-701 |
3.85e-12 |
|
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: 70.04 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 515 MGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIwELDPQVLGERIGYLPQDVHLFKG-TLKNNIMLAGGINdARFLEVAE 593
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLK-GRSWEEAQ 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 594 LlGLDRVAADSprSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLI 673
Cdd:TIGR01257 1040 L-EMEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMS 1116
|
170 180
....*....|....*....|....*...
gi 2542252196 674 ATHRPRLLSLANRLLIMRRGQVIADGPP 701
Cdd:TIGR01257 1117 THHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
164-382 |
6.16e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 67.10 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 164 KRWLLEVGVATVVVNLLAVATSLFsMQ-VYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQ 242
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLY-LQlVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 243 QLYEHLLDLRLD---KrpRSLGSLAAQMNGLETVRTFFSSTIVFAMTD-----LPFGLMFI--VFIAAIGGMISTVYLAL 312
Cdd:cd18567 80 NLFRHLLRLPLSyfeK--RHLGDIVSRFGSLDEIQQTLTTGFVEALLDglmaiLTLVMMFLysPKLALIVLAAVALYALL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 313 LpvslllgWLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKS 382
Cdd:cd18567 158 R-------LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRL 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
499-699 |
7.58e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 499 LQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLY---KPAEGQVKLGGADIW---ELDPQVLGER--IGYLPQDVHLF- 569
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregRLARDIRKSRanTGYIFQQFNLVn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 570 KGTLKNNIMLaGGINDARFLEVA-----------ELLGLDRVAadsprsMDTEISEGGQGLSGGQRQLTAISRIFLARPR 638
Cdd:PRK09984 100 RLSVLENVLI-GALGSTPFWRTCfswftreqkqrALQALTRVG------MVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 639 VWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAT-HR-PRLLSLANRLLIMRRGQVIADG 699
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQvDYALRYCERIVALRQGHVFYDG 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
509-704 |
8.51e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAE-GQVKLGGAdiweldpqvlgerIGYLPQDVHLFKGTLKNNIMLAGGINDAR 587
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 588 FLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRP 667
Cdd:PLN03232 710 YWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK 789
|
170 180 190
....*....|....*....|....*....|....*..
gi 2542252196 668 TDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PLN03232 790 GKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
519-705 |
1.05e-11 |
|
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: 66.62 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 519 GCGKSTLLKLAAGLYKP---AEGQVKLGGADIWELDP----QVLGERIGYLPQD-------VHLFKGTLKNNIMLAGGIN 584
Cdd:COG0444 41 GSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrKIRGREIQMIFQDpmtslnpVMTVGDQIAEPLRIHGGLS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 ----DARFLEVAELLGLD---RVAADSPrsmdteisegGQgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV 657
Cdd:COG0444 121 kaeaRERAIELLERVGLPdpeRRLDRYP----------HE-LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 658 LKALQSHTRPTD--IVLIaTHRprlLSL----ANRLLIMRRGQVIADGPPAEVI 705
Cdd:COG0444 190 LNLLKDLQRELGlaILFI-THD---LGVvaeiADRVAVMYAGRIVEEGPVEELF 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
482-704 |
1.64e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGY 561
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 562 LPQDV-HLFKGT---------LKNNIMlaggINDARFLEVAELLG----LDRvAADSPrsmdteiseggQGLSGGQRQLT 627
Cdd:PRK13648 88 VFQNPdNQFVGSivkydvafgLENHAV----PYDEMHRRVSEALKqvdmLER-ADYEP-----------NALSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIA-THRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
482-703 |
1.73e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGtpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP---QVLGer 558
Cdd:PRK10762 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 559 IGYLPQDVHLFKG-TLKNNIMLA-------GGINDARFLEVAELLgLDRVaaDSPRSMDTEISEggqgLSGGQRQLTAIS 630
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGrefvnrfGRIDWKKMYAEADKL-LARL--NLRFSSDKLVGE----LSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 631 RIFLARPRVWLLDEPSASL-DTESEE--RVLKALQSHTRptDIVLIaTHRPR-LLSLANRLLIMRRGQVIADGPPAE 703
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALtDTETESlfRVIRELKSQGR--GIVYI-SHRLKeIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
481-695 |
1.86e-11 |
|
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: 63.22 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRFAYPGTPVirlqveTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP-QVLGERI 559
Cdd:cd03215 4 VLEVRGLSVKGAVRDV------SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQDVH---LFKG-TLKNNIMLaggindarflevaellgldrvaadsprsmdteisegGQGLSGGQRQLTAISRIFLA 635
Cdd:cd03215 78 AYVPEDRKregLVLDlSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542252196 636 RPRVWLLDEPSASLDTESEERVLKALQSHT-RPTDIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
435-694 |
2.17e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 435 PIAQSVGILVQWQHVREALEMVNRLlALEGNRPEgkvLLVPETLPD--RLELEGVRFAYPGtpvirlqvETLAFGP---- 508
Cdd:PRK10522 278 PLLSAVGALPTLLSAQVAFNKLNKL-ALAPYKAE---FPRPQAFPDwqTLELRNVTFAYQD--------NGFSVGPinlt 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 ---GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAggiND 585
Cdd:PRK10522 346 ikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPA---NP 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 586 ARFLEVAELLGL-DRVAADSPRSMDTEiseggqgLSGGQRQLTAIsRIFLARPR-VWLLDEPSASLDTESEERVLKALQS 663
Cdd:PRK10522 423 ALVEKWLERLKMaHKLELEDGRISNLK-------LSKGQKKRLAL-LLALAEERdILLLDEWAADQDPHFRREFYQVLLP 494
|
250 260 270
....*....|....*....|....*....|..
