|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-523 |
0e+00 |
|
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: 756.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI------------LgesgsgksvsssAIMNLIDmPPGKITS 68
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALvgesgsgksvtaL------------SILRLLP-DPAAHPS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGKDLLKMSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALPDAER 147
Cdd:COG4172 69 GSILFDGQDLLGLSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHrGLSGAAARARALELLERVGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 ALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVV 227
Cdd:COG4172 149 RLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 228 VMEKGQLVESGTVRDVYRNPQHAYTKKLIAAAPgKGEMHEPEAQGEPILSVKDARKSY-----------GDFEALKGVSF 296
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAAPQHPYTRKLLAAEP-RGDPRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 297 DLKQGETVAVVGESGSGKSTLARILLRLEePDGGTAHWKGKDLFTMSPGDLFKLRRDLQMVFQDPTQSLNPRMTVYQLIS 376
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 377 EAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVIT 456
Cdd:COG4172 387 EGLRVHGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 457 LLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALLAASLDPD 523
Cdd:COG4172 467 LLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-525 |
0e+00 |
|
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: 671.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPGKITSGEILLDGKDLLKMSAE 84
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL--PHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARrevnGRRIAMIFQDPLSHLNPVyTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQRV 164
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVY 244
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 245 RNPQhaytkkLIAAAPGKGEMH----EPEAQGEPILSVKDARKSY-----GDFEALKGVSFDLKQGETVAVVGESGSGKS 315
Cdd:COG1123 232 AAPQ------ALAAVPRLGAARgraaPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 316 TLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQMVFQDPTQSLNPRMTVYQLISEAWIIHpEILPKAKWRERV 395
Cdd:COG1123 306 TLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLH-GLLSRAERRERV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 396 GELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHD 475
Cdd:COG1123 385 AELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2087084196 476 LPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALLAASLDPDPD 525
Cdd:COG1123 465 LAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-531 |
5.61e-177 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 512.86 E-value: 5.61e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGK----- 76
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 77 DLLKMSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALPDAERALDKYPHE 155
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 236 ESGTVRDVYRNPQHAYTKKLIAAAPGKGEM-------------------HEPEAQ------GEPILSVKDARKSYG---- 286
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGAMkgldyprrfplislehpakQEPPIEqdtvvdGEPILQVRNLVTRFPlrsg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 -------DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQMVFQ 359
Cdd:PRK10261 329 llnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 360 DPTQSLNPRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVC 439
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVH-GLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 440 DEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALLAAS 519
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
570
....*....|..
gi 2087084196 520 LDPDPDVQAANR 531
Cdd:PRK10261 568 PVADPSRQRPQR 579
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-519 |
1.31e-171 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 495.76 E-value: 1.31e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLK 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALPDAERALDKYPHEFSGG 159
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 160 QRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGT 239
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 240 VRDVYRNPQHAYTKKLIAAAPgKGEMHEPEAQGEPILSVKDARKSY-----------GDFEALKGVSFDLKQGETVAVVG 308
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEP-SGDPVPLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 309 ESGSGKSTLARILLRLEEPDGGTAhWKGKDLFTMSPGDLFKLRRDLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEILPK 388
Cdd:PRK15134 320 ESGSGKSTTGLALLRLINSQGEIW-FDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 389 AKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIA 468
Cdd:PRK15134 399 AQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLA 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 469 FIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALLAAS 519
Cdd:PRK15134 479 YLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
270-525 |
6.16e-140 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 407.20 E-value: 6.16e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 270 AQGEPILSVKDARKSY----GDFE-------ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKD 338
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 339 LFTMSPGDLFKLRRDLQMVFQDPTQSLNPRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSG 418
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIH-GLASKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 419 GQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260
....*....|....*....|....*..
gi 2087084196 499 TVAQVFDNPQKPYTQALLAASLDPDPD 525
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVPVPDPE 267
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-274 |
2.32e-136 |
|
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: 397.89 E-value: 2.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIdmPPGKITSGEILLD 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLvgesgsgkstLAR----------AILGLL--PPPGITSGEILFD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALPDAERALDKYP 153
Cdd:COG0444 69 GEDLLKLSEKELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHgGLSKAEARERAIELLERVGLPDPERRLDRYP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2087084196 234 LVESGTVRDVYRNPQHAYTKKLIAAAPGKGEMHEPEA--QGEP 274
Cdd:COG0444 229 IVEEGPVEELFENPRHPYTRALLSSIPRLDPDGRRLIpiPGEP 271
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-527 |
1.06e-127 |
|
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: 375.55 E-value: 1.06e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEP---DGGTAHWKGKDLFTMSPGDL 347
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 348 FKLR-RDLQMVFQDPTQSLNPRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSL--EHMGRYPHQFSGGQRQRI 424
Cdd:COG0444 81 RKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIH-GGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 425 AIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260
....*....|....*....|...
gi 2087084196 505 DNPQKPYTQALLAASLDPDPDVQ 527
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGR 262
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-498 |
5.23e-108 |
|
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: 321.76 E-value: 5.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL 350
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-521 |
3.30e-105 |
|
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: 315.59 E-value: 3.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYG----DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklR 351
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RDLQMVFQDPTQSLNPRMTVYQLISEAWIIH--PEIlpkakwRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARA 429
Cdd:COG1124 79 RRVQMVFQDPYASLHPRHTVDRILAEPLRIHglPDR------EERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQK 509
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
250
....*....|..
gi 2087084196 510 PYTQALLAASLD 521
Cdd:COG1124 233 PYTRELLAASLA 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
290-527 |
2.67e-104 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 316.26 E-value: 2.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQMVFQDPTQSLNPRM 369
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 370 TVYQLISEAWII-HPEiLPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV 448
Cdd:PRK15079 116 TIGEIIAEPLRTyHPK-LSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 449 SVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALLAASLDPDPDVQ 527
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLE 273
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
271-524 |
1.86e-103 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 313.82 E-value: 1.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 271 QGEPILSVKDARKSY----GDF------EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLF 340
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 341 TMSPGDLFKLRRDLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEiLPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQ 420
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTS-LSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 421 RQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTV 500
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260
....*....|....*....|....*.
gi 2087084196 501 AQVFDNPQKPYTQALLAA--SLDPDP 524
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSAtpRLNPDD 265
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-238 |
1.03e-100 |
|
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: 303.27 E-value: 1.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLidmppGKITSGEILLD 74
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLvgesgsgkstLAR----------AILGL-----LKPTSGSIIFD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSaEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERALDKYPH 154
Cdd:cd03257 66 GKDLLKLS-RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
....
gi 2087084196 235 VESG 238
Cdd:cd03257 225 VEEG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
273-530 |
1.64e-96 |
|
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: 303.14 E-value: 1.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPD----GGTAHWKGKDLFTMSP 344
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 GDLFKLR-RDLQMVFQDPTQSLNPRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGL--SLEHMGRYPHQFSGGQR 421
Cdd:COG4172 84 RELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLH-RGLSGAAARARALELLERVGIpdPERRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 422 QRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVA 501
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250 260
....*....|....*....|....*....
gi 2087084196 502 QVFDNPQKPYTQALLAASLDPDPDVQAAN 530
Cdd:COG4172 243 ELFAAPQHPYTRKLLAAEPRGDPRPVPPD 271
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-276 |
7.24e-88 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 273.92 E-value: 7.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDF-------HTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIDMpp 63
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLvgesgcgkstLGR----------LLLRLEEP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 64 gkiTSGEILLDGKDLLKMSAEARREVNgRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGI-STTQAQAEALRLFKRVAL 142
Cdd:COG4608 71 ---TSGEILFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEV 222
Cdd:COG4608 147 R--PEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHI 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 223 ADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLIAAAPGKgemhEPEAQGEPIL 276
Cdd:COG4608 225 SDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLSAVPVP----DPERRRERIV 274
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
273-518 |
5.44e-87 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 269.40 E-value: 5.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSY---------GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmS 343
Cdd:COG4167 2 SALLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL---E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 344 PGDlFKLR-RDLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEILPKAKwRERVGELLGQVGLSLEHMGRYPHQFSGGQRQ 422
Cdd:COG4167 79 YGD-YKYRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEER-EERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 423 RIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*.
gi 2087084196 503 VFDNPQKPYTQALLAA 518
Cdd:COG4167 237 VFANPQHEVTKRLIES 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-260 |
2.47e-86 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 270.07 E-value: 2.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPpGKITSGEILLDGKDLLKMSAE 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALPDAERALDKYPHEFSGGQRQR 163
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*..
gi 2087084196 244 YRNPQHAYTKKLIAAAP 260
Cdd:PRK11022 242 FRAPRHPYTQALLRALP 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-260 |
2.02e-85 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 267.75 E-value: 2.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidMPPGKITSGEILLDGKDLLK 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL--LAANGRIGGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALPDAERALDKYPHEFSGG 159
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 160 QRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGT 239
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|.
gi 2087084196 240 VRDVYRNPQHAYTKKLIAAAP 260
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVP 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-261 |
1.94e-81 |
|
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: 254.34 E-value: 1.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIdmppgKITSGEILLD 74
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLvgesgsgkstLLR----------ALAGLE-----RPWSGEVTFD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEARRevngRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGIstTQAQAEALRLFKRVALPdaERALDKYPH 154
Cdd:COG1124 66 GRPVTRRRRKAFR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLP--PSFLDRYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:COG1124 138 QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
250 260
....*....|....*....|....*..
gi 2087084196 235 VESGTVRDVYRNPQHAYTKKLIAAAPG 261
Cdd:COG1124 218 VEELTVADLLAGPKHPYTRELLAASLA 244
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-259 |
6.53e-77 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 241.89 E-value: 6.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 24 AVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmPPGKITSGEILLDGKDLLKMSaearreVNGRRIAMIFQDPLS 103
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLP-PGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 104 HLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPT 183
Cdd:TIGR02770 74 AFNPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 184 TALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLIAAA 259
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
291-524 |
2.47e-75 |
|
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: 239.32 E-value: 2.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQMVFQDPTQSLNPRMT 370
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSV 450
Cdd:TIGR02769 107 VRQIIGEP-LRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 451 QAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNpQKPYTQALLAASLDPDP 524
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVLPEHP 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
275-531 |
1.07e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 239.98 E-value: 1.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL 350
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDPtqSLNPRMTVYQLISeawiiHP-EI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIA 427
Cdd:COG1135 81 RRKIGMIFQHF--NLLSSRTVAENVA-----LPlEIagVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250 260
....*....|....*....|....
gi 2087084196 508 QKPYTQALLAASLDPDPDVQAANR 531
Cdd:COG1135 233 QSELTRRFLPTVLNDELPEELLAR 256
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
274-525 |
3.68e-74 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 236.12 E-value: 3.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSY---------GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSP 344
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 GDLFKLRRDLQMVFQDPTQSLNPRMTVYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRI 424
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREIIREP-LRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 425 AIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTV--AQ 502
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVgdKL 240
|
250 260
....*....|....*....|...
gi 2087084196 503 VFDNPQkpyTQALLAASLDPDPD 525
Cdd:PRK10419 241 TFSSPA---GRVLQNAVLPAFPV 260
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-260 |
1.53e-71 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 231.72 E-value: 1.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MAdhLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmPPGKITSGEILLDGKDLLK 80
Cdd:COG4170 1 MP--LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNGIDLLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGISTT------QAQAEALRLFKRVALPDAERALDKYPH 154
Cdd:COG4170 78 LSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfkWRKKRAIELLHRVGIKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250 260
....*....|....*....|....*.
gi 2087084196 235 VESGTVRDVYRNPQHAYTKKLIAAAP 260
Cdd:COG4170 238 VESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-260 |
2.47e-71 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 231.13 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTG---------TVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDG 75
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV-----KATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 76 KDLLKMSAEARREVNgRRIAMIFQDPLSHLNPVYTVGWQMREALKTH--GISTTQAQAEALRLFKRVALpdAERALDKYP 153
Cdd:PRK15079 83 KDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGL--LPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260
....*....|....*....|....*..
gi 2087084196 234 LVESGTVRDVYRNPQHAYTKKLIAAAP 260
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-517 |
2.12e-70 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 225.26 E-value: 2.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKLRRDL 354
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQdptqSLN--PRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:COG1126 80 GMVFQ----QFNlfPHLTVLENVTLAPIKV-KKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYT 512
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
....*
gi 2087084196 513 QALLA 517
Cdd:COG1126 233 RAFLS 237
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
265-520 |
1.06e-69 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 224.31 E-value: 1.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 265 MHEPEaqgEPILSVKDARKSYGDFE----ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK--- 337
Cdd:COG4107 1 MTNEE---QPLLSVRGLSKRYGPGCgtvvACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRdgg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 338 --DLFTMSPGDLFKLRR-DLQMVFQDPTQSLNPRMTV-----YQLISEAWIIHPEIlpkakwRERVGELLGQVGLSLEHM 409
Cdd:COG4107 78 prDLFALSEAERRRLRRtDWGMVYQNPRDGLRMDVSAggniaERLMAAGERHYGDI------RARALEWLERVEIPLERI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 410 GRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVM 489
Cdd:COG4107 152 DDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVM 231
|
250 260 270
....*....|....*....|....*....|.
gi 2087084196 490 QKGEVVELGTVAQVFDNPQKPYTQALLAASL 520
Cdd:COG4107 232 KNGRVVESGLTDQVLEDPQHPYTQLLVSSVL 262
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-508 |
1.39e-67 |
|
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: 217.83 E-value: 1.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL 350
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDpTQSLNPRmTVYQLISeawiiHP-EI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIA 427
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSR-TVFENVA-----LPlEIagVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
.