gi 2542252196 664 HTRPTDIVLIA-THRPRLLSLANRLLIMRRGQ 694
Cdd:PRK10522 495 LLQEMGKTIFAiSHDDHYFIHADRLLEMRNGQ 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
508-699 |
2.37e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGErigylPQDVHLFK----------------- 570
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE-----AERRRLLRtewgfvhqhprdglrmq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 571 ----GTLKNNIMLAGGINDARFLEVAeLLGLDRVAADSPRsmdteISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPS 646
Cdd:PRK11701 106 vsagGNIGERLMAVGARHYGDIRATA-GDWLERVEIDAAR-----IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 647 ASLDTESEERVLKALQSHTRPTDI-VLIATHR---PRLlsLANRLLIMRRGQVIADG 699
Cdd:PRK11701 180 GGLDVSVQARLLDLLRGLVRELGLaVVIVTHDlavARL--LAHRLLVMKQGRVVESG 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
538-677 |
2.79e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 538 GQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLagGINDARFLEV---AELLGLDRVAADSPRSMDTEISE 614
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKF--GKEDATREDVkraCKFAAIDEFIESLPNKYDTNVGP 1354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 615 GGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTD--IVLIAtHR 677
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADktIITIA-HR 1418
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
508-704 |
2.92e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 64.44 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIwELDPQVLGERIGYLPQDV------------------HLf 569
Cdd:COG4598 33 KGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDRDGELVPADRRQLqrirtrlgmvfqsfnlwsHM- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 570 kgTLKNNIMLAG----GINDARFLEVAELLgLDRVAADSPRsmDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEP 645
Cdd:COG4598 111 --TVLENVIEAPvhvlGRPKAEAIERAEAL-LAKVGLADKR--DAYPAH----LSGGQQQRAAIARALAMEPEVMLFDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 646 SASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL-SLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4598 182 TSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFArDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
519-704 |
3.27e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 519 GCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP-QVLGERIGYLPQDVH---LFKG-TLKNNIMLA--------GGIND 585
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPEDRKgegLVLDlSIRENITLAsldrlsrgGLLDR 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 586 ARFLEVAEllgldRVAAD---SPRSMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLD--TESE-ERVLK 659
Cdd:COG1129 368 RRERALAE-----EYIKRlriKTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiYRLIR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2542252196 660 ALqshtrpTD----IVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG1129 439 EL------AAegkaVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
509-704 |
4.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQV-----KLGGADIWELDpqvlgERIGYLPQ--DVHLFKGTLKNNImlAG 581
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEENVWDIR-----HKIGMVFQnpDNQFVGATVEDDV--AF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 GIND---------ARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTE 652
Cdd:PRK13650 106 GLENkgipheemkERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 653 SEERVLKALQSHTRPTDIVLIA-THRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISiTHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
503-676 |
5.22e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.64 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLA--AGLYKP---AEGQVKLGGADIW--ELDPQVLGERIGYLPQDVHLFKGTLKN 575
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYspRTDTVDLRKEIGMVFQQPNPFPMSIYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 NIMLA---GGINDARFLEVAELLGLdrVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTE 652
Cdd:PRK14239 105 NVVYGlrlKGIKDKQVLDEAVEKSL--KGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPI 182
|
170 180
....*....|....*....|....*...
gi 2542252196 653 S----EERVLKALQSHTrptdiVLIATH 676
Cdd:PRK14239 183 SagkiEETLLGLKDDYT-----MLLVTR 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
503-658 |
5.38e-11 |
|
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: 63.22 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKL----GGADIWELDP-QVLGER---IGYLPQdvhlfkgtlk 574
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPrEILALRrrtIGYVSQ---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 575 nnimlaggindarFLE----------VAELL---GLDR-VAADSPRSMDT--EISEGGQGL-----SGGQRQLTAISRIF 633
Cdd:COG4778 101 -------------FLRviprvsaldvVAEPLlerGVDReEARARARELLArlNLPERLWDLppatfSGGEQQRVNIARGF 167
|
170 180
....*....|....*....|....*
gi 2542252196 634 LARPRVWLLDEPSASLDTESEERVL 658
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVV 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
482-705 |
5.95e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVirLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGL--YKPAEGQV------------------- 540
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 541 -----KLGG------ADIWELDPQV---LGERIGYLPQDVHLFKG--TLKNNIMLAggindarfLEVAELLGLDRV--AA 602
Cdd:TIGR03269 79 gepcpVCGGtlepeeVDFWNLSDKLrrrIRKRIAIMLQRTFALYGddTVLDNVLEA--------LEEIGYEGKEAVgrAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 603 D--SPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAT-HRPR 679
Cdd:TIGR03269 151 DliEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPE 230
|
250 260
....*....|....*....|....*..
gi 2542252196 680 LLS-LANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR03269 231 VIEdLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
504-682 |
7.79e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQvklGGADIWELDpqvlgerigyLPQDVhlfkgTLKNNIMLAGGI 583
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA---GCVDVPDNQ----------FGREA-----SLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 584 NDArflevAELLGldRVAADSPRSMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS 663
Cdd:COG2401 113 KDA-----VELLN--AVGLSDAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170 180
....*....|....*....|
gi 2542252196 664 HTRPTDI-VLIATHRPRLLS 682
Cdd:COG2401 182 LARRAGItLVVATHHYDVID 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
514-705 |
9.51e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.82 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIW--ELDPQVLG-----ERIGYLPQDVHLF-KGTLKNNIMLAGGIN- 584
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWvdMTKPGPDGrgrakRYIGILHQEYDLYpHRTVLDNLTEAIGLEl 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 -----DARFLEVAELLGLDRVAADS--PRSMDTeiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV 657
Cdd:TIGR03269 395 pdelaRMKAVITLKMVGFDEEKAEEilDKYPDE--------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDV 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2542252196 658 LKA-LQSHTRPTDIVLIATH-RPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:TIGR03269 467 THSiLKAREEMEQTFIIVSHdMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
507-696 |
9.98e-11 |
|
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: 61.89 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 507 GPGDRVVVMGPNGCGKSTLLKLAAGL---YKPAEGQVKLGGADIWELDPQVLGERIgYLPQ-DVHLFKGTLKNNImlagg 582
Cdd:cd03233 31 KPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSEeDVHFPTLTVRETL----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 583 indaRFleVAELLGLDRVaadsprsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQ 662
Cdd:cd03233 105 ----DF--ALRCKGNEFV----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2542252196 663 SHTRPTDIVLIAT---HRPRLLSLANRLLIMRRGQVI 696
Cdd:cd03233 163 TMADVLKTTTFVSlyqASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-704 |
1.61e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 497 IRLQVETLAfGPGDRVV-----------VMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQ-VLGERIGYLPQ 564
Cdd:PRK10762 256 VRLKVDNLS-GPGVNDVsftlrkgeilgVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 565 DVhlfKG-------TLKNNIML---------AGGIN-DARFLEVAELLGLDRVaaDSPrSMDTEISEggqgLSGGQRQLT 627
Cdd:PRK10762 335 DR---KRdglvlgmSVKENMSLtalryfsraGGSLKhADEQQAVSDFIRLFNI--KTP-SMEQAIGL----LSGGNQQKV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKAL-QSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLInQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQA 482
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
508-699 |
1.80e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKP-AEGQVKLGGadiweldpqvlgeRIGYLPQDVHLFKGTLKNNIMLAGGINDA 586
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG-------------TVAYVPQVSWIFNATVRDNILFGSPFDPE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 587 RFLEVAELLGLDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVL-KALQSHT 665
Cdd:PLN03130 709 RYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDEL 788
|
170 180 190
....*....|....*....|....*....|....