gi 2087084196 508 Q 508
Cdd:cd03258 233 Q 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
273-518 |
8.11e-67 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 219.21 E-value: 8.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDG---GTAHWKGKDLFTMSPG 345
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 346 DLFKLR-RDLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEILPKAKWRERVgELLGQVGL--SLEHMGRYPHQFSGGQRQ 422
Cdd:PRK09473 90 ELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESV-RMLDAVKMpeARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 423 RIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250
....*....|....*.
gi 2087084196 503 VFDNPQKPYTQALLAA 518
Cdd:PRK09473 249 VFYQPSHPYSIGLLNA 264
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-261 |
6.11e-65 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 214.44 E-value: 6.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSvDFHTV-------TGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAImNLIDMPpgkiTSGEILL 73
Cdd:PRK11308 1 SQQPLLQAIDLK-KHYPVkrglfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLL-TMIETP----TGGELYY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 74 DGKDLLKMSAEARREVNgRRIAMIFQDPLSHLNPVYTVGWQMREALKthgISTTQAQAE----ALRLFKRVALpDAERAl 149
Cdd:PRK11308 75 QGQDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLL---INTSLSAAErrekALAMMAKVGL-RPEHY- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 DKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:PRK11308 149 DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
250 260 270
....*....|....*....|....*....|..
gi 2087084196 230 EKGQLVESGTVRDVYRNPQHAYTKKLIAAAPG 261
Cdd:PRK11308 229 YLGRCVEKGTKEQIFNNPRHPYTQALLSATPR 260
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
276-512 |
6.94e-64 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 212.31 E-value: 6.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFT-MSPGDlfklrRDL 354
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRE-----RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPtqSLNPRMTVYQLISeawiIHPEILP--KAKWRERVGELLGQVGLslEHMG-RYPHQFSGGQRQRIAIARALA 431
Cdd:COG1118 78 GFVFQHY--ALFPHMTVAENIA----FGLRVRPpsKAEIRARVEELLELVQL--EGLAdRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPY 511
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
.
gi 2087084196 512 T 512
Cdd:COG1118 230 V 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
274-511 |
3.36e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 210.34 E-value: 3.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklRRD 353
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-----KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPtqSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALE 433
Cdd:COG3842 79 VGMVFQDY--ALFPHLTVAENV--AFGLRMRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHD----LPLvrdfADYVMVMQKGEVVELGTVAQVFDNPQK 509
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL----ADRIAVMNDGRIEQVGTPEEIYERPAT 229
|
..
gi 2087084196 510 PY 511
Cdd:COG3842 230 RF 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
271-507 |
6.08e-62 |
|
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: 203.29 E-value: 6.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 271 QGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL 350
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQ-----DptqSlnprMTVYQLISEAWIIHPEiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIA 425
Cdd:COG1127 81 RRRIGMLFQggalfD---S----LTVFENVAFPLREHTD-LSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 426 IARALALEPQLIVCDEAVSALD-VSvqAQVI-TLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpIT--SAVIdELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
....*.
gi 2087084196 504 F--DNP 507
Cdd:COG1127 230 LasDDP 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-496 |
1.04e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 202.20 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLF 348
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 KLRRD-LQMVFQDPTqsLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIA 427
Cdd:COG1136 82 RLRRRhIGFVFQFFN--LLPELTALENVALPLLLAG--VSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDlPLVRDFADYVMVMQKGEVVE 496
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
279-523 |
5.90e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 204.26 E-value: 5.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 279 KDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDL 354
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDpTQSLNPRmTVYQLISEAWiihpEI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK11153 85 GMIFQH-FNLLSSR-TVFDNVALPL----ELagTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYT 512
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
250
....*....|.
gi 2087084196 513 QALLAASLDPD 523
Cdd:PRK11153 238 REFIQSTLHLD 248
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
276-509 |
1.22e-60 |
|
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: 199.48 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDL 354
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDP-TQSLNPrmTVYQliseawiihpEI--------LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIA 425
Cdd:COG1122 78 GLVFQNPdDQLFAP--TVEE----------DVafgpenlgLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 426 IARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFD 505
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
....
gi 2087084196 506 NPQK 509
Cdd:COG1122 224 DYEL 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-503 |
3.94e-60 |
|
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: 207.35 E-value: 3.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPgkiTSGEIL------------- 72
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP---TSGRIIyhvalcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 ---LDGK--------------DLLKMSAEARREVNgRRIAMIFQDPLShLNPVYTVGWQMREALKTHGISTTQAQAEALR 135
Cdd:TIGR03269 74 rpsKVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 136 LFKRVALpdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHD 215
Cdd:TIGR03269 152 LIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 216 LGVVSEVADRVVVMEKGQLVESGTVRDVyrnpqhayTKKLIAAAPGKGEMHEPEaQGEPILSVKDARKSY-----GDFEA 290
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECEVE-VGEPIIKVRNVSKRYisvdrGVVKA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWK-GKDLFTMS-PGDLFKLR--RDLQMVFQDptQSLN 366
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTkPGPDGRGRakRYIGILHQE--YDLY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 367 PRMTVYQLISEAwiIHPEiLPKAKWRERVGELLGQVGLSLEH----MGRYPHQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:TIGR03269 378 PHRTVLDNLTEA--IGLE-LPDELARMKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 443 VSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-261 |
8.50e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.07 E-value: 8.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVHAVRNISYYLDRGE-------------TLAILgesgsgksvsssaiMNLIDMPpgkiTSGEIL 72
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEifgiigysgagksTLIRC--------------INLLERP----TSGSVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 LDGKDLLKMSAEARREVNgRRIAMIFQdplsHLN--PVYTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALPDae 146
Cdd:COG1135 64 VDGVDLTALSERELRAAR-RKIGMIFQ----HFNllSSRTV----AEnvalPLEIAGVPKAEIRKRVAELLELVGLSD-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRV 226
Cdd:COG1135 133 KA-DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRV 211
|
250 260 270
....*....|....*....|....*....|....*
gi 2087084196 227 VVMEKGQLVESGTVRDVYRNPQHAYTKKLIAAAPG 261
Cdd:COG1135 212 AVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLN 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
273-522 |
2.16e-58 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 194.76 E-value: 2.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK-----DLFTMSPGDL 347
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 348 -FKLRRDLQMVFQDPTQSLnpRMTVY-------QLISEAWIIHPEIlpkakwRERVGELLGQVGLSLEHMGRYPHQFSGG 419
Cdd:PRK11701 84 rRLLRTEWGFVHQHPRDGL--RMQVSaggnigeRLMAVGARHYGDI------RATAGDWLERVEIDAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 420 QRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGT 499
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250 260
....*....|....*....|...
gi 2087084196 500 VAQVFDNPQKPYTQALLAASLDP 522
Cdd:PRK11701 236 TDQVLDDPQHPYTQLLVSSVLQV 258
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
273-518 |
2.45e-58 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 195.01 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSY----GDF-----EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmS 343
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL---H 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 344 PGDLFKLRRDLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEILPKAKwRERVGELLGQVGLSLEHMGRYPHQFSGGQRQR 423
Cdd:PRK15112 79 FGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQR-EKQIIETLRQVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
250
....*....|....*
gi 2087084196 504 FDNPQKPYTQALLAA 518
Cdd:PRK15112 238 LASPLHELTKRLIAG 252
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
276-498 |
1.01e-57 |
|
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: 191.58 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklRRDLQ 355
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03259 76 MVFQDY--ALFPHLTVAENI--AFGLKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
276-494 |
1.04e-57 |
|
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: 191.55 E-value: 1.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLR 351
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RD-LQMVFQDPTqsLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:cd03255 81 RRhIGFVFQSFN--LLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRdFADYVMVMQKGEV 494
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-258 |
1.10e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 193.13 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 4 HLLEVRNLSVDFHTVTG-----TVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPgkiTSGEILLDGKDL 78
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGII--EP---TSGEILINGHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 79 LKMSAEARrevnGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRL-FKRVAL-PDAeraLDKYPHEF 156
Cdd:COG4167 78 EYGDYKYR----CKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFAtLRLVGLlPEH---ANFYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVE 236
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 2087084196 237 SGTVRDVYRNPQHAYTKKLIAA 258
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIES 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-258 |
1.56e-57 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 192.22 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTgtvhaVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidMPPG-KITSGEILLDGKDLlkmsae 84
Cdd:PRK10418 5 IELRNIALQAAQPL-----VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI--LPAGvRQTAGRVLLDGKPV------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGISTTQAQ-AEALRlfkRVALPDAERALDKYPHEFSGGQRQR 163
Cdd:PRK10418 72 APCALRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATlTAALE---AVGLENAARVLKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|....*
gi 2087084196 244 YRNPQHAYTKKLIAA 258
Cdd:PRK10418 229 FNAPKHAVTRSLVSA 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
278-511 |
1.29e-56 |
|
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: 189.47 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 278 VKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDLQMV 357
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDptQSLNPRMTVYQLISEAWIIHP--EILPKAKWRERVGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALALEP 434
Cdd:cd03296 80 FQH--YALFRHMTVFDNVAFGLRVKPrsERPPEAEIRAKVHELLKLVQLDwLAD--RYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPY 511
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
5-259 |
2.28e-56 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 189.64 E-value: 2.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI----------LgesgsgksvsssaiMNLI--DMPPgkiTSGEIL 72
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIvgesgsgkstL--------------LKCLyfDLAP---TSGSVY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 LDGK-----DLLKMSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGI-STTQAQAEALRLFKRVALPdAE 146
Cdd:COG4107 71 YRDRdggprDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGErHYGDIRARALEWLERVEIP-LE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RaLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRV 226
Cdd:COG4107 150 R-IDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRT 228
|
250 260 270
....*....|....*....|....*....|...
gi 2087084196 227 VVMEKGQLVESGTVRDVYRNPQHAYTKKLIAAA 259
Cdd:COG4107 229 MVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-507 |
1.71e-55 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 190.28 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDLQ 355
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQLISeawiiHP-EI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:COG3839 79 MVFQSY--ALYPHMTVYENIA-----FPlKLrkVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHD----LPLvrdfADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-503 |
1.78e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.80 E-value: 1.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRR 352
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDPtqSLNPRMTVYQ---------------LISeawiihpeILPKAkWRERVGELLGQVGLsLEHMGRYPHQFS 417
Cdd:COG3638 81 RIGMIFQQF--NLVPRLSVLTnvlagrlgrtstwrsLLG--------LFPPE-DRERALEALERVGL-ADKAYQRADQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 418 GGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVEL 497
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFD 228
|
....*.
gi 2087084196 498 GTVAQV 503
Cdd:COG3638 229 GPPAEL 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-248 |
4.77e-55 |
|
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: 185.09 E-value: 4.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGsgksvsssA-------IMNLIDMPpgkiTSGEILLDGKD 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSG--------AgkstlirCINGLERP----TSGSVLVDGTD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 78 LLKMSAEARREVNgRRIAMIFQdplsHLNPVY--TVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERAldkYPHE 155
Cdd:cd03258 69 LTLLSGKELRKAR-RRIGMIFQ----HFNLLSsrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADA---YPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
250
....*....|...
gi 2087084196 236 ESGTVRDVYRNPQ 248
Cdd:cd03258 221 EEGTVEEVFANPQ 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
276-508 |
1.22e-54 |
|
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: 184.24 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQ 355
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQ----LISEawiiHpEILPKAKWRERVGELLGQVGLSLEHmGRYPHQFSGGQRQRIAIARALA 431
Cdd:cd03261 81 MLFQSG--ALFDSLTVFEnvafPLRE----H-TRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF--DNPQ 508
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
276-508 |
2.55e-54 |
|
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: 183.21 E-value: 2.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklRRDLQ 355
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDptQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03300 76 TVFQN--YALFPHLTVFENI--AFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-495 |
4.14e-54 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 190.23 E-value: 4.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaiMN------LIdmppgKI-------TS 68
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLG-------------ENgagkstLM-----KIlsgvyqpDS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGKDLLKMS-AEARRevngRRIAMIFQDP--LSHLnpvyTVG---WQMREALKTHGISTTQAQAEALRLFKRVAL 142
Cdd:COG1129 59 GEILLDGEPVRFRSpRDAQA----AGIAIIHQELnlVPNL----SVAeniFLGREPRRGGLIDWRAMRRRARELLARLGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 P-DAERALDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDvtvQAEV---LALLKELqRETGMGVLIITHDLGV 218
Cdd:COG1129 131 DiDPDTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASLT---EREVerlFRIIRRL-KAQGVAIIYISHRLDE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 219 VSEVADRVVVMEKGQLVESGTVRDVYRNpqhaytkKLIAAAPGKgEM-----HEPEAQGEPILSVKDARKSygdfEALKG 293
Cdd:COG1129 203 VFEIADRVTVLRDGRLVGTGPVAELTED-------ELVRLMVGR-ELedlfpKRAAAPGEVVLEVEGLSVG----GVVRD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 294 VSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL--------RRdlqmvfqdpTQSL 365
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayvpedRK---------GEGL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTVYQ---LISEAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:COG1129 342 VLDLSIREnitLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 443 VSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
277-493 |
4.89e-54 |
|
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: 181.51 E-value: 4.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 277 SVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDL 354
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDP-TQSLNPrmTVYQLISeawiIHPEIL--PKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALA 431
Cdd:cd03225 78 GLVFQNPdDQFFGP--TVEEEVA----FGLENLglPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGE 493
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
275-496 |
5.74e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 181.79 E-value: 5.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRD 353
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDptQSLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALE 433
Cdd:COG2884 81 IGVVFQD--FRLLPDRTVYENVALPLRVTG--KSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKeMGIAfIFIA-HDLPLVRDFADYVMVMQKGEVVE 496
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINR-RGTT-VLIAtHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
276-494 |
7.27e-54 |
|
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: 181.19 E-value: 7.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKLRRDLQ 355
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTqsLNPRMTVYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03262 80 MVFQQFN--LFPHLTVLENITLA-PIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-538 |
3.49e-53 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 183.40 E-value: 3.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKS--TLArILLRLEEPDGGTAH---WKGKDLFTMSPg 345
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSLA-IMGLIDYPGRVMAEkleFNGQDLQRISE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 346 dlfKLRR-----DLQMVFQDPTQSLNPRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLS--LEHMGRYPHQFSG 418
Cdd:PRK11022 81 ---KERRnlvgaEVAMIFQDPMTSLNPCYTVGFQIMEAIKVH-QGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 419 GQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2087084196 499 TVAQVFDNPQKPYTQALLAASldpdPDVqaANRNARLASV 538
Cdd:PRK11022 237 KAHDIFRAPRHPYTQALLRAL----PEF--AQDKARLASL 270
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
276-503 |
6.88e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.49 E-value: 6.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfKLRRDLQ 355
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:COG1131 77 YVPQEP--ALYPDLTVRENLRFFARLYG--LPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-263 |
5.09e-52 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 180.38 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNlIDMPPGKITSGEILLDGKDLLKMSAE 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALK--THGISTTQA----QAEALRLFKRVALPDAERALDKYPHEFSG 158
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPgwTYKGRWWQRfgwrKRRAIELLHRVGIKDHKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 159 GQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260
....*....|....*....|....*
gi 2087084196 239 TVRDVYRNPQHAYTKKLIAAAPGKG 263
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIPDFG 266
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
276-493 |
5.77e-52 |
|
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: 175.07 E-value: 5.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpGDLFKLRRDLQ 355
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQliseawiihpeilpkakwrervgellgQVGLSLehmgryphqfSGGQRQRIAIARALALEPQ 435
Cdd:cd03229 80 MVFQDF--ALFPHLTVLE---------------------------NIALGL----------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGE 493
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-518 |
6.55e-52 |
|
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: 177.54 E-value: 6.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDL 354
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPTqsLNPRMTVYQLISEAWIIHPEIL--PKAKWRERVGELLGQVGLslEHM-GRYPHQFSGGQRQRIAIARALA 431
Cdd:COG1120 78 AYVPQEPP--APFGLTVRELVALGRYPHLGLFgrPSAEDREAVEEALERTGL--EHLaDRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFdnpqkpy 511
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL------- 226
|
....*..
gi 2087084196 512 TQALLAA 518
Cdd:COG1120 227 TPELLEE 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
274-525 |
1.14e-51 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 184.52 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDA----RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRL------EEPdGGTAHWKGKDLFTMS 343
Cdd:PRK15134 4 PLLAIENLsvafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYP-SGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 344 PGDLFKLRRD-LQMVFQDPTQSLNPRMTVYQLISEAWIIHPEILPKAKwRERVGELLGQVGL--SLEHMGRYPHQFSGGQ 420
Cdd:PRK15134 83 EQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAA-RGEILNCLDRVGIrqAAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 421 RQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTV 500
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260
....*....|....*....|....*
gi 2087084196 501 AQVFDNPQKPYTQALLAASLDPDPD 525
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLNSEPSGDPV 266
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-236 |
1.71e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 175.62 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI----------LgesgsgksvsssaiMNLI---DMPpgkiTSGEI 71
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIvgpsgsgkstL--------------LNILgglDRP----TSGEV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 72 LLDGKDLLKMSAEARREVNGRRIAMIFQDPlsHLNPVYTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALpdAER 147
Cdd:COG1136 66 LIDGQDISSLSERELARLRRRHIGFVFQFF--NLLPELTA----LEnvalPLLLAGVSRKERRERARELLERVGL--GDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 aLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLgVVSEVADRVV 227
Cdd:COG1136 138 -LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVI 215
|
....*....
gi 2087084196 228 VMEKGQLVE 236
Cdd:COG1136 216 RLRDGRIVS 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-503 |
4.85e-51 |
|
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: 174.29 E-value: 4.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEE-----PDGGTAHWKGKDLFTMSPgDLFKL 350
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDV-DVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDPtqslNP-RMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSLEHMGR-YPHQFSGGQRQRIAIAR 428
Cdd:cd03260 80 RRRVGMVFQKP----NPfPGSIYDNVAYGLRLH-GIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 429 ALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
270-507 |
5.22e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 175.28 E-value: 5.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 270 AQGEPILSVKDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFtmspg 345
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 346 dlfKLRRDLQMVFQDPTqsLNPRMTVYQLIseawIIHPEI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQR 423
Cdd:COG1116 77 ---GPGPDRGVVFQEPA--LLPWLTVLDNV----ALGLELrgVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLP----LvrdfADYVMVMQKGEvvelGT 499
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfL----ADRVVVLSARP----GR 218
|
....*...
gi 2087084196 500 VAQVFDNP 507
Cdd:COG1116 219 IVEEIDVD 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-495 |
5.42e-51 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 182.15 E-value: 5.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILgesgsgksvsssaimnlidmppG----------KI---- 66
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALL----------------------GengagkstlmKIlygl 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 ---TSGEILLDGKDL-LKMSAEARRevngRRIAMIFQDPLshLNPVYTV------GwqmREALKTHGISTTQAQAEALRL 136
Cdd:COG3845 55 yqpDSGEILIDGKPVrIRSPRDAIA----LGIGMVHQHFM--LVPNLTVaenivlG---LEPTKGGRLDRKAARARIREL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 137 FKRVALP-DaeraLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALdvTVQ--AEVLALLKELqRETGMGVLIIT 213
Cdd:COG3845 126 SERYGLDvD----PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRL-AAEGKSIIFIT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 214 HDLGVVSEVADRVVVMEKGQLVESGTVRDVyrnpqhayTKKLIAA-----APGKGEMHEPEAQGEPILSVKD--ARKSYG 286
Cdd:COG3845 199 HKLREVMAIADRVTVLRRGKVVGTVDTAET--------SEEELAElmvgrEVLLRVEKAPAEPGEVVLEVENlsVRDDRG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DfEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklRRDLQMVF--QDP-TQ 363
Cdd:COG3845 271 V-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRLGVAYipEDRlGR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 SLNPRMTVYQ-LI---------SEAWIIHpeilpKAKWRERVGELlgqvglslehMGRY------PHQ----FSGGQRQR 423
Cdd:COG3845 346 GLVPDMSVAEnLIlgryrrppfSRGGFLD-----RKAIRAFAEEL----------IEEFdvrtpgPDTparsLSGGNQQK 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
273-520 |
8.15e-51 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 174.63 E-value: 8.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKD-----LFTMSPGDL 347
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 348 FKL-RRDLQMVFQDPTQSLNPRMTVYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAI 426
Cdd:TIGR02323 81 RRLmRTEWGFVHQNPRDGLRMRVSAGANIGER-LMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 427 ARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDN 506
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
250
....*....|....
gi 2087084196 507 PQKPYTQALLAASL 520
Cdd:TIGR02323 240 PQHPYTQLLVSSIL 253
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-254 |
3.63e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.49 E-value: 3.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAIlgesgsgksvsssaI-------------MNLIDMPpgkiTSGEI 71
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVI--------------IgpsgsgkstllrcINLLEEP----DSGTI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 72 LLDGKDLLKMSAEAR--RevngRRIAMIFQdplsHLN--PVYTVGWQMREAL-KTHGISTTQAQAEALRLFKRVALpdAE 146
Cdd:COG1126 59 TVDGEDLTDSKKDINklR----RKVGMVFQ----QFNlfPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGL--AD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRV 226
Cdd:COG1126 129 KA-DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRV 206
|
250 260
....*....|....*....|....*...
gi 2087084196 227 VVMEKGQLVESGTVRDVYRNPQHAYTKK 254
Cdd:COG1126 207 VFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
276-511 |
4.38e-50 |
|
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: 172.10 E-value: 4.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlFKLRRDL 354
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDptQSLNPRMTVYQLISeawiIHPEIL--PKAKWRERVGELLGQVGL-SLEHMGRYPHQFSGGQRQRIAIARALA 431
Cdd:cd03295 78 GYVIQQ--IGLFPHMTVEENIA----LVPKLLkwPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPY 511
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
276-522 |
6.30e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 172.61 E-value: 6.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDlfTMSPGDLFKLRRD 353
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTqslNprmtvyQLIseAWIIHPEI--------LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIA 425
Cdd:TIGR04520 79 VGMVFQNPD---N------QFV--GATVEDDVafglenlgVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 426 IARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFD 505
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
250
....*....|....*..
gi 2087084196 506 NPQKpytqaLLAASLDP 522
Cdd:TIGR04520 226 QVEL-----LKEIGLDV 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
276-495 |
3.35e-49 |
|
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: 170.06 E-value: 3.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDL 354
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPtqSLNPRMTVYQLI-------SEAWIIHPEILPKAKwRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIA 427
Cdd:cd03256 81 GMIFQQF--NLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEE-KQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
286-521 |
6.38e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 172.01 E-value: 6.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 286 GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGG-TA---HWKGKDLFTMSPGDLFKL-RRDLQMVFQD 360
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHvTAdrfRWNGIDLLKLSPRERRKIiGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 361 PTQSLNPRMTVYQLISEA---WIIHPEILPKAKWR-ERVGELLGQVGLSlEH---MGRYPHQFSGGQRQRIAIARALALE 433
Cdd:COG4170 98 PSSCLDPSAKIGDQLIEAipsWTFKGKWWQRFKWRkKRAIELLHRVGIK-DHkdiMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQ 513
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTK 256
|
....*...
gi 2087084196 514 ALLAASLD 521
Cdd:COG4170 257 ALLRSMPD 264
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-259 |
1.13e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.52 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAIlgesgsgksvsssaI-------------MNLIDMPpgkiTSGEILL 73
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGV--------------IgasgagkstlircINLLERP----TSGRVLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 74 DGKDLLKMSAEARREVNgRRIAMIFQdplsHLNPV--YTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdAERAlDK 151
Cdd:PRK11153 65 DGQDLTALSEKELRKAR-RQIGMIFQ----HFNLLssRTVFDNVALPLELAGTPKAEIKARVTELLELVGL--SDKA-DR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 152 YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEK 231
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA 216
|
250 260
....*....|....*....|....*...
gi 2087084196 232 GQLVESGTVRDVYRNPQHAYTKKLIAAA 259
Cdd:PRK11153 217 GRLVEQGTVSEVFSHPKHPLTREFIQST 244
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-507 |
1.61e-47 |
|
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: 164.57 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfklr 351
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 rDLQMVFQDPtqSLNPRMTVYQLISeawiIHPEI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARA 429
Cdd:cd03293 74 -DRGYVFQQD--ALLPWLTVLDNVA----LGLELqgVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLplvrD----FADYVMVMQKGEvvelGTVAQVFD 505
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI----DeavfLADRVVVLSARP----GRIVAEVE 217
|
..
gi 2087084196 506 NP 507
Cdd:cd03293 218 VD 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
240-511 |
2.37e-47 |
|
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: 165.89 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 240 VRDVY----RNPQHAYtkKLIAAAPGKGEMHepeaqgepilsvkdarKSYGDFEALKGVSFDLKQGETVAVVGESGSGKS 315
Cdd:cd03294 3 IKGLYkifgKNPQKAF--KLLAKGKSKEEIL----------------KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 316 TLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRR-DLQMVFQdpTQSLNPRMTVyqLISEAWIIHPEILPKAKWRER 394
Cdd:cd03294 65 TLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQ--SFALLPHRTV--LENVAFGLEVQGVPRAEREER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 395 VGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIA 473
Cdd:cd03294 141 AAEALELVGLEgWEH--KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFIT 218
|
250 260 270
....*....|....*....|....*....|....*...
gi 2087084196 474 HDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPY 511
Cdd:cd03294 219 HDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-505 |
2.86e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.88 E-value: 2.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFtmspgdlfKLRR 352
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDPTQSLNPRMTVYQLISEAWIIHPEIL--PKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:COG1121 76 RIGYVPQRAEVDWDFPITVRDVVLMGRYGRRGLFrrPSRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGeVVELGTVAQVFD 505
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
276-498 |
4.65e-47 |
|
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: 163.19 E-value: 4.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDLQ 355
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDptQSLNPRMTVYQLISEAWIIHpeILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03301 76 MVFQN--YALYPHMTVYDNIAFGLKLR--KVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
276-508 |
7.80e-47 |
|
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: 163.28 E-value: 7.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEaLKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfkLRRDLQ 355
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-----EKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDptQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03299 75 YVPQN--YALFPHMTVYKNI--AYGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
8.00e-47 |
|
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: 162.66 E-value: 8.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAI-----------LgesgsgksvsssAIMNLIDMPpgkiTSGEILLD 74
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIvgpsgsgkstlL------------NILGGLDRP----TSGEVRVD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEARREVNGRRIAMIFQDPlsHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAeraLDKYPH 154
Cdd:cd03255 65 GTDISKLSEKELAAFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDR---LNHYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvADRVVVMEKGQL 234
Cdd:cd03255 140 ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
276-508 |
8.97e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 8.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDL-FT--MSPGDLFKLRR 352
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdFSqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDptQSLNPRMTVYQLISEA--WIIHpeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:COG4161 83 KVGMVFQQ--YNLWPHLTVMENLIEApcKVLG---LSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLrKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTvAQVFDNPQ 508
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
276-508 |
1.17e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.26 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDL-FTMSPGD--LFKLRR 352
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdFSKTPSDkaIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDptQSLNPRMTVYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK11124 83 NVGMVFQQ--YNLWPHLTVQQNLIEA-PCRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRkEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTvAQVFDNPQ 508
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
276-494 |
4.54e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 4.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDLQ 355
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTQslnPRMTVYQLISEAWIIHPEILPkakwRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:COG4619 78 YVPQEPAL---WGGTVRDNLPFPFQLRERKFD----RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
260-503 |
7.76e-46 |
|
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: 171.17 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 260 PGKGEMHEPEAQGEpiLSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK 337
Cdd:COG2274 460 EGRSKLSLPRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 338 DLFTMSPGDlfkLRRDLQMVFQDPTQ---SL-------NPRMTVYQLISEAWI--IHPEI--LPKaKWRERVGEllgqvg 403
Cdd:COG2274 538 DLRQIDPAS---LRRQIGVVLQDVFLfsgTIrenitlgDPDATDEEIIEAARLagLHDFIeaLPM-GYDTVVGE------ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 404 lslehMGRyphQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfA 483
Cdd:COG2274 608 -----GGS---NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-A 676
|
250 260
....*....|....*....|
gi 2087084196 484 DYVMVMQKGEVVELGTVAQV 503
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEEL 696
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
276-520 |
1.20e-45 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 160.90 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGD--------- 346
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 347 -LFKLRRDLQMVFQDptQSLNPRMTVYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIA 425
Cdd:PRK10619 86 qLRLLRTRLTMVFQH--FNLWSHMTVLENVMEA-PIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 426 IARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFD 505
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|....*
gi 2087084196 506 NPQKPYTQALLAASL 520
Cdd:PRK10619 242 NPQSPRLQQFLKGSL 256
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-251 |
1.71e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 163.35 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaimnlidmpP---GK------------ 65
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLG--------------------PsgcGKttllrmiagfet 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 66 ITSGEILLDGKDLLKMSAEARRevngrrIAMIFQD----PlsHLnpvyTVgwqmRE----ALKTHGISTTQAQAEALRLF 137
Cdd:COG3842 57 PDSGRILLDGRDVTGLPPEKRN------VGMVFQDyalfP--HL----TV----AEnvafGLRMRGVPKAEIRARVAELL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 138 KRVALPDAEralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLg 217
Cdd:COG3842 121 ELVGLEGLA---DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ- 196
|
250 260 270
....*....|....*....|....*....|....*..