gi 2542252196 666 RPTDIVLIaTHRPRLLSLANRLLIMRRGQVIADG 699
Cdd:PLN03130 789 RGKTRVLV-TNQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
508-700 |
2.88e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLgERIG-----------YLP--------QDVHl 568
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFA-RRIGvvfgqrsqlwwDLPaidsfrllKAIY- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 fkgtlknnimlagGINDARFL----EVAELLGLDRVaadsprsMDTEISEggqgLSGGQR---QLTAisrIFLARPRVWL 641
Cdd:COG4586 125 -------------RIPDAEYKkrldELVELLDLGEL-------LDTPVRQ----LSLGQRmrcELAA---ALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 642 LDEPSASLDTESEERV---LKALQSHTRPTdiVLIATHRPR-LLSLANRLLIMRRGQVIADGP 700
Cdd:COG4586 178 LDEPTIGLDVVSKEAIrefLKEYNRERGTT--ILLTSHDMDdIEALCDRVIVIDHGRIIYDGS 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
482-704 |
4.26e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIR--LQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWEL----DPQV 554
Cdd:PRK13649 3 INLQNVSYTYqAGTPFEGraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 LGERIGYLPQ--DVHLFKGTLKNNIMLaGGINDARFLEVAELLGLDRVAAdsprsmdTEISEGGQG-----LSGGQRQLT 627
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAF-GPQNFGVSQEEAEALAREKLAL-------VGISESLFEknpfeLSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 628 AISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
493-700 |
4.93e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.33 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 493 GTPVIRLQV---ETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPA--EGQVKLGGADiwelDPQVLGERI-GYLPQ-D 565
Cdd:PLN03140 887 GVTEDRLQLlreVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP----KKQETFARIsGYCEQnD 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 566 VHLFKGTLKNNIMLA---------GGINDARFL-EVAELLGLDRVAaDSPRSMdteisEGGQGLSGGQRQLTAISRIFLA 635
Cdd:PLN03140 963 IHSPQVTVRESLIYSaflrlpkevSKEEKMMFVdEVMELVELDNLK-DAIVGL-----PGVTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 636 RPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPR--LLSLANRLLIMRR-GQVIADGP 700
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSidIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-676 |
6.99e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.44 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 514 VMGPNGCGKSTLLKLAAGLYK-----PAEGQVKLGGADIWE--LDPQVLGERIGYLPQDVHLFKGTLKNNImlAGGINDA 586
Cdd:PRK14258 38 IIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFPMSVYDNV--AYGVKIV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 587 RFLEVAELLGLDRVA---ADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS 663
Cdd:PRK14258 116 GWRPKLEIDDIVESAlkdADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQS 195
|
170
....*....|....
gi 2542252196 664 HTRPTDI-VLIATH 676
Cdd:PRK14258 196 LRLRSELtMVIVSH 209
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
505-693 |
8.65e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 505 AFGPGDRVVVMGPNGCGKSTLLKLAAGlYKPA---EGQVKLGGADIweldPQVLGERIGYLPQ-DVHLfkgtlknnimla 580
Cdd:cd03232 29 YVKPGTLTALMGESGAGKTTLLDVLAG-RKTAgviTGEILINGRPL----DKNFQRSTGYVEQqDVHS------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 581 ggindaRFLEVAELLgldrvaadsprsmdtEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEE---RV 657
Cdd:cd03232 92 ------PNLTVREAL---------------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYnivRF 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 2542252196 658 LKALQSHTRPtdiVLIATHRP--RLLSLANRLLIMRRG 693
Cdd:cd03232 151 LKKLADSGQA---ILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
503-679 |
9.07e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.73 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGerigYLPQDVHL-FKGTLKNNIMLAG 581
Cdd:PRK13541 20 SITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT----YIGHNLGLkLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 GINDArflevAELLgldrVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL 661
Cdd:PRK13541 96 EIYNS-----AETL----YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
170
....*....|....*...
gi 2542252196 662 QSHTRPTDIVLIATHRPR 679
Cdd:PRK13541 167 VMKANSGGIVLLSSHLES 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
458-700 |
1.20e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 458 RLLALEgnrPEGKVLLVPETLPDRLELEGVRFAYPGTPVI-------RLQVETLAFG--PGDRVVVMGPNGCGKST---- 524
Cdd:PRK15134 255 KLLNSE---PSGDPVPLPEPASPLLDVEQLQVAFPIRKGIlkrtvdhNVVVKNISFTlrPGETLGLVGESGSGKSTtgla 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 525 LLKLAAglykpAEGQVKLGGADIWELDPQVL---GERIGYLPQDVH------------LFKGTLKNNIMLAGGINDARFL 589
Cdd:PRK15134 332 LLRLIN-----SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnprlnvlqiIEEGLRVHQPTLSAAQREQQVI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 590 EVAELLGLDrvaADSPRSMDTEiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERV---LKALQSHTR 666
Cdd:PRK15134 407 AVMEEVGLD---PETRHRYPAE-------FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIlalLKSLQQKHQ 476
|
250 260 270
....*....|....*....|....*....|....*
gi 2542252196 667 PTDIVLiaTHRPRLL-SLANRLLIMRRGQVIADGP 700
Cdd:PRK15134 477 LAYLFI--SHDLHVVrALCHQVIVLRQGEVVEQGD 509
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
489-661 |
1.29e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 489 FAYPGTPVIrlqVETLAFGPG--DRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKlggadiweLDPQVlgeRIGYLPQDv 566
Cdd:PLN03073 516 FGYPGGPLL---FKNLNFGIDldSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKV---RMAVFSQH- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 567 HLFKGTLKNNIMLA-----GGINDARFLEVAELLGLDRVAADSPrsMDTeiseggqgLSGGQRQLTAISRIFLARPRVWL 641
Cdd:PLN03073 581 HVDGLDLSSNPLLYmmrcfPGVPEQKLRAHLGSFGVTGNLALQP--MYT--------LSGGQKSRVAFAKITFKKPHILL 650
|
170 180
....*....|....*....|
gi 2542252196 642 LDEPSASLDTESEERVLKAL 661
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGL 670
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
488-676 |
1.36e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 488 RFAYPGTPVIRlqvetlafgPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGqvKLGGADIW----------ELD---PQV 554
Cdd:cd03236 14 SFKLHRLPVPR---------EGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWdeildefrgsELQnyfTKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 555 LGERIGYL--PQDVHLFKGTLKNNIMLAGGINDAR--FLEVAELLGLDRVaadsprsMDTEISEggqgLSGGQRQLTAIS 630
Cdd:cd03236 83 LEGDVKVIvkPQYVDLIPKAVKGKVGELLKKKDERgkLDELVDQLELRHV-------LDRNIDQ----LSGGELQRVAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2542252196 631 RIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATH 676