gi 2087084196 218 vvSE---VADRVVVMEKGQLVESGTVRDVYRNPQHAY 251
Cdd:COG3842 197 --EEalaLADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-248 |
3.43e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 158.65 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSvdfHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssaIMN-LIdmppgKITSGEILLD 74
Cdd:COG1122 1 IELENLS---FSYPGGTPALDDVSLSIEKGEFVAIigpngsgkstLLR-----------LLNgLL-----KPTSGEVLVD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEARRevngRRIAMIFQDPLSHL-NPvyTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALpdaERAL 149
Cdd:COG1122 62 GKDITKKNLRELR----RKVGLVFQNPDDQLfAP--TV----EEdvafGPENLGLPREEIRERVEEALELVGL---EHLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 DKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:COG1122 129 DRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVL 207
|
250
....*....|....*....
gi 2087084196 230 EKGQLVESGTVRDVYRNPQ 248
Cdd:COG1122 208 DDGRIVADGTPREVFSDYE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-243 |
1.82e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.15 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILgesgsgksvsssAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLgpngagktttirMLLGLL-----RPTSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrRIAMIFQDPlsHLNPVYTVgwqmREAL----KTHGISTTQAQAEALRLFKRVALPDAeraLDKYPHEFSGGQR 161
Cdd:COG1131 72 RR-----RIGYVPQEP--ALYPDLTV----RENLrffaRLYGLPRKEARERIDELLELFGLTDA---ADRKVGTLSGGMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 162 QRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVR 241
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
..
gi 2087084196 242 DV 243
Cdd:COG1131 217 EL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
276-503 |
2.13e-44 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 156.94 E-value: 2.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfKLRRDLQ 355
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR----EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:COG4555 78 VLPDER--GLYDRLTVRENIRYFAELYG--LFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
273-521 |
4.71e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 157.48 E-value: 4.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGkdlFTMSPGDLFKL 350
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDP-TQSLNprMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARA 429
Cdd:PRK13635 80 RRQVGMVFQNPdNQFVG--ATVQDDV--AFGLENIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRdFADYVMVMQKGEVVELGTVAQVFDnpqk 509
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIFK---- 229
|
250
....*....|..
gi 2087084196 510 pYTQALLAASLD 521
Cdd:PRK13635 230 -SGHMLQEIGLD 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-508 |
1.06e-43 |
|
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: 154.90 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFklRRDLQ 355
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQLI--------SEAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIA 427
Cdd:cd03219 79 RTFQIP--RLFPELTVLENVmvaaqartGSGLLLARARREEREARERAEELLERVGLA-DLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRkEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
.
gi 2087084196 508 Q 508
Cdd:cd03219 235 R 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
265-514 |
2.38e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 154.81 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 265 MHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRL-EEPDG----GTAHWKGKDL 339
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPGarveGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 340 FtmSPG-DLFKLRRDLQMVFQDPtqslNP-RMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGL------------- 404
Cdd:COG1117 81 Y--DPDvDVVELRRRVGMVFQKP----NPfPKSIYDNVAYGLRLH-GIKSKSELDEIVEESLRKAALwdevkdrlkksal 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 405 SLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALD-VSVqAQVITLLDKLRKEMGIafIFIAHDLPLVRDFA 483
Cdd:COG1117 154 GL----------SGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKDYTI--VIVTHNMQQAARVS 220
|
250 260 270
....*....|....*....|....*....|.
gi 2087084196 484 DYVMVMQKGEVVELGTVAQVFDNPQKPYTQA 514
Cdd:COG1117 221 DYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
276-494 |
5.21e-43 |
|
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: 151.01 E-value: 5.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKLRRDLQ 355
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYQLIseawiihpeilpkakwrervgellgqvglslehmgryphQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03230 77 YLPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
273-496 |
8.07e-43 |
|
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: 152.59 E-value: 8.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEA----LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLF 348
Cdd:COG4181 6 APIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 KLRRD-LQMVFQDPTqsLNPRMTVYQ-----LiseawiihpEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQ 422
Cdd:COG4181 86 RLRARhVGFVFQSFQ--LLPTLTALEnvmlpL---------ELAGRRDARARARALLERVGLG-HRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 423 RIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVE 496
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-243 |
2.51e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 151.73 E-value: 2.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIdmppgKITSGEILL 73
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALlgpngsgkstlLR-----------ALAGLL-----KPSSGEVLL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 74 DGKDLLKMSAEARRevngRRIAMIFQDPLSHLNpvYTVgwqmREA--------LKTHGISTTQAQAEALRLFKRVALPD- 144
Cdd:COG1120 61 DGRDLASLSRRELA----RRIAYVPQEPPAPFG--LTV----RELvalgryphLGLFGRPSAEDREAVEEALERTGLEHl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERALDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVAD 224
Cdd:COG1120 131 ADRPVD----ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYAD 206
|
250
....*....|....*....
gi 2087084196 225 RVVVMEKGQLVESGTVRDV 243
Cdd:COG1120 207 RLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
291-442 |
6.05e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.41 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDLQMVFQDPTqsLNPRMT 370
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 371 VYQLISEAWIIhpEILPKAKWRERVGELLGQVGLSL---EHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:pfam00005 76 VRENLRLGLLL--KGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-242 |
7.21e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 150.99 E-value: 7.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDF--HTVTGTVHA---VRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidmppGKITSGEILLDGKDLL 79
Cdd:PRK10419 3 LLNVSGLSHHYahGGLSGKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-----ESPSQGNVSWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 80 KMSAEARREVNgRRIAMIFQDPLSHLNPVYTVGWQMREALKtH--GISTTQAQAEALRLFKRVALPDAEraLDKYPHEFS 157
Cdd:PRK10419 78 KLNRAQRKAFR-RDIQMVFQDSISAVNPRKTVREIIREPLR-HllSLDKAERLARASEMLRAVDLDDSV--LDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 158 GGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVES 237
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
....*
gi 2087084196 238 GTVRD 242
Cdd:PRK10419 234 QPVGD 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
276-516 |
7.63e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.91 E-value: 7.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEalkgVSFDL--KQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRD 353
Cdd:COG3840 2 LRLDDLTYRYGDFP----LRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-----RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDptQSLNPRMTVYQLISEAwiIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALE 433
Cdd:COG3840 73 VSMLFQE--NNLFPHLTVAQNIGLG--LRPGLKLTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQ 513
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
...
gi 2087084196 514 ALL 516
Cdd:COG3840 228 AYL 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
278-520 |
8.36e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.29 E-value: 8.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 278 VKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSP-----GDLFKLRR 352
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkGLIRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDptQSLNPRMTVYQLISEAWIIHPEIlPKAKWRERVGELLGQVGLSLEHmGRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK11264 86 HVGFVFQN--FNLFPHRTVLENIIEGPVIVKGE-PKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIfIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYT 512
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*...
gi 2087084196 513 QALLAASL 520
Cdd:PRK11264 241 RQFLEKFL 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
277-493 |
9.33e-42 |
|
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: 147.01 E-value: 9.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 277 SVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDLQM 356
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 357 VFQdptqslnprmtvyqliseawiihpeilpkakwrervgellgqvglslehmgryphqFSGGQRQRIAIARALALEPQL 436
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 437 IVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGE 493
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
264-507 |
1.10e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 153.56 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 264 EMHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMS 343
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 344 PGDlfklRRDLQMVFQdpTQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVglSLEHMG-RYPHQFSGGQRQ 422
Cdd:PRK09452 82 PAE----NRHVNTVFQ--SYALFPHMTVFENV--AFGLRMQKTPAAEITPRVMEALRMV--QLEEFAqRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 423 RIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
....*
gi 2087084196 503 VFDNP 507
Cdd:PRK09452 232 IYEEP 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
277-498 |
1.56e-41 |
|
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: 148.45 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 277 SVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFtmspgdlfKLRRDLQM 356
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 357 VFQDPTQSLNPRMTVYQLISEAWIIHPEIL--PKAKWRERVGELLGQVGLSleHMGRYP-HQFSGGQRQRIAIARALALE 433
Cdd:cd03235 73 VPQRRSIDRDFPISVRDVVLMGLYGHKGLFrrLSKADKAKVDEALERVGLS--ELADRQiGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMqKGEVVELG 498
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
276-493 |
1.80e-41 |
|
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: 146.76 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDF--EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRD 353
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPtqslnprmtvyQLISEAwiIHPEILpkakwrervgellgqvglslehmgryphqfSGGQRQRIAIARALALE 433
Cdd:cd03228 78 IAYVPQDP-----------FLFSGT--IRENIL------------------------------SGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDfADYVMVMQKGE 493
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
279-516 |
1.98e-41 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.09 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 279 KDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKLRRDLQMVF 358
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 QdptQ-SLNPRMTVYQLISEAwIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLI 437
Cdd:PRK09493 84 Q---QfYLFPHLTALENVMFG-PLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 438 VCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALL 516
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-256 |
3.84e-41 |
|
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: 148.20 E-value: 3.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIdmppgKITSG 69
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIiggsgsgksvlLK-----------LIIGLL-----RPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 70 EILLDGKDLLKMSAEARREVNgRRIAMIFQDP--LSHLNpVY-TVGWQMREALKthgISTTQAQAEALRLFKRVALPDAE 146
Cdd:COG1127 61 EILVDGQDITGLSEKELYELR-RRIGMLFQGGalFDSLT-VFeNVAFPLREHTD---LSEAEIRELVLEKLELVGLPGAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 ralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALD-VTVqAEVLALLKELQRETGMGVLIITHDLGVVSEVADR 225
Cdd:COG1127 136 ---DKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADR 211
|
250 260 270
....*....|....*....|....*....|.
gi 2087084196 226 VVVMEKGQLVESGTVRDVyRNPQHAYTKKLI 256
Cdd:COG1127 212 VAVLADGKIIAEGTPEEL-LASDDPWVRQFL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-238 |
4.02e-41 |
|
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: 147.28 E-value: 4.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE-----RPDSGEILIDGRDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrrIAMIFQDP--LSHLnpvyTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQR 163
Cdd:cd03259 72 RN------IGMVFQDYalFPHL----TVAENIAFGLKLRGVPKAEIRARVRELLELVGL---EGLLNRYPHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-247 |
2.21e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.77 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILgesgsgksvsssaIMNLI---DMPpgkiTSGEILLDGKD 77
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVgpsgc----gkstLLRLIaglEKP----TSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 78 LLKMsaearrevnGRRIAMIFQDPLshLNPVYTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALPDAEralDKYP 153
Cdd:COG1116 75 VTGP---------GPDRGVVFQEPA--LLPWLTV----LDnvalGLELRGVPKAERRERARELLELVGLAGFE---DAYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDV----TVQAEVLallkELQRETGMGVLIITHDlgvVSE---VADRV 226
Cdd:COG1116 137 HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELL----RLWQETGKTVLFVTHD---VDEavfLADRV 209
|
250 260
....*....|....*....|.