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
482-664 |
2.03e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGtpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYkPA---EGQVklggadIWELDPQVLG-- 556
Cdd:PRK13549 6 LEMKNITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEI------IFEGEELQASni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ---ER--IGYLPQDVHLFKG-TLKNNIML-----AGGIND--ARFLEVAELLGLDRVAADsprsMDTEISEggqgLSGGQ 623
Cdd:PRK13549 77 rdtERagIAIIHQELALVKElSVLENIFLgneitPGGIMDydAMYLRAQKLLAQLKLDIN----PATPVGN----LGLGQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2542252196 624 RQLTAISRIFLARPRVWLLDEPSASLdTESEERVL----KALQSH 664
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASL-TESETAVLldiiRDLKAH 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
467-650 |
2.47e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 467 PEGKVLLVPETLPD---RLELEGVRFAYPGTPVI-RL--QVEtlafgPGDRVVVMGPNGCGKSTLLKLAAG--------- 531
Cdd:PRK10938 243 PEPDEPSARHALPAnepRIVLNNGVVSYNDRPILhNLswQVN-----PGEHWQIVGPNGAGKSTLLSLITGdhpqgysnd 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 532 --LYkpaeGQVKLGGADIWELDpqvlgERIGYLPQDVHL---FKGTLKNNImLAG-----GINDA-----RFL--EVAEL 594
Cdd:PRK10938 318 ltLF----GRRRGSGETIWDIK-----KHIGYVSSSLHLdyrVSTSVRNVI-LSGffdsiGIYQAvsdrqQKLaqQWLDI 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 595 LGLDRVAADSPRsmdteiseggQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLD 650
Cdd:PRK10938 388 LGIDKRTADAPF----------HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-704 |
3.62e-09 |
|
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: 59.70 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 458 RLLALEgnrPEGKVLLVPETLPDRLELEGVRFAYP------GTPVIRLQ-VE--TLAFGPGDRVVVMGPNGCGKSTL--- 525
Cdd:COG4172 255 KLLAAE---PRGDPRPVPPDAPPLLEARDLKVWFPikrglfRRTVGHVKaVDgvSLTLRRGETLGLVGESGSGKSTLgla 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 526 -LKLAaglykPAEGQVKLGGADIWEL-----------------DP-----------QVLGErigylPQDVHlfkgtlknN 576
Cdd:COG4172 332 lLRLI-----PSEGEIRFDGQDLDGLsrralrplrrrmqvvfqDPfgslsprmtvgQIIAE-----GLRVH--------G 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 577 IMLAGGINDARfleVAELL---GLDrvaadsPRSMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTES 653
Cdd:COG4172 394 PGLSAAERRAR---VAEALeevGLD------PAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 654 EERV---LKALQ----------SHtrptDIVLIAthrprllSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG4172 461 QAQIldlLRDLQrehglaylfiSH----DLAVVR-------ALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
502-650 |
5.01e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 58.59 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 502 ETLAfgpgdrvvVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE---RIGYLPQD----------Vhl 568
Cdd:COG4608 45 ETLG--------LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDpyaslnprmtV-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 569 fkGT-----LKNNIMLAGGINDARFLEVAELLGLDRVAADS-PRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLL 642
Cdd:COG4608 115 --GDiiaepLRIHGLASKAERRERVAELLELVGLRPEHADRyPHE-----------FSGGQRQRIGIARALALNPKLIVC 181
|
....*...
gi 2542252196 643 DEPSASLD 650
Cdd:COG4608 182 DEPVSALD 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
508-700 |
9.85e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAA----GLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDVHLFKGTLKNNIMLAG-- 581
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAArc 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 --------GINDARFLE-----VAELLGLD-----RVAADSPRsmdteiseggqGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:TIGR00956 166 ktpqnrpdGVSREEYAKhiadvYMATYGLShtrntKVGNDFVR-----------GVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 644 EPSASLDTESEERVLKALQSHTRPTD-IVLIATHR--PRLLSLANRLLIMRRGQVIADGP 700
Cdd:TIGR00956 235 NATRGLDSATALEFIRALKTSANILDtTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFGP 294
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
475-695 |
9.96e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 475 PETLPDRL-ELEGVRFAYpGTPVIrLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGadiweldpq 553
Cdd:PRK10636 305 PESLPNPLlKMEKVSAGY-GDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK--------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 554 vlGERIGYLPQdvhlfkgtlknnimlaggiNDARFLEVAE--LLGLDRVAadsPRSMDTEISE--GGQG----------- 618
Cdd:PRK10636 374 --GIKLGYFAQ-------------------HQLEFLRADEspLQHLARLA---PQELEQKLRDylGGFGfqgdkvteetr 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 619 -LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPtdIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:PRK10636 430 rFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA--LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
508-705 |
1.06e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPA--EGQVKLGGAdiwELDPQVLgERIGYLPQDVHLFKG-TLKNNIMLAGgin 584
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR---KPTKQIL-KRTGFVTQDDILYPHlTVRETLVFCS--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 darflevaeLLGLDRVAA--DSPRSMDTEISEGG--------------QGLSGGQRQLTAISRIFLARPRVWLLDEPSAS 648
Cdd:PLN03211 166 ---------LLRLPKSLTkqEKILVAESVISELGltkcentiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 649 LDTESEERVLKALQSHTRPTDIVLIATHRP--RLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPssRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
509-700 |
1.13e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 509 GDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLgerIGYLPQ--DVHLFKGTLKNNIMLAGGINDA 586
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQseEVDWSFPVLVEDVVMMGRYGHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 587 RFLEVAELLGLDRVAADSPRSMDTEISEGGQG-LSGGQRQltaisRIFLARP-----RVWLLDEPSASLDTESEERVLKA 660
Cdd:PRK15056 110 GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGeLSGGQKK-----RVFLARAiaqqgQVILLDEPFTGVDVKTEARIISL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2542252196 661 LQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGP 700
Cdd:PRK15056 185 LRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
508-696 |
1.36e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGaDI----WELDP-------------QVLGERIGYL-------- 562
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLivarLQQDPprnvegtvydfvaEGIEEQAEYLkryhdish 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 -----PQDVHLFK-GTLKNNIMLAGGIN-DARFLEVAELLGLDrvaadsprsMDTEISEggqgLSGGQRQLTAISRIFLA 635
Cdd:PRK11147 107 lvetdPSEKNLNElAKLQEQLDHHNLWQlENRINEVLAQLGLD---------PDAALSS----LSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 636 RPRVWLLDEPSASLDTES---EERVLKALQShtrptDIVLIATHRPRLLSLANRLLIMRRGQVI 696
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETiewLEGFLKTFQG-----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-672 |
3.05e-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: 54.12 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 496 VIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVklggadiwELDpqvlGERIGYLPQDVHlfkgtlkn 575
Cdd:cd03222 12 VFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND--------EWD----GITPVYKPQYID-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 nimlaggindarflevaellgldrvaadsprsmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESE- 654
Cdd:cd03222 72 -------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRl 108
|
170 180
....*....|....*....|
gi 2542252196 655 --ERVLKALQSHTRPTDIVL 672
Cdd:cd03222 109 naARAIRRLSEEGKKTALVV 128
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
482-681 |
4.80e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIR---LQVEtlafgPGDRVVVMGPNGCGKSTLLKLAAGL--YKPAEGQVKLGGADIWELDPQvlg 556
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRglnLEVR-----PGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 557 ERIG---YLPQDVHLFKGTLKNNIMLAGGINDARflEVAELLGLDRVaaDSPRSMDTEIS-----------EGGQGLSGG 622
Cdd:PRK09580 74 DRAGegiFMAFQYPVEIPGVSNQFFLQTALNAVR--SYRGQEPLDRF--DFQDLMEEKIAllkmpedlltrSVNVGFSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 623 QRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLL 681
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRIL 208
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
506-692 |
5.66e-08 |
|
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: 52.75 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 506 FGPGDRVVVMGPNGCGKSTLLK---LAAGLYKPAEGQVKLGGADIWEldPQVLGERIGYLPQdvhlfkgtlknnimlagg 582
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAGCIV--AAVSAELIFTRLQ------------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 583 indarflevaellgldrvaadsprsmdteiseggqgLSGGQRQLTAISRIF----LARPRVWLLDEPSASLDTESEERVL 658
Cdd:cd03227 78 ------------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|....
gi 2542252196 659 KALQSHTRPTDIVLIATHRPRLLSLANRLLIMRR 692
Cdd:cd03227 122 EAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
504-700 |
8.18e-08 |
|
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: 55.60 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 504 LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPA--EGQVKLGGAdiwELDPQVLGER----IGYLPQDVHLFKGT----- 572
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGS---PLKASNIRDTeragIVIIHQELTLVPELsvaen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 573 --LKNNIMLAGGI--NDARFLEVAELLGLDRVAADSprsmdteISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSAS 648
Cdd:TIGR02633 99 ifLGNEITLPGGRmaYNAMYLRAKNLLRELQLDADN-------VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 649 LdTESEERVL----KALQSHTrpTDIVLIATHRPRLLSLANRLLIMRRGQVIADGP 700
Cdd:TIGR02633 172 L-TEKETEILldiiRDLKAHG--VACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
483-655 |
8.73e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPG--------TPVIRlqvetlafgpGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGA-DIW----- 548
Cdd:PRK11147 321 EMENVNYQIDGkqlvkdfsAQVQR----------GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAyfdqh 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 549 --ELDPqvlgERigylpqdvhlfkgTLKNNimLAGGINDarflevAELLGLDRVAAD-------SPRSMDTEIseggQGL 619
Cdd:PRK11147 391 raELDP----EK-------------TVMDN--LAEGKQE------VMVNGRPRHVLGylqdflfHPKRAMTPV----KAL 441
|
170 180 190
....*....|....*....|....*....|....*.
gi 2542252196 620 SGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEE 655
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
506-700 |
1.34e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 506 FGPGDRVVVMGPNGCGKSTLLKLAAGLYKPA---EGQVKLGGAdiwELDpQVLGERIGYLPQ-DVHLFKGTLKNNIMLAG 581
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGR---PLD-SSFQRSIGYVQQqDLHLPTSTVRESLRFSA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 582 GINDA---------RFLE-VAELLGLDRVAadsprsmDTEISEGGQGLSGGQRQLTAISRIFLARPRVWL-LDEPSASLD 650
Cdd:TIGR00956 862 YLRQPksvsksekmEYVEeVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 651 TESEERVLKALQSHTRPTDIVLIATHRPRLLSLA--NRLLIMRRG-QVIADGP 700
Cdd:TIGR00956 935 SQTAWSICKLMRKLADHGQAILCTIHQPSAILFEefDRLLLLQKGgQTVYFGD 987
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
508-700 |
1.47e-07 |
|
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: 51.22 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLggadiweldpqvlgerigylpqdvhlfkgtlknnimlaggINDAR 587
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------------------IDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 588 FLEVAELlgldrvaadspRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHT-- 665
Cdd:smart00382 41 ILEEVLD-----------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 2542252196 666 ---RPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGP 700
Cdd:smart00382 110 llkSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
484-700 |
2.55e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 484 LEGVRFAYPGtpVIRLQVETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADI-WELDPQVLGERIGYL 562
Cdd:PRK10982 1 MSNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 563 PQDVHLFKG-TLKNNIMLAGGINDARFLEVAELLGlDRVAADSPRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWL 641
Cdd:PRK10982 79 HQELNLVLQrSVMDNMWLGRYPTKGMFVDQDKMYR-DTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 642 LDEPSASLdTESEE----RVLKALQShtRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGP 700
Cdd:PRK10982 158 MDEPTSSL-TEKEVnhlfTIIRKLKE--RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQP 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
501-705 |
3.03e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 501 VETLAF--GPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERIGYLPQDV-----------H 567
Cdd:PRK15112 29 VKPLSFtlREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 568 LFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSA 647
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM----------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 648 SLDTESEERVLKALQSHTRPTDI--VLIATHRPRLLSLANRLLIMRRGQVIADGPPAEVI 705
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
618-698 |
3.47e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 618 GLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL-QSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVI 696
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
..