gi 2087084196 227 VVMEKGqlveSGTVRDVYRNP 247
Cdd:COG1116 210 VVLSAR----PGRIVEEIDVD 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
2.51e-40 |
|
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: 144.98 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAImNLIDmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLE----EPDSGTIIIDGLKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREVngRRIAMIFQDplSHLNPVYTVGWQMREAL-KTHGISTTQAQAEALRLFKRVALPDaeRAlDKYPHEFSGGQRQRV 164
Cdd:cd03262 72 NELR--QKVGMVFQQ--FNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLAD--KA-DAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-495 |
1.17e-39 |
|
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: 141.41 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfKLRRDLQ 355
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVfqdptqslnprmtvyqliseawiihpeilpkakwrervgellgqvglslehmgrypHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03216 79 MV--------------------------------------------------------YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-256 |
1.83e-39 |
|
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: 144.71 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 19 TGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEARREVNGRRIAMIF 98
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI-----EPTSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 99 QD--PLSHLNPVYTVGWqmreALKTHGISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQRVMIAMALALKPDL 176
Cdd:cd03294 109 QSfaLLPHRTVLENVAF----GLEVQGVPRAEREERAAEALELVGLEGWE---HKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 177 LIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-258 |
2.04e-39 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 144.55 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTG-----TVHAVRNISYYLDRGETLAILGESGSGKSvsssaimNLIDMPPGKI--TSGEILLDGKD 77
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKS-------TLAKMLAGMIepTSGELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 78 LLKMSAEARREvngrRIAMIFQDPLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVA--LPDAeraLDKYPHE 155
Cdd:PRK15112 77 LHFGDYSYRSQ----RIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVglLPDH---ASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 2087084196 236 ESGTVRDVYRNPQHAYTKKLIAA 258
Cdd:PRK15112 230 ERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-247 |
9.14e-39 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 141.07 E-value: 9.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGesgsgksvsssaimnlidmPPG--------------KITSGEI 71
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVG-------------------PSGcgkstllriiagleRPTSGEV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 72 LLDGKdllkmsaearrEVNG--RRIAMIFQDPlsHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAEral 149
Cdd:cd03293 62 LVDGE-----------PVTGpgPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFE--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 DKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:cd03293 126 NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
250
....*....|....*...
gi 2087084196 230 EKgqlvESGTVRDVYRNP 247
Cdd:cd03293 206 SA----RPGRIVAEVEVD 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
283-507 |
1.05e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.84 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 283 KSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDLQMVFQDpt 362
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVGFVFQH-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 QSLNPRMTVYQLISEAWIIHP--EILPKAKWRERVGELLGQVglSLEHM-GRYPHQFSGGQRQRIAIARALALEPQLIVC 439
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVLPrrERPNAAAIKAKVTQLLEMV--QLAHLaDRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 440 DEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
277-498 |
1.11e-38 |
|
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: 139.49 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 277 SVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRrdlqm 356
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 357 vfqdptqslnprmtvyqliseAWIihPEILpkakwrERVGellgqvglsLEHM-GRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03214 76 ---------------------AYV--PQAL------ELLG---------LAHLaDRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
259-499 |
1.14e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.16 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 259 APGKGEMHEPEAQGEpiLSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK 337
Cdd:COG1132 325 PDPPGAVPLPPVRGE--IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 338 DLFTMSPGDLfklRRDLQMVFQDP---TQSL-------NPRMTVYQLISEAWI--IHPEI--LPKaKWRERVGELlgqvG 403
Cdd:COG1132 403 DIRDLTLESL---RRQIGVVPQDTflfSGTIrenirygRPDATDEEVEEAAKAaqAHEFIeaLPD-GYDTVVGER----G 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 404 LSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfA 483
Cdd:COG1132 475 VNL----------SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-A 541
|
250
....*....|....*.
gi 2087084196 484 DYVMVMQKGEVVELGT 499
Cdd:COG1132 542 DRILVLDDGRIVEQGT 557
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
274-512 |
1.64e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 144.98 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfkLRRD 353
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-----YQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQdpTQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARALALE 433
Cdd:PRK11607 93 INMMFQ--SYALFPHMTVEQNI--AFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 434 PQLIVCDEAVSALDVSV----QAQVITLLDKLrkemGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQK 509
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
...
gi 2087084196 510 PYT 512
Cdd:PRK11607 244 RYS 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
279-499 |
1.64e-38 |
|
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: 140.83 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 279 KDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDLQMV 357
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPT----------QSLNPRMTVYQLI--SEAWIIHPEI--LPKaKWRERVGELlgqvGLSLehmgryphqfSGGQRQR 423
Cdd:cd03253 81 PQDTVlfndtigyniRYGRPDATDEEVIeaAKAAQIHDKImrFPD-GYDTIVGER----GLKL----------SGGEKQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-243 |
2.50e-38 |
|
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: 140.33 E-value: 2.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPgkiTSGEILLDGKDLLKMSAEA 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL--RP---DSGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREVnGRRIAMIFQDP--LSHLNPVYTVGWQMRE--ALKTHGIstTQAQAEALRLfkrVALPDAEralDKYPHEFSGGQR 161
Cdd:cd03261 72 LYRL-RRRMGMLFQSGalFDSLTVFENVAFPLREhtRLSEEEI--REIVLEKLEA---VGLRGAE---DLYPAELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 162 QRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVR 241
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
..
gi 2087084196 242 DV 243
Cdd:cd03261 223 EL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
269-521 |
3.21e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 141.43 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 269 EAQGEPILSVKDARKSYGDFEA--LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlfTMSPGD 346
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 347 LFKLRRDLQMVFQDPTQSLNPRMTVYQLiseAWIIHPEILPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAI 426
Cdd:PRK13648 78 FEKLRKHIGIVFQNPDNQFVGSIVKYDV---AFGLENHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 427 ARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDN 506
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
250
....*....|....*
gi 2087084196 507 pqkpyTQALLAASLD 521
Cdd:PRK13648 233 -----AEELTRIGLD 242
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
278-500 |
4.48e-38 |
|
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: 139.43 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 278 VKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKLRRDLQMV 357
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPtqSLNPRMTVYqlisEAWIIHPEI--LPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03265 79 FQDL--SVDDELTGW----ENLYIHARLygVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTV 500
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
290-506 |
4.61e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 140.99 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDlfTMSPGDLFKLRRDLQMVFQDPTQSLnprm 369
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 370 tVYQLISEAWIIHPEIL--PKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALD 447
Cdd:PRK13633 99 -VATIVEEDVAFGPENLgiPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 448 VSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDN 506
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-520 |
4.99e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 140.05 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEE--PDG---GTAHWKGKDLFTMspgDLFKL 350
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKM---DVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDPTQSlnPRMTVYQLISEAWIIHPEILPKAKWRERVGELLGQVGLSLE---HMGRYPHQFSGGQRQRIAIA 427
Cdd:PRK14247 81 RRRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEvkdRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
250
....*....|...
gi 2087084196 508 QKPYTQALLAASL 520
Cdd:PRK14247 237 RHELTEKYVTGRL 249
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-233 |
6.08e-38 |
|
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: 138.75 E-value: 6.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSvdFHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssaIMNLIdmppGKITSGEILLDGK 76
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIvgpngsgkstLLR-----------LLNGL----LGPTSGEVLVDGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 77 DLLKMSAEARRevngRRIAMIFQDPLSHL-NPvyTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALPDAeraLDK 151
Cdd:cd03225 64 DLTKLSLKELR----RKVGLVFQNPDDQFfGP--TV----EEevafGLENLGLPEEEIEERVEEALELVGLEGL---RDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 152 YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEK 231
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLED 209
|
..
gi 2087084196 232 GQ 233
Cdd:cd03225 210 GK 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-503 |
6.75e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.55 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRr 352
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 dLQMVFQDPtqSLNPRMTVYQ------LISEAWIIHpeilpKAKWRERVGELLGQVGLSL---EHMGRYphqfSGGQRQR 423
Cdd:COG1129 81 -IAIIHQEL--NLVPNLSVAEniflgrEPRRGGLID-----WRAMRRRARELLARLGLDIdpdTPVGDL----SVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDvsvQAQVITLLDKLR--KEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVA 501
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVA 225
|
..
gi 2087084196 502 QV 503
Cdd:COG1129 226 EL 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
280-511 |
1.03e-37 |
|
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: 142.17 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 280 DARKSYGDFEaLKgVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPG-DLFKLRRDLQMVF 358
Cdd:TIGR02142 4 RFSKRLGDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 QDPtqSLNPRMTVYQ-LISEAWIIHPEiLPKAKWrERVGELLGqvglsLEHM-GRYPHQFSGGQRQRIAIARALALEPQL 436
Cdd:TIGR02142 82 QEA--RLFPHLSVRGnLRYGMKRARPS-ERRISF-ERVIELLG-----IGHLlGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 437 IVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPY 511
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-256 |
3.51e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.67 E-value: 3.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaimnlidmpP---GKIT------------SGE 70
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLG--------------------PsgsGKTTllriiagletpdSGR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 71 ILLDGKDLLkmsaeARREVNGRRIAMIFQDPL--SHLnpvyTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALPD 144
Cdd:COG1118 59 IVLNGRDLF-----TNLPPRERRVGFVFQHYAlfPHM----TV----AEniafGLRVRPPSKAEIRARVEELLELVQLEG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AEralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVAD 224
Cdd:COG1118 126 LA---DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELAD 202
|
250 260 270
....*....|....*....|....*....|..
gi 2087084196 225 RVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:COG1118 203 RVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-508 |
5.10e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.29 E-value: 5.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKLRRD 353
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDP-TQSLNPrmTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK13639 80 VGIVFQNPdDQLFAP--TVEEDV--AFGPLNLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-256 |
6.05e-37 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 140.37 E-value: 6.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 19 TGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMppgkiTSGEILLDGKDLLKMSAEARREVNGRRIAMIF 98
Cdd:TIGR01186 3 TGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEP-----TAGQIFIDGENIMKQSPVELREVRRKKIGMVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 99 QDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQRVMIAMALALKPDLLI 178
Cdd:TIGR01186 78 QQ--FALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYE---HRYPDELSGGMQQRVGLARALAAEPDILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 179 ADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:TIGR01186 153 MDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
273-508 |
1.07e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.04 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlfTMSPGDLFKL 350
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDP-TQSLNprMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARA 429
Cdd:PRK13632 82 RKKIGIIFQNPdNQFIG--ATVEDDI--AFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
280-507 |
2.18e-36 |
|
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: 138.70 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 280 DARKSYGDFeALKgVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPG-DLFKLRRDLQMVF 358
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 QDPtqSLNPRMTVYQLISEAWIIHPEILPKAKWrERVGELLGqvglsLEH-MGRYPHQFSGGQRQRIAIARALALEPQLI 437
Cdd:COG4148 84 QEA--RLFPHLSVRGNLLYGRKRAPRAERRISF-DEVVELLG-----IGHlLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 438 VCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
287-499 |
2.19e-36 |
|
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: 135.36 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDLQMVFQDPT---- 362
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQIGLVSQEPVlfdg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 -------QSLNPRmTVYQLISEAWI--IHPEIlpkAKWRERVGELLGQVGLSLehmgryphqfSGGQRQRIAIARALALE 433
Cdd:cd03249 92 tiaenirYGKPDA-TDEEVEEAAKKanIHDFI---MSLPDGYDTLVGERGSQL----------SGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
280-498 |
2.81e-36 |
|
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: 134.34 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 280 DARKSYGDFEaLKgVSFDLKqGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPG-DLFKLRRDLQMVF 358
Cdd:cd03297 5 DIEKRLPDFT-LK-IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 QDPTqsLNPRMTVYQLISEAWIIHPEilpkAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIV 438
Cdd:cd03297 82 QQYA--LFPHLNVRENLAFGLKRKRN----REDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 439 CDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-236 |
4.71e-36 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 134.02 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLiDMPpgkiTSGEILLDGKDLLKMSAE 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGL-DNP----TSGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNGRRIAMIFQdpLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQRV 164
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVsEVADRVVVMEKGQLVE 236
Cdd:TIGR02211 151 AIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEMKDGQLFN 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-233 |
6.09e-36 |
|
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: 131.93 E-value: 6.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLlkMSAEA 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDL--TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREVNGRRIAMIFQDPLshLNPVYTVgwqmrealkthgisttqaqaealrlFKRVALPdaeraldkypheFSGGQRQRVM 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDFA--LFPHLTV-------------------------LENIALG------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 166 IAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-243 |
8.54e-36 |
|
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: 133.46 E-value: 8.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDL--LKMSA 83
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIydLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EARRevngRRIAMIFQDPlshlNPV-YTVGWQMREALKTHGISTTQAQAEALR-LFKRVALPDaeRALDK-YPHEFSGGQ 160
Cdd:cd03260 77 LELR----RRVGMVFQKP----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWD--EVKDRlHALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtgMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTV 240
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 2087084196 241 RDV 243
Cdd:cd03260 225 EQI 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
55-248 |
1.22e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.22 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 55 IMNLIDMPpgkiTSGEILLDGK--DL-----LKMSAEARREVngrriAMIFQDplSHLNPVYTVGWQMREA-LKTHGIST 126
Cdd:PRK11124 47 VLNLLEMP----RSGTLNIAGNhfDFsktpsDKAIRELRRNV-----GMVFQQ--YNLWPHLTVQQNLIEApCRVLGLSK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 127 TQAQAEALRLFKRVALpdAERAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETG 206
Cdd:PRK11124 116 DQALARAEKLLERLRL--KPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETG 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087084196 207 MGVLIITHDLGVVSEVADRVVVMEKGQLVESGTvRDVYRNPQ 248
Cdd:PRK11124 192 ITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-258 |
1.28e-35 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 133.90 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLID--MPPgkiTSGEILLDGK-- 76
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKT----TLLNALSarLAP---DAGEVHYRMRdg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 77 ---DLLKMSAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGIST-TQAQAEALRLFKRVALpDAERaLDKY 152
Cdd:PRK11701 71 qlrDLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEI-DAAR-IDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 153 PHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKG 232
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|....*.
gi 2087084196 233 QLVESGTVRDVYRNPQHAYTKKLIAA 258
Cdd:PRK11701 229 RVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-248 |
1.93e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 132.83 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 20 GTVHAVRNISYYLDRGETLAILGESGSGKSVSSSaIMNLIDMPpgkiTSGEILLDGKDL---LKMSAEARREVNgRRIAM 96
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETP----DSGQLNIAGHQFdfsQKPSEKAIRLLR-QKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 97 IFQDplSHLNPVYTVGWQMREA-LKTHGISTTQAQAEALRLFKRVALPDAeraLDKYPHEFSGGQRQRVMIAMALALKPD 175
Cdd:COG4161 87 VFQQ--YNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDK---ADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 176 LLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVrDVYRNPQ 248
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-248 |
2.03e-35 |
|
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: 132.56 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAIlgesgsgksvsssaI----------MNLI--DMPPgkiTSGEILL 73
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGL--------------IgpngagkttlFNLIsgFLRP---TSGSVLF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 74 DGKDLLKMSAearREVNGRRIAMIFQDP---------------LSHLNPVYTVGWQMREALKthgisttQAQAEALRLFK 138
Cdd:cd03219 60 DGEDITGLPP---HEIARLGIGRTFQIPrlfpeltvlenvmvaAQARTGSGLLLARARREER-------EARERAEELLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 139 RVALpdAERAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGV 218
Cdd:cd03219 130 RVGL--ADLA-DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDV 205
|
250 260 270
....*....|....*....|....*....|
gi 2087084196 219 VSEVADRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:cd03219 206 VMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
276-506 |
2.18e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 132.17 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfkLRRDLQ 355
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDptQSLNPRMTVYQ-LISEAWIIHPEilpKAKWR-ERV-------GELLGQVGLSLehmgryphqfSGGQRQRIAI 426
Cdd:cd03224 79 YVPEG--RRIFPELTVEEnLLLGAYARRRA---KRKARlERVyelfprlKERRKQLAGTL----------SGGEQQMLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 427 ARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDN 506
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
65-238 |
2.27e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKMSaeaRREVNG--RRIAMIFQDP--LSHLNpVYtvgwqmrE----ALKTHGISTTQAQAEALRL 136
Cdd:COG2884 53 RPTSGQVLVNGQDLSRLK---RREIPYlrRRIGVVFQDFrlLPDRT-VY-------EnvalPLRVTGKSRKEIRRRVREV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 137 FKRVALPDAEralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQReTGMGVLIITHDL 216
Cdd:COG2884 122 LDLVGLSDKA---KALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDL 197
|
170 180
....*....|....*....|..
gi 2087084196 217 GVVSEVADRVVVMEKGQLVESG 238
Cdd:COG2884 198 ELVDRMPKRVLELEDGRLVRDE 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
306-516 |
2.78e-35 |
|
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: 134.93 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 306 VVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklRRDLQMVFQdpTQSLNPRMTVYQLIseAWIIHPEI 385
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQ--SYALFPHMTVEENV--AFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 386 LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEM 465
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 466 GIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALL 516
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
276-507 |
3.93e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.97 E-value: 3.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDL 354
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDptQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQvgLSLEHM-GRYPHQFSGGQRQRIAIARALALE 433
Cdd:PRK11650 79 AMVFQN--YALYPHMSVRENM--AYGLKIRGMPKAEIEERVAEAARI--LELEPLlDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
279-494 |
4.21e-35 |
|
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: 130.99 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 279 KDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQMV 357
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDptQSLNPRMTVYQLISEAWIIHPEilPKAKWRERVGELLGQVGLSLEHMGrYPHQFSGGQRQRIAIARALALEPQLI 437
Cdd:cd03292 84 FQD--FRLLPDRNVYENVAFALEVTGV--PPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 438 VCDEAVSALDVSVQAQVITLLDKLRKeMGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-234 |
4.95e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSvdfHTVTGTVHaVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIdmPPgkiTSGEILLD 74
Cdd:COG4619 1 LELEGLS---FRVGGKPI-LSPVSLTLEAGECVAItgpsgsgkstlLR-----------ALADLD--PP---TSGEIYLD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEARRevngRRIAMIFQDPLSHLNpvyTVGWQMREALKTHGISTTQAqaEALRLFKRVALPDAerALDKYPH 154
Cdd:COG4619 61 GKPLSAMPPPEWR----RQVAYVPQEPALWGG---TVRDNLPFPFQLRERKFDRE--RALELLERLGLPPD--ILDKPVE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:COG4619 130 RLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
128-496 |
5.89e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 137.89 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 128 QAQAEALRLFKRVALPDAEraLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDvtvqAEVLALLKE-LQRETG 206
Cdd:COG0488 127 EAEARAEEILSGLGFPEED--LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 207 mGVLIITHDLGVVSEVADRVVVMEKGQL----------VESGTVRDvyRNPQHAYTKK---------------------- 254
Cdd:COG0488 201 -TVLVVSHDRYFLDRVATRILELDRGKLtlypgnysayLEQRAERL--EQEAAAYAKQqkkiakeeefirrfrakarkak 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 255 -------------LIAAAPGKGEMH----EPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTL 317
Cdd:COG0488 278 qaqsrikalekleREEPPRRDKTVEirfpPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 318 ARILLRLEEPDGGTAHWkGKdlfTMSPGdlfklrrdlqmVF-QDpTQSLNPRMTVYQLISEAwiihpeiLPKAKwRERVG 396
Cdd:COG0488 358 LKLLAGELEPDSGTVKL-GE---TVKIG-----------YFdQH-QEELDPDKTVLDELRDG-------APGGT-EQEVR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 397 ELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV-SVQAqvitLLDKLRKEMGiAFIFIAHD 475
Cdd:COG0488 414 GYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHD 488
|
410 420
....*....|....*....|.
gi 2087084196 476 LPLVRDFADYVMVMQKGEVVE 496
Cdd:COG0488 489 RYFLDRVATRILEFEDGGVRE 509
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
290-499 |
7.07e-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: 130.69 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDLQMVFQDPT------- 362
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 QSLNPrmtvYQLISEAWIIhpEILPKAKWRERVGELLGQVGLSLEHMGRyphQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:cd03244 96 SNLDP----FGEYSDEELW--QALERVGLKEFVESLPGGLDTVVEEGGE---NLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 443 VSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFaDYVMVMQKGEVVELGT 499
Cdd:cd03244 167 TASVDPETDALIQKTIREAFKDCTV--LTIAHRLDTIIDS-DRILVLDKGRVVEFDS 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
7.40e-35 |
|
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: 129.09 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIdmppgKITSGEILLDG 75
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGIlgpngagkstlLK-----------TLAGLL-----KPSSGEILLDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 76 KDLLKMSAEARRevngRRIAMIFQdplshlnpvytvgwqmreALKTHGIsttqaqaEALrlfkrvalpdAERALDkyphE 155
Cdd:cd03214 61 KDLASLSPKELA----RKIAYVPQ------------------ALELLGL-------AHL----------ADRPFN----E 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:cd03214 98 LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
...
gi 2087084196 236 ESG 238
Cdd:cd03214 178 AQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-256 |
8.33e-35 |
|
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: 130.82 E-value: 8.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaimnlidmPPG--------------KITSGEI 71
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLG-------------------PSGcgkttllrliagfeTPTSGEI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 72 LLDGKDLLKMSAearrevNGRRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERaldK 151
Cdd:cd03300 58 LLDGKDITNLPP------HKRPVNTVFQN--YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYAN---R 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 152 YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEK 231
Cdd:cd03300 127 KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK 206
|
250 260
....*....|....*....|....*
gi 2087084196 232 GQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:cd03300 207 GKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-259 |
1.06e-34 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 131.11 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPGKITSGEILLDGK--DLLKMS 82
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRL--APDHGTATYIMRSGAelELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGIS-TTQAQAEALRLFKRVALPDAEraLDKYPHEFSGGQR 161
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhYGNIRATAQDWLEEVEIDPTR--IDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 162 QRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVR 241
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
250
....*....|....*...
gi 2087084196 242 DVYRNPQHAYTKKLIAAA 259
Cdd:TIGR02323 235 QVLDDPQHPYTQLLVSSI 252
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
1.16e-34 |
|
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: 128.28 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILgesgsgksvsssAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLgpngagkttlikIILGLL-----KPDSGEIKVLGKDIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrRIAMIFQDPlsHLNPVYTVgwqmREALKthgisttqaqaealrlfkrvalpdaeraldkypheFSGGQRQRVM 165
Cdd:cd03230 72 KR-----RIGYLPEEP--SLYENLTV----RENLK-----------------------------------LSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 166 IAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
67-248 |
1.51e-34 |
|
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: 131.42 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARREVNgRRIAMIFQDPLSHL--NPVYtvgwqmRE---ALKTHGISTTQAQAEALRLFKRVA 141
Cdd:TIGR04521 58 TSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFPEHQLfeETVY------KDiafGPKNLGLSEEEAEERVKEALELVG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 142 LPdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSE 221
Cdd:TIGR04521 131 LD--EEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAE 208
|
170 180
....*....|....*....|....*..
gi 2087084196 222 VADRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:TIGR04521 209 YADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-247 |
1.89e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.21 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 13 VDFHTVT---GTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidmppGKITSGEILLDGKDLLKMSAEARrev 89
Cdd:PRK09493 2 IEFKNVSkhfGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDER--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 90 NGRRIA-MIFQ--DPLSHLNPVYTVgwqMREALKTHGISTTQAQAEALRLFKRVALpdAERAlDKYPHEFSGGQRQRVMI 166
Cdd:PRK09493 74 LIRQEAgMVFQqfYLFPHLTALENV---MFGPLRVRGASKEEAEKQARELLAKVGL--AERA-HHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 167 AMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRN 246
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
.
gi 2087084196 247 P 247
Cdd:PRK09493 227 P 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
267-502 |
1.92e-34 |
|
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: 136.81 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 267 EPEAQGEPILSVKDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPG 345
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 346 DLfklRRDLQMVFQDPT---QSL-------NPRMT---VYQLISEAWIiHPEI--LPkAKWRERVGEllGQVGLSlehmg 410
Cdd:COG4988 408 SW---RRQIAWVPQNPYlfaGTIrenlrlgRPDASdeeLEAALEAAGL-DEFVaaLP-DGLDTPLGE--GGRGLS----- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 411 ryphqfsGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQ 490
Cdd:COG4988 476 -------GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLD 545
|
250
....*....|..
gi 2087084196 491 KGEVVELGTVAQ 502
Cdd:COG4988 546 DGRIVEQGTHEE 557
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-246 |
2.47e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 130.63 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSvdFHTVTGTVHAVRNISYYLDRGE-------------TLAILgesgsgksvsssaiMNLIDMPpgkiTSGEIL 72
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEfvaiighngsgksTLAKL--------------LNGLLLP----TSGKVT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 LDGKDLLkmSAEARREVNgRRIAMIFQDPLSHLnpvytVGWQMRE----ALKTHGISTTQAQ---AEALrlfKRVALPDA 145
Cdd:TIGR04520 61 VDGLDTL--DEENLWEIR-KKVGMVFQNPDNQF-----VGATVEDdvafGLENLGVPREEMRkrvDEAL---KLVGMEDF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 eraLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLgvvSEV--A 223
Cdd:TIGR04520 130 ---RDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDM---EEAvlA 203
|
250 260
....*....|....*....|...
gi 2087084196 224 DRVVVMEKGQLVESGTVRDVYRN 246
Cdd:TIGR04520 204 DRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
275-504 |
2.77e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 130.74 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdLFKLRRD 353
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTQSLNpRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLslEHMGRYP-HQFSGGQRQRIAIARALAL 432
Cdd:PRK13636 84 VGMVFQDPDNQLF-SASVYQDVSFGAVNLK--LPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-243 |
2.80e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvTGTVHAVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIDmppgkITSGEILL 73
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALigpsgagkstlLR-----------CLNGLVE-----PTSGEILV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 74 DGKDLLKMSAEARREVNgRRIAMIFQDPlsHLNPVYTV-------------GWQMrealkTHGISTTQAQAEALRLFKRV 140
Cdd:COG3638 63 DGQDVTALRGRALRRLR-RRIGMIFQQF--NLVPRLSVltnvlagrlgrtsTWRS-----LLGLFPPEDRERALEALERV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 141 ALpdAERALDKyPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVS 220
Cdd:COG3638 135 GL--ADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLAR 211
|
250 260
....*....|....*....|...
gi 2087084196 221 EVADRVVVMEKGQLVESGTVRDV 243
Cdd:COG3638 212 RYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
290-516 |
3.48e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 133.62 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRD-LQMVFQdpTQSLNPR 368
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQ--SFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 369 MTVyqLISEAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGrYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV 448
Cdd:PRK10070 121 MTV--LDNTAFGMELAGINAEERREKALDALRQVGLENYAHS-YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 449 SVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALL 516
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-500 |
3.92e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 135.15 E-value: 3.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 272 GEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLR 351
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 rdLQMVFQDPtqSLNPRMTVYQ---LISEAWiiHPEILPKAKWRERVGELLGQVGLSLEhMGRYPHQFSGGQRQRIAIAR 428
Cdd:COG3845 82 --IGMVHQHF--MLVPNLTVAEnivLGLEPT--KGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 429 ALALEPQLIVCDEAVSALdvSVQ--AQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVelGTV 500
Cdd:COG3845 155 ALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV--GTV 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
286-521 |
5.24e-34 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 131.46 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 286 GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDggtahWK-GKDLFTMSPGDLFKL----RRDL-----Q 355
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN-----WRvTADRMRFDDIDLLRLspreRRKLvghnvS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTQSLNPRMTV-YQLISEAwiihPEILPKAKWRERVG-------ELLGQVGLSlEH---MGRYPHQFSGGQRQRI 424
Cdd:PRK15093 93 MIFQEPQSCLDPSERVgRQLMQNI----PGWTYKGRWWQRFGwrkrraiELLHRVGIK-DHkdaMRSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 425 AIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
250
....*....|....*..