gi 2542252196 697 AD 698
Cdd:TIGR02633 483 GD 484
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
166-298 |
4.76e-07 |
|
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: 52.08 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 166 WLLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLY 245
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 246 EHLLDLRL---DKRPrsLGSLAAQ-MNGLETVRTFFSSTIVFAMTDLpFGLMFIVFI 298
Cdd:cd18545 81 SHLQKLSFsffDSRP--VGKILSRvINDVNSLSDLLSNGLINLIPDL-LTLVGIVII 134
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
506-565 |
5.89e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 5.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 506 FGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKlggadiweLDPqvlGERIGYLPQD 565
Cdd:PRK15064 24 FGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS--------LDP---NERLGKLRQD 72
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
508-658 |
6.02e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 508 PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGERigylPQDVHL-FK------------GT-- 572
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLL----RQKIQIvFQnpygslnprkkvGQil 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 573 ---LKNNIMLAGGINDARFLEVAELLGLDRVAADSPRSMdteiseggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASL 649
Cdd:PRK11308 116 eepLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHM----------FSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
....*....
gi 2542252196 650 DTESEERVL 658
Cdd:PRK11308 186 DVSVQAQVL 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
425-704 |
7.19e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 425 CTIL-GGKVIG---PIAQSVGILVQWqhvrealeMVNRLLALEGNRPEgkvllvPETLPDRLELEGVRFAyPGTPVIRLQ 500
Cdd:COG3845 211 VTVLrRGKVVGtvdTAETSEEELAEL--------MVGREVLLRVEKAP------AEPGEVVLEVENLSVR-DDRGVPALK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 501 VETLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP-QVLGERIGYLPQDVH---LFKG-TLKN 575
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRLgrgLVPDmSVAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 576 NIMLaGGINDARFlevAELLGLDRVAADS------------PRSMDTEISeggqGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:COG3845 356 NLIL-GRYRRPPF---SRGGFLDRKAIRAfaeelieefdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 644 EPSASLDTESEERVLKALQSH-TRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
482-662 |
9.66e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGtpviRLQVETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGgadiweldPQVlgeRI 559
Cdd:TIGR03719 323 IEAENLTKAFGD----KLLIDDLSFKlpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------ETV---KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 GYLPQdvhlFKGTLKNN------------IMLAGG--INDARFLEVAELLGLD---RVaadsprsmdteisegGQgLSGG 622
Cdd:TIGR03719 388 AYVDQ----SRDALDPNktvweeisggldIIKLGKreIPSRAYVGRFNFKGSDqqkKV---------------GQ-LSGG 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2542252196 623 QRqltaiSRIFLAR-----PRVWLLDEPSASLDTESeervLKALQ 662
Cdd:TIGR03719 448 ER-----NRVHLAKtlksgGNVLLLDEPTNDLDVET----LRALE 483
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
167-436 |
1.07e-06 |
|
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: 50.72 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 167 LLEVGVATVVVNLLAVATSLFSMQVYDRVVPTFAYATLW--AMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQL 244
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 245 YEHLLDLRL---DKRPrsLGSLAAQM-NGLETVRTFFSSTIVFAMTDLPFGLMFIVFIAAIGGMISTVYLALLPVSLLLG 320
Cdd:pfam00664 81 FKKILRQPMsffDTNS--VGELLSRLtNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 321 WLAQRQLRTLARLEIQRGHERHGLLVDTIQGAETIQSSGSGWFFADLWRSITASMAAYSLKSKLISSLTTTTTATLSTVG 400
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 2542252196 401 YVAAVVVGVLLIEAGQLTTGGLIACTILGGKVIGPI 436
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
620-704 |
1.18e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 620 SGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIAT-HRPRLLSLANRLLIMRRGQVIAD 698
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTqYMEEAEQLAHELTVIDRGRVIAD 225
|
....*.
gi 2542252196 699 GPPAEV 704
Cdd:NF000106 226 GKVDEL 231
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
503-688 |
3.69e-06 |
|
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: 48.23 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVmGPNGCGKSTLLKlaaglykpaegqvklggADIWeldpqVLGE------RIGYLPqDVhLFKG----- 571
Cdd:cd03278 17 TIPFPPGLTAIV-GPNGSGKSNIID-----------------AIRW-----VLGEqsakslRGEKMS-DV-IFAGsetrk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 572 ---------TLKN-----NIMLAGGINdaRFLEvaellgldrvaadSPRSMDTEISEggqgLSGGQRQLTAISRIF---L 634
Cdd:cd03278 72 panfaevtlTFDNsdgrySIISQGDVS--EIIE-------------APGKKVQRLSL----LSGGEKALTALALLFaifR 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 635 ARPRVW-LLDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLLSLANRLL 688
Cdd:cd03278 133 VRPSPFcVLDEVDAALDDANVERFARLLKEFSKETQFIVI-THRKGTMEAADRLY 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
482-704 |
3.72e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYpGTPVIRLQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDPQVLGE---- 557
Cdd:PRK11831 8 VDMRGVSFTR-GNRCIFDNI-SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 558 -----RIGYLPQDVHLFKGT---LKNNIMLAGGINDARFLEVAELLGLdRVAADsprSMDTEiseggqgLSGGQRQLTAI 629
Cdd:PRK11831 86 msmlfQSGALFTDMNVFDNVaypLREHTQLPAPLLHSTVMMKLEAVGL-RGAAK---LMPSE-------LSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2542252196 630 SRIFLARPRVWLLDEPSASLDTESEERVLKALQ--SHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISelNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
519-695 |
6.05e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 519 GCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP-QVLGERIGYLPQ---DVHLFKG-TLKNNIMLAGGINDARFlevAE 593
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFPNfSIAQNMAISRSLKDGGY---KG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 594 LLGL-----DRVAADSPR--------SMDTEISEggqgLSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKA 660
Cdd:PRK09700 376 AMGLfhevdEQRTAENQRellalkchSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKV 451
|
170 180 190
....*....|....*....|....*....|....*.
gi 2542252196 661 LQSHTRPTDIVL-IATHRPRLLSLANRLLIMRRGQV 695
Cdd:PRK09700 452 MRQLADDGKVILmVSSELPEIITVCDRIAVFCEGRL 487
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
619-696 |
9.62e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQLTAISRIF---LARPR-VWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLLSLANRLL--IMRR 692
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqKYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVI-SLREEMLEKADKLVgvTMVE 1156
|
....