gi 2087084196 505 DNPQKPYTQALLAASLD 521
Cdd:PRK15093 248 TTPHHPYTQALIRAIPD 264
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
290-499 |
6.31e-34 |
|
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: 128.11 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDPT------- 362
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQDTFlfsgtim 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 -----QSLNPRMTVYQLISEAWIIHPEI--LPKakwrervgellgqvGLsLEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03254 95 enirlGRPNATDEEVIEAAKEAGAHDFImkLPN--------------GY-DTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-236 |
1.23e-33 |
|
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: 127.55 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSgksvsssaimnlidmppGK------------ITS 68
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGS-----------------GKstllgllagldrPTS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGKDLLKMSAEARREVNGRRIAMIFQDplSHLNPVYT----VGWQMREAlkthgiSTTQAQAEALRLFKRVALpd 144
Cdd:COG4181 67 GTVRLAGQDLFALDEDARARLRARHVGFVFQS--FQLLPTLTalenVMLPLELA------GRRDARARARALLERVGL-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERaLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGvVSEVAD 224
Cdd:COG4181 137 GHR-LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCD 214
|
250
....*....|..
gi 2087084196 225 RVVVMEKGQLVE 236
Cdd:COG4181 215 RVLRLRAGRLVE 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-247 |
1.24e-33 |
|
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: 127.80 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmpPgkiTSGEILLDGKDLLKMSAEA 85
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE--P---TSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERAlDKYPHEFSGGQRQRVM 165
Cdd:cd03295 73 LR----RKIGYVIQQ--IGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFA-DRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 166 IAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYR 245
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
..
gi 2087084196 246 NP 247
Cdd:cd03295 226 SP 227
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-247 |
7.85e-33 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 128.62 E-value: 7.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLiDMPpgkiTSGEILLDGKDLLKMSAEA 85
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-ERQ----TAGTIYQGGRDITRLPPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrrIAMIFQdplSH-LNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERaldKYPHEFSGGQRQRV 164
Cdd:TIGR03265 76 RD------YGIVFQ---SYaLFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSER---KYPGQLSGGQQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVY 244
Cdd:TIGR03265 144 ALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
...
gi 2087084196 245 RNP 247
Cdd:TIGR03265 224 RHP 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-508 |
8.36e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 125.48 E-value: 8.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL-- 350
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 ------RRdlqmVFqdptqslnPRMTVYQ-LISEAWIIHPEilPKAKWR-ERV-------GELLGQVGLSLehmgryphq 415
Cdd:COG0410 81 gyvpegRR----IF--------PSLTVEEnLLLGAYARRDR--AEVRADlERVyelfprlKERRRQRAGTL--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 416 fSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:COG0410 138 -SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIV 215
|
250
....*....|...
gi 2087084196 496 ELGTVAQVFDNPQ 508
Cdd:COG0410 216 LEGTAAELLADPE 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
275-507 |
8.90e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.46 E-value: 8.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRD 353
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPT-QSLNPrmTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK13652 80 VGLVFQNPDdQIFSP--TVEQDIAFGPINLG--LDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
290-502 |
1.05e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 132.77 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDLQMVFQdptqslNPRM 369
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVRRQLGVVLQ------NGRL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 370 ---TVYQLIseawIIHPEILPKAKWrervgELLGQVGLSlEHMGRYPHQF-----------SGGQRQRIAIARALALEPQ 435
Cdd:TIGR03797 539 msgSIFENI----AGGAPLTLDEAW-----EAARMAGLA-EDIRAMPMGMhtvisegggtlSGGQRQRLLIARALVRKPR 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRkemgIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQ 502
Cdd:TIGR03797 609 ILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
289-499 |
1.18e-32 |
|
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: 124.91 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDLQMVFQDPT------ 362
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQVGVVLQENVlfnrsi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 ----QSLNPRMTVYQLISEAWI--IHPEILpkaKWRERVGELLGQVGLSLehmgryphqfSGGQRQRIAIARALALEPQL 436
Cdd:cd03252 93 rdniALADPGMSMERVIEAAKLagAHDFIS---ELPEGYDTIVGEQGAGL----------SGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 437 IVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-244 |
1.27e-32 |
|
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: 125.10 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSAE 84
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE-----PSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNgRRIAMIFQD-----PLSHLNPV------YTVGWQMrealkTHGISTTQAQAEALRLFKRVALpdAERALDKyP 153
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQHynlieRLTVLENVlhgrlgYKPTWRS-----LLGRFSEEDKERALSALERVGL--ADKAYQR-A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:TIGR02315 144 DQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
250
....*....|.
gi 2087084196 234 LVESGTVRDVY 244
Cdd:TIGR02315 224 IVFDGAPSELD 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-256 |
1.50e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.03 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLKMSAEA 85
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDPlshlNPVYTVGWQMREALkthGISTTQAQAEALRLFKRV--ALPDAE------RALDKYPHEFS 157
Cdd:PRK14247 80 LR----RRVQMVFQIP----NPIPNLSIFENVAL---GLKLNRLVKSKKELQERVrwALEKAQlwdevkDRLDAPAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 158 GGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtgMGVLIITHDLGVVSEVADRVVVMEKGQLVES 237
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
250
....*....|....*....
gi 2087084196 238 GTVRDVYRNPQHAYTKKLI 256
Cdd:PRK14247 227 GPTREVFTNPRHELTEKYV 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
291-504 |
1.50e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDLQMVFQDPTQSLnPRMT 370
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVFQNPDNQF-VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSV 450
Cdd:PRK13650 99 VEDDV--AFGLENKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 451 QAQVITLLDKLRKEMGIAFIFIAHDLPLVRdFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-251 |
2.01e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADhlLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaimnlidmPPG--------------KI 66
Cdd:COG3839 1 MAS--LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLG-------------------PSGcgkstllrmiagleDP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngrrIAMIFQDPLshLNPVYTVgwqmRE----ALKTHGISTTQAQ------AEALRL 136
Cdd:COG3839 56 TSGEILIGGRDVTDLPPKDRN------IAMVFQSYA--LYPHMTV----YEniafPLKLRKVPKAEIDrrvreaAELLGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 137 fkrvalpdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDL 216
Cdd:COG3839 124 ---------EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
250 260 270
....*....|....*....|....*....|....*...
gi 2087084196 217 gvvSEV---ADRVVVMEKGQLVESGTVRDVYRNPQHAY 251
Cdd:COG3839 195 ---VEAmtlADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
56-248 |
3.04e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.53 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 56 MNLIDMPpgkiTSGEILLDGKDL-LKMSAEARREVNGR--------RIAMIFQ--DPLSHLnpvyTVGWQMREA-LKTHG 123
Cdd:COG4598 54 INLLETP----DSGEIRVGGEEIrLKPDRDGELVPADRrqlqrirtRLGMVFQsfNLWSHM----TVLENVIEApVHVLG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 124 ISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQR 203
Cdd:COG4598 126 RPKAEAIERAEALLAKVGLADKR---DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087084196 204 EtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:COG4598 203 E-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
274-475 |
3.16e-32 |
|
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: 122.97 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKLRRD 353
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPtqSLNPRMTVYQLISeawiIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALE 433
Cdd:COG4133 77 LAYLGHAD--GLKPELTVRENLR----FWAALYGLRADREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAfIFIAHD 475
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQ 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-248 |
3.97e-32 |
|
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: 123.60 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSV---DFHtvtgtvhaVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMS 82
Cdd:cd03299 1 LKVENLSKdwkEFK--------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI-----KPDSGKILLNGKDITNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARRevngrrIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQ 162
Cdd:cd03299 68 PEKRD------ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRD 242
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
....*.
gi 2087084196 243 VYRNPQ 248
Cdd:cd03299 217 VFKKPK 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
273-513 |
4.53e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.73 E-value: 4.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEE--PD---GGTAHWKGKDLFtmSP-GD 346
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIY--SPrTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 347 LFKLRRDLQMVFQDPtqslNP-RMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSLEHMGRYpHQ----FSGGQR 421
Cdd:PRK14239 81 TVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLK-GIKDKQVLDEAVEKSLKGASIWDEVKDRL-HDsalgLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 422 QRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVMQKGEVVELGTVA 501
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
250
....*....|..
gi 2087084196 502 QVFDNPQKPYTQ 513
Cdd:PRK14239 233 QMFMNPKHKETE 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
288-509 |
7.02e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.36 E-value: 7.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 288 FE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWkGKDLFT--MSPGDLFKLRRDLQMVFQDPTq 363
Cdd:PRK13634 18 FErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagKKNKKLKPLRKKVGIVFQFPE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 slnprmtvYQLISEAwiIHPEI--------LPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:PRK13634 96 --------HQLFEET--VEKDIcfgpmnfgVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQK 509
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
274-495 |
7.08e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 130.23 E-value: 7.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSY----GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFK 349
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 350 LRRD-LQMVFQDptqslnprmtvYQLISEAWIIH----PEI---LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQR 421
Cdd:PRK10535 83 LRREhFGFIFQR-----------YHLLSHLTAAQnvevPAVyagLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 422 QRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRkEMGIAFIFIAHDlPLVRDFADYVMVMQKGEVV 495
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-251 |
7.42e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIdmppgKITSG 69
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIvgpngagkstlLK-----------AILGLL-----PPTSG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 70 EILLDGKDLLKmsaearrevNGRRIAMIFQD-------PLShlnpVY-TVGWQMREALKTHGISTTQAQAEALRLFKRVA 141
Cdd:COG1121 62 TVRLFGKPPRR---------ARRRIGYVPQRaevdwdfPIT----VRdVVLMGRYGRRGLFRRPSRADREAVDEALERVG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 142 LPD-AERALDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVS 220
Cdd:COG1121 129 LEDlADRPIG----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVR 203
|
250 260 270
....*....|....*....|....*....|...
gi 2087084196 221 EVADRVVVMEKGqLVESGTVRDVYR--NPQHAY 251
Cdd:COG1121 204 EYFDRVLLLNRG-LVAHGPPEEVLTpeNLSRAY 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-520 |
1.04e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 128.36 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSaIMNLIDMPpgkiTSGEILLDGKDLLK 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMK-VLSGIHEP----TKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEARREVNgrrIAMIFQ-----DPLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHE 155
Cdd:PRK09700 72 LDHKLAAQLG---IGIIYQelsviDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALdvtVQAEV---LALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKG 232
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdylFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 233 QLVESGTVRDVY----------RNPQHAYTkkliAAAPGKGEMhepeaQGEPILSVKDARKSygDFEALKGVSFDLKQGE 302
Cdd:PRK09700 222 SSVCSGMVSDVSnddivrlmvgRELQNRFN----AMKENVSNL-----AHETVFEVRNVTSR--DRKKVRDISFSVCRGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 303 TVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL--------RRDLQMVfqdPTQSLNPRMTVYQL 374
Cdd:PRK09700 291 ILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayitesRRDNGFF---PNFSIAQNMAISRS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 375 ISE-----AW-IIHPEilPKAKWRERVGELLGQVGLSLEhmgRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV 448
Cdd:PRK09700 368 LKDggykgAMgLFHEV--DEQRTAENQRELLALKCHSVN---QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 449 SVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEvvelgtVAQVFDNPQKPYTQALLAASL 520
Cdd:PRK09700 443 GAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR------LTQILTNRDDMSEEEIMAWAL 507
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-243 |
1.36e-31 |
|
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: 122.27 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAE 84
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL-----KPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARRevngrRIAMIFQDPlsHLNPVYTVgwqmREALK----THGISTTQAQAEALRLFKRVALPDAeraLDKYPHEFSGGQ 160
Cdd:COG4555 72 ARR-----QIGVLPDER--GLYDRLTV----RENIRyfaeLYGLFDEELKKRIEELIELLGLEEF---LDRRVGELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTV 240
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
...
gi 2087084196 241 RDV 243
Cdd:COG4555 217 DEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
68-247 |
1.63e-31 |
|
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: 124.83 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARREVNGRRIAMIFQDPlsHLNPVYTVGWQMREALKTHGISTTQAQAEALrlfkrVALPDAER 147
Cdd:COG4148 53 SGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA--RLFPHLSVRGNLLYGRKRAPRAERRISFDEV-----VELLGIGH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 ALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVV 227
Cdd:COG4148 126 LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVV 205
|
170 180
....*....|....*....|
gi 2087084196 228 VMEKGQLVESGTVRDVYRNP 247
Cdd:COG4148 206 LLEQGRVVASGPLAEVLSRP 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
255-502 |
2.26e-31 |
|
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: 127.96 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 255 LIAAAPGKGEMHEPE-AQGEPILSVKDARKSY--GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT 331
Cdd:COG4987 312 LLDAPPAVTEPAEPApAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 332 AHWKGKDLFTMSPGDlfkLRRDLQMVFQDP---TQSL--NPRMTvyqliseawiihpeiLPKAKwRERVGELLGQVGL-- 404
Cdd:COG4987 392 ITLGGVDLRDLDEDD---LRRRIAVVPQRPhlfDTTLreNLRLA---------------RPDAT-DEELWAALERVGLgd 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 405 ---SLEH-----MGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDL 476
Cdd:COG4987 453 wlaALPDgldtwLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRL 530
|
250 260
....*....|....*....|....*.
gi 2087084196 477 PLVrDFADYVMVMQKGEVVELGTVAQ 502
Cdd:COG4987 531 AGL-ERMDRILVLEDGRIVEQGTHEE 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
287-504 |
2.33e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.97 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGG-------TAHWKGKDLFtmspgdLFKLRRDLQMVFQ 359
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvddiTITHKTKDKY------IRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 360 DPTQslnprmtvyQLISEAwiIHPEIL--PK------AKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALA 431
Cdd:PRK13646 93 FPES---------QLFEDT--VEREIIfgPKnfkmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-251 |
3.42e-31 |
|
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: 120.91 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLiDMPpgkiTSGEILLDGKDLLKMSAea 85
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERP----DSGTILFGGEDATDVPV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 rREvngRRIAMIFQD--PLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQR 163
Cdd:cd03296 72 -QE---RNVGFVFQHyaLFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQL---DWLADRYPAQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
....*...