gi 2542252196 693 GQVI 696
Cdd:pfam02463 1157 NGVS 1160
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
172-307 |
1.14e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 47.81 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 172 VATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHLLDL 251
Cdd:cd18542 6 LALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 252 RLD--KRPRSlGSLAAQMNG-LETVRTFFSSTIVFamtdlpFGLMFIVFIAAIGGMIST 307
Cdd:cd18542 86 SFSfhDKART-GDLMSRCTSdVDTIRRFLAFGLVE------LVRAVLLFIGALIIMFSI 137
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
482-543 |
1.16e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 482 LELEGVRFAYPGtpviRLQVETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLG 543
Cdd:PRK11819 325 IEAENLSKSFGD----RLLIDDLSFSlpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG 384
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
619-695 |
1.48e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542252196 619 LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLK-ALQSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQV 695
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQlIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
482-705 |
1.50e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAY-PGTPVIRLQVET--------LAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP 552
Cdd:PRK15439 253 LELPGNRRQQaAGAPVLTVEDLTgegfrnisLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 553 -QVLGERIGYLPQD-----VHLFKGTLKNNIMLAGGINDARFLEVAELLGLDRVAadspRSMDTEISEGGQ---GLSGGQ 623
Cdd:PRK15439 333 aQRLARGLVYLPEDrqssgLYLDAPLAWNVCALTHNRRGFWIKPARENAVLERYR----RALNIKFNHAEQaarTLSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 624 RQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQS-HTRPTDIVLIATHRPRLLSLANRLLIMRRGQvIADGPPA 702
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSiAAQNVAVLFISSDLEEIEQMADRVLVMHQGE-ISGALTG 487
|
...
gi 2542252196 703 EVI 705
Cdd:PRK15439 488 AAI 490
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
516-705 |
2.43e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 516 GPNGCGKSTLLKLAAGLYKPAEGQVKLGGAdiwELDPQVLG--ERIGYLPQDVHLFKG-TLKNNIML--------AGGIN 584
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIAtrRRVGYMSQAFSLYGElTVRQNLELharlfhlpAAEIA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 585 dARFLEVAELLGLDRVAADSPRSmdteiseggqgLSGGQRQltaisRIFLA-----RPRVWLLDEPSASLDTESEE---R 656
Cdd:NF033858 376 -ARVAEMLERFDLADVADALPDS-----------LPLGIRQ-----RLSLAvavihKPELLILDEPTSGVDPVARDmfwR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 657 VLKALQSHTRPTdiVLIATH------RPRLLSLanrlliMRRGQVIADGPPAEVI 705
Cdd:NF033858 439 LLIELSREDGVT--IFISTHfmneaeRCDRISL------MHAGRVLASDTPAALV 485
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
481-688 |
2.73e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 45.38 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 481 RLELEGVRfAYPGTPVIrlqvetlafGPGDRV-VVMGPNGCGKSTLLKlaaglykpaegqvklggADIWeldpqVLGERi 559
Cdd:cd03239 3 QITLKNFK-SYRDETVV---------GGSNSFnAIVGPNGSGKSNIVD-----------------AICF-----VLGGK- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 560 gylpqDVHLFKGTLKNNIMLAG--GINDAR----FLEVAELLGLDRVaadsprsmdteisegGQGLSGGQRQLTAISRIF 633
Cdd:cd03239 50 -----AAKLRRGSLLFLAGGGVkaGINSASveitFDKSYFLVLQGKV---------------EQILSGGEKSLSALALIF 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 634 ----LARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLL 688
Cdd:cd03239 110 alqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLI 168
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
172-305 |
2.86e-05 |
|
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: 46.73 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 172 VATVVVNLLAVATSLFSMQVYDRVV----PTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEH 247
Cdd:cd18563 6 LLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEH 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542252196 248 LLDLRL---DKrpRSLGSLAAQMNG-LETVRTFFSSTIVFAMTDLpfgLMFIvfiaAIGGMI 305
Cdd:cd18563 86 LQRLSLsffDK--RQTGSLMSRVTSdTDRLQDFLSDGLPDFLTNI---LMII----GIGVVL 138
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
619-698 |
3.67e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKAL-QSHTRPTDIVLIATHRPRLLSLANRLLIMRRGQVIA 697
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLInQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
.
gi 2542252196 698 D 698
Cdd:PRK13549 486 D 486
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
482-704 |
4.62e-05 |
|
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: 46.60 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 482 LELEGVRFAYPGTPVIRLQVETLAF--GPGDRVVVMGPNGCGKS----TLLKLAAGLYKPAEGQVKLGGADIWELDPQVL 555
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFdiAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 556 ----GERIGYLPQD-------VHlfkgTLKNNI----MLAGGIN--DARfLEVAELlgLDRVAADSPRSMdteISEGGQG 618
Cdd:COG4172 87 rrirGNRIAMIFQEpmtslnpLH----TIGKQIaevlRLHRGLSgaAAR-ARALEL--LERVGIPDPERR---LDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQltaisRIFLA-----RPRVWLLDEPSASLDTESEERVLKALQSHTRPTD--IVLIaTHRPRLLS-LANRLLIM 690
Cdd:COG4172 157 LSGGQRQ-----RVMIAmalanEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGmaLLLI-THDLGVVRrFADRVAVM 230
|
250
....*....|....
gi 2542252196 691 RRGQVIADGPPAEV 704
Cdd:COG4172 231 RQGEIVEQGPTAEL 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
501-704 |
5.45e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 501 VETLAFG--PGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIWELDP---QVLGERIGYLPQDVHLF---KGT 572
Cdd:PRK10261 340 VEKVSFDlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 573 LKNNIM--------LAGGINDARFLEVAELLGL-DRVAADSPRSmdteiseggqgLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:PRK10261 420 VGDSIMeplrvhglLPGKAAAARVAWLLERVGLlPEHAWRYPHE-----------FSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 644 EPSASLDTESEERVLKALQSHTRPTDIV-LIATHRPRLLS-LANRLLIMRRGQVIADGPPAEV 704
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAyLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAV 551
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
503-696 |
2.33e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 503 TLAFGPGDRVVVMGPNGCGKS-TLLKLAAGLYKPA----EGQVKLGGADIWELDPQVL----GERIGYLPQD-------V 566
Cdd:PRK15134 29 SLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQEpmvslnpL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 567 HLFKGTLKNNIMLAGGIND--ARflevAELLG-LDRVAAdspRSMDTEISEGGQGLSGGQRQLTAISRIFLARPRVWLLD 643
Cdd:PRK15134 109 HTLEKQLYEVLSLHRGMRReaAR----GEILNcLDRVGI---RQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 644 EPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLL-SLANRLLIMRRGQVI 696
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMgLLFITHNLSIVrKLADRVAVMQNGRCV 236
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
170-301 |
2.88e-04 |
|
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: 43.63 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 170 VGVATVVV-NLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHL 248
Cdd:cd18546 3 LALLLVVVdTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2542252196 249 LDLRLD--KRPRSlGSLAAQM-NGLETVRTFFSSTIVFAMTdlpfGLMFIVFIAAI 301
Cdd:cd18546 83 QRLSLDfhERETS-GRIMTRMtSDIDALSELLQTGLVQLVV----SLLTLVGIAVV 133
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
619-704 |
4.46e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLI-ATHRPRLLS-LANRLLIMRRGQVI 696
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVlITHDLALVAeAAHKIIVMYAGQVV 233
|
....*...
gi 2542252196 697 ADGPPAEV 704
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
479-704 |
8.09e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 479 PDRLELEGVRFAYPGTPV--IRLQVETlafgpGDRVVVMGPNGCGKS-----TLLKLAAGLYKPAeGQVKLGGAdiwELD 551
Cdd:PRK10418 2 PQQIELRNIALQAAQPLVhgVSLTLQR-----GRVLALVGGSGSGKSltcaaALGILPAGVRQTA-GRVLLDGK---PVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 552 PQVL-GERIGYLPQD-------VHLFKGTLKNNIMLAGGI-NDARFLEVAELLGLDrvaaDSPRSMDTEISEggqgLSGG 622
Cdd:PRK10418 73 PCALrGRKIATIMQNprsafnpLHTMHTHARETCLALGKPaDDATLTAALEAVGLE----NAARVLKLYPFE----MSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 623 QRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLS-LANRLLIMRRGQVIADGP 700
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgMLLVTHDMGVVArLADDVAVMSHGRIVEQGD 224
|
....
gi 2542252196 701 PAEV 704
Cdd:PRK10418 225 VETL 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
483-564 |
8.10e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 483 ELEGVRFAYPGTPVIRlQVeTLAFGPGDRVVVMGPNGCGKSTLLKLAAGLYKPAEGQVKLGGADIweLDP---QVLGERI 559
Cdd:NF033858 3 RLEGVSHRYGKTVALD-DV-SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM--ADArhrRAVCPRI 78
|
....*
gi 2542252196 560 GYLPQ 564
Cdd:NF033858 79 AYMPQ 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-688 |
1.03e-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: 42.74 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542252196 619 LSGGQRQLTAIS---RIFLARPRVW-LLDEPSASLDTESEERVLKALQSHTRPTDIVLIaTHRPRLLSLANRLL 688
Cdd:TIGR02168 1090 LSGGEKALTALAllfAIFKVKPAPFcILDEVDAPLDDANVERFANLLKEFSKNTQFIVI-THNKGTMEVADQLY 1162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
619-699 |
1.17e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQLTAISRIFLARPRVWLLDEPSASLDTESEERVLKALQSHTRPTDI-VLIATHRPRLLS-LANRLLIMRRGQVI 696
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAeIADRVLVMYQGEAV 248
|
...
gi 2542252196 697 ADG 699
Cdd:PRK10261 249 ETG 251
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
172-307 |
1.38e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 41.31 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 172 VATVVVNLLAVATSLFSMQVYDRVVPTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHL--L 249
Cdd:cd18543 6 LAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLqrL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542252196 250 DLRLDKRPRSlGSLAAQMNG-LETVRTFFSstivfamtdlpFGLMFIV----FIAAIGGMIST 307
Cdd:cd18543 86 DGAFHDRWQS-GQLLSRATSdLSLVQRFLA-----------FGPFLLGnlltLVVGLVVMLVL 136
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
617-686 |
1.44e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 41.09 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542252196 617 QGLSGGQRQLTAISRIFlARPRV-----WLLDEPSASLDTESEERVLKALQSHTRPTDIVlIATHRPRLLSLANR 686
Cdd:cd03272 157 QQLSGGQKSLVALALIF-AIQKCdpapfYLFDEIDAALDAQYRTAVANMIKELSDGAQFI-TTTFRPELLEVADK 229
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
595-703 |
1.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 595 LGLDRVAADspRSMDTeiseggqgLSGGQRQLTAISRIFLARPR--VWLLDEPSASLDTESEERVLKALQSHTRPTDIVL 672
Cdd:PRK00635 463 LGLPYLTPE--RALAT--------LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
|
90 100 110
....*....|....*....|....*....|....*..
gi 2542252196 673 IATHRPRLLSLANRLL-IMRR-----GQVIADGPPAE 703
Cdd:PRK00635 533 LVEHDEQMISLADRIIdIGPGagifgGEVLFNGSPRE 569
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
170-359 |
3.30e-03 |
|
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: 40.09 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 170 VGVATVVVNLLAVATSLFSMQVYDRVV-PTFAYATLWAMVAGMVIMVLLDWVLKFIRSRILDEVAKRVDIALSQQLYEHL 248
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 249 LDLR-LDKRPRSLGSLAAQ-MNGLETVRTFFS--------------------------STIVFAMTdLPFglmFIVFIAA 300
Cdd:cd18584 81 LALGpALLRRQSSGELATLlTEGVDALDGYFArylpqlvlaaivpllilvavfpldwvSALILLVT-APL---IPLFMIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2542252196 301 IGGMISTvylallpvslllgwLAQRQLRTLARLeiqrgherHGLLVDTIQGAETIQSSG 359
Cdd:cd18584 157 IGKAAQA--------------ASRRQWAALSRL--------SGHFLDRLRGLPTLKLFG 193
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
619-701 |
8.02e-03 |
|
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: 38.75 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542252196 619 LSGGQRQltaisRIFLAR--------PRVWLLDEPSASLDTESEERVLKALQSHTRPTDIVLIATHRPRLLSLANRLLIM 690
Cdd:cd03271 170 LSGGEAQ-----RIKLAKelskrstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244
|
90
....*....|....*..
gi 2542252196 691 ------RRGQVIADGPP 701
Cdd:cd03271 245 gpeggdGGGQVVASGTP 261
|
|
| |