gi 2087084196 244 YRNPQHAY 251
Cdd:cd03296 225 YDHPASPF 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-256 |
4.30e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISyyLD--RGETLAIlgesgsgksvsssaI-------------MN-LIDMPPGKITSG 69
Cdd:COG1117 12 IEVRNLNVYY----GDKQALKDIN--LDipENKVTAL--------------IgpsgcgkstllrcLNrMNDLIPGARVEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 70 EILLDGKDLL--KMSAEARRevngRRIAMIFQDPlshlNP---------VYtvgwqmreALKTHGISTTQAQAE----AL 134
Cdd:COG1117 72 EILLDGEDIYdpDVDVVELR----RRVGMVFQKP----NPfpksiydnvAY--------GLRLHGIKSKSELDEiveeSL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 135 RlfkRVALPD--AERaLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtgMGVLII 212
Cdd:COG1117 136 R---KAALWDevKDR-LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2087084196 213 THDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:COG1117 210 THNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
68-235 |
5.68e-31 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 119.74 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARREVNgRRIAMIFQdplSH-LNPVYTVGWQMREALKTH-GISTTQAQAEALRLFKRVALpda 145
Cdd:TIGR02982 59 EGSLKVLGQELHGASKKQLVQLR-RRIGYIFQ---AHnLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGL--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDlGVVSEVADR 225
Cdd:TIGR02982 132 GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADR 210
|
170
....*....|
gi 2087084196 226 VVVMEKGQLV 235
Cdd:TIGR02982 211 ILQMEDGKLL 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
289-509 |
6.17e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 121.69 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKLRRDLQMVFQDPTqslnpr 368
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 369 mtvYQLISEAwiIHPEI--------LPKAKWRERVGELLGQVGLSLEHM-GRYPHQFSGGQRQRIAIARALALEPQLIVC 439
Cdd:PRK13637 94 ---YQLFEET--IEKDIafgpinlgLSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 440 DEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQK 509
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
296-498 |
7.28e-31 |
|
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: 119.13 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 296 FDLK--QGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDLQMVFQDptQSLNPRMTVYQ 373
Cdd:cd03298 17 FDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQE--NNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 374 LISEAwiIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQ 453
Cdd:cd03298 90 NVGLG--LSPGLKLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087084196 454 VITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-256 |
7.73e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 120.24 E-value: 7.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTgtvhAVRNISYYLDRGETLAILGESGSGKSVSSSAImNLIDMP-PGKITSGEILLDGKDLLKMSAE 84
Cdd:PRK11264 4 IEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPeAGTIRVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNgRRIAMIFQDplSHLNPVYTVGWQMREA-LKTHGISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQR 163
Cdd:PRK11264 79 LIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVlIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMV-IVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
250
....*....|...
gi 2087084196 244 YRNPQHAYTKKLI 256
Cdd:PRK11264 232 FADPQQPRTRQFL 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
161-494 |
1.46e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 124.78 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALdvtVQAEVLALLKELQ--RETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 239 TVRD------------VYRNPQHAYTKKLIAAAPGKgemHEPEAQGEPILSVKDARKsygdfEALKGVSFDLKQGETVAV 306
Cdd:PRK15439 223 KTADlstddiiqaitpAAREKSLSASQKLWLELPGN---RRQQAAGAPVLTVEDLTG-----EGFRNISLEVRAGEILGL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 307 VGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGD-----LFKLRRDLQM--VFQDPTQSLNPRMTVYQLISeaW 379
Cdd:PRK15439 295 AGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlargLVYLPEDRQSsgLYLDAPLAWNVCALTHNRRG--F 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 380 IIHPeilpkAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLD 459
Cdd:PRK15439 373 WIKP-----ARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIR 447
|
330 340 350
....*....|....*....|....*....|....*
gi 2087084196 460 KLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PRK15439 448 SIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
276-503 |
1.56e-30 |
|
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: 118.78 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfKLRRDLQ 355
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDptQSLNPRMTVY---QLISEAwiihpeiLPKAKwRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:TIGR03410 79 YVPQG--REIFPRLTVEenlLTGLAA-------LPRRS-RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
275-508 |
1.58e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRR 352
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDPTQSLnprmtVYQLISE--AWIIHPEILPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:PRK13640 85 KVGIVFQNPDNQF-----VGATVGDdvAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVrDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-503 |
1.70e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.60 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKL---- 350
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIgylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 --RrdlqmvfqdptqSLNPRMTVY-QLISEAwiihpEI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIA 425
Cdd:COG4152 78 eeR------------GLYPKMKVGeQLVYLA-----RLkgLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 426 IARALALEPQLIVCDEAVSALD-VSVQaqviTLLDKLR--KEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpVNVE----LLKDVIRelAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
.
gi 2087084196 503 V 503
Cdd:COG4152 216 I 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-520 |
1.72e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.56 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEE--PDG---GTAHWKGKDLFTMSPgDLFKL 350
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDV-DPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDPTQSlnPRMTVYQLISEAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGR---YPHQFSGGQRQRIAIA 427
Cdd:PRK14267 84 RREVGMVFQYPNPF--PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
250
....*....|...
gi 2087084196 508 QKPYTQALLAASL 520
Cdd:PRK14267 240 EHELTEKYVTGAL 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
282-505 |
1.74e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.03 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 282 RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlftMSPgdLFklrrDLQMVFqdp 361
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSA--LL----ELGAGF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 362 tqslNPRMTVYQLIseawiihpeilpkakwrervgELLGQV-GLSLEHM-------------GRYPHQ----FSGGQRQR 423
Cdd:COG1134 100 ----HPELTGRENI---------------------YLNGRLlGLSRKEIdekfdeivefaelGDFIDQpvktYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 424 IAIARALALEPQ-LIVcDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:COG1134 155 LAFAVATAVDPDiLLV-DEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
...
gi 2087084196 503 VFD 505
Cdd:COG1134 233 VIA 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
276-505 |
1.90e-30 |
|
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: 118.87 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRD 353
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDP-----TQSLN-----PRMTVYQLISEAWIIHP----EILPkakwrERVGELLGQVGLSLehmgryphqfSGG 419
Cdd:cd03251 78 IGLVSQDVflfndTVAENiaygrPGATREEVEEAARAANAhefiMELP-----EGYDTVIGERGVKL----------SGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 420 QRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
....*.
gi 2087084196 500 VAQVFD 505
Cdd:cd03251 220 HEELLA 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
287-513 |
2.07e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 119.38 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEE-------PDGGTAHWkGKDLFTMspgDLFKLRRDLQMVFQ 359
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskikVDGKVLYF-GKDIFQI---DAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 360 DPTQSlnPRMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGLSLEHMGRY---PHQFSGGQRQRIAIARALALEPQL 436
Cdd:PRK14246 98 QPNPF--PHLSIYDNIAYPLKSH-GIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 437 IVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQ 513
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-245 |
2.38e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.73 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSvdFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLdgkdllk 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 mSAEARREVNgRRIAMIFQDPLSHLnpvytVGWQMRE----ALKTHGISTTQAQAEALRLFKRVALPDAeraLDKYPHEF 156
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPDNQF-----VGATVQDdvafGLENIGVPREEMVERVDQALRQVGMEDF---LNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvADRVVVMEKGQLVE 236
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
....*....
gi 2087084196 237 SGTVRDVYR 245
Cdd:PRK13635 221 EGTPEEIFK 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
291-502 |
2.44e-30 |
|
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: 125.32 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDLQMVFQDpTQSLNprMT 370
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQD-TVLFN--DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLI-------SEAWI--------IHPEI--LPKaKWRERVGELlgqvGLSLehmgryphqfSGGQRQRIAIARALALE 433
Cdd:COG5265 448 IAYNIaygrpdaSEEEVeaaaraaqIHDFIesLPD-GYDTRVGER----GLKL----------SGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQ 502
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAE 578
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-232 |
2.86e-30 |
|
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: 117.63 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA- 85
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL-----KPTSGSIRVFGKPLEKERKRIg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 ----RREVNgrriamiFQDPLSHLNPVYTVGWQMREALKTHGISTTQAQAEALrlfKRVALPD-AERALDkyphEFSGGQ 160
Cdd:cd03235 72 yvpqRRSID-------RDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEAL---ERVGLSElADRQIG----ELSGGQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKG 232
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
149-488 |
2.93e-30 |
|
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: 124.90 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 149 LDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVV 228
Cdd:COG1245 206 LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 229 M--EKGQLvesGTVRDVY--RNPQHAYTKKLIAA-------APGKGEMHEP--EAQGEPILSVKDARKSYGDFEaLKGVS 295
Cdd:COG1245 285 LygEPGVY---GVVSKPKsvRVGINQYLDGYLPEenvrirdEPIEFEVHAPrrEKEEETLVEYPDLTKSYGGFS-LEVEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 296 FDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlftMSpgdlFKlrrdlqmvfqdPtQSLNP--RMTVYQ 373
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----IS----YK-----------P-QYISPdyDGTVEE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 374 LISEAwiiHPEILPKAKWRERVGEllgqvGLSLEH-MGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQA 452
Cdd:COG1245 421 FLRSA---NTDDFGSSYYKTEIIK-----PLGLEKlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
330 340 350
....*....|....*....|....*....|....*.
gi 2087084196 453 QVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMV 488
Cdd:COG1245 493 AVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
290-499 |
3.08e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 124.69 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDPtqslnprM 369
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNIAVVFQDA-------G 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 370 TVYQLISEAWII------HPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAV 443
Cdd:PRK13657 420 LFNRSIEDNIRVgrpdatDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 444 SALDVSVQAQVITLLDKLRKEMgIAFIfIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGR-TTFI-IAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
289-480 |
4.09e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.99 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLR-RDLQMVFQdpTQSLNP 367
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 368 RMTVYQLISEAWIIHPEilPKAKWRERVGELLGQVGLslEHMGRY-PHQFSGGQRQRIAIARALALEPQLIVCDEAVSAL 446
Cdd:PRK11629 101 DFTALENVAMPLLIGKK--KPAEINSRALEMLAAVGL--EHRANHrPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|....
gi 2087084196 447 DVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVR 480
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-184 |
5.16e-30 |
|
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: 114.67 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 25 VRNISYYLDRGETLAILgesgsgksvsssaIMNLI--DMPPgkiTSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPl 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVgpnga----gkstLLKLIagLLSP---TEGTILLDGQDLTDDERKSLR----KEIGYVFQDP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 103 sHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPD-AERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADE 181
Cdd:pfam00005 69 -QLFPRLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 2087084196 182 PTT 184
Cdd:pfam00005 148 PTA 150
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
271-494 |
1.34e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 117.09 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 271 QGEPILsVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGtahwkgkDLFTMSpGDLFKL 350
Cdd:PRK11247 9 QGTPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGT-APLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQDptQSLNPRMTVyqliseawIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:PRK11247 80 REDTRLMFQD--ARLLPWKKV--------IDNVGLGLKGQWRDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
292-520 |
1.81e-29 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 116.72 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 292 KGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPdgGTAHWKGKDLFTMSPGDLFKLR-RDLQMVFQDPTQSLNPRMT 370
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPCALRgRKIATIMQNPRSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLISEAWiihpEILPKAKWRERVGELLGQVGLSLEH--MGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV 448
Cdd:PRK10418 98 MHTHARETC----LALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 449 SVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQKPYTQALLAASL 520
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHL 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
291-509 |
3.53e-29 |
|
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: 115.26 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfklrrDLQMVFQDptQSLNPRMT 370
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP--------DRMVVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLISEAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSV 450
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 451 QAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV-FDNPQK 509
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
276-502 |
3.94e-29 |
|
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: 114.52 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKLRRD 353
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTqsLNPRMTVYQLIseawIIHPEI--LPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALA 431
Cdd:cd03263 77 LGYCPQFDA--LFDELTVREHL----RFYARLkgLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-240 |
4.00e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.91 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLiDMPpgkiTSGEILLDGKDLLKMSAE 84
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTP----TSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNGRRIAMIFQdpLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQRV 164
Cdd:PRK11629 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVaDRVVVMEKGQLVESGTV 240
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
291-507 |
4.70e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.75 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDLQMVFQDPtqsLNPRMT 370
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEP---VLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLISEAWIIHP--EILPKAKW---RERVGELlgQVGLSLEhMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSA 445
Cdd:TIGR00958 571 VRENIAYGLTDTPdeEIMAAAKAanaHDFIMEF--PNGYDTE-VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 446 LDVSVQAqvitLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:TIGR00958 648 LDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
276-507 |
4.94e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.90 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklRRDLQ 355
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQdpTQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALALEP 434
Cdd:PRK11432 82 MVFQ--SYALFPHMSLGENV--GYGLKMLGVPKEERKQRVKEALELVDLAgFED--RYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
277-503 |
7.76e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.80 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 277 SVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFK----LRr 352
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrlaiLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 dlqmvfQDPtqSLNPRMTVYQLISEAWIIHPEILPKAKWRERVGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALA 431
Cdd:COG4604 82 ------QEN--HINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEdLAD--RYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
290-507 |
1.54e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 114.70 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDlfTMSPGDLFKLRRDLQMVFQDPTQSLnprm 369
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGIRKLVGIVFQNPETQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 370 tVYQLISEAWIIHPE--ILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALD 447
Cdd:PRK13644 91 -VGRTVEEDLAFGPEnlCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 448 VSVQAQVITLLDKLRkEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK13644 169 PDSGIAVLERIKKLH-EKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
274-529 |
2.24e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.71 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRD 353
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LqmvfqdPTQS-LNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALA 431
Cdd:PRK13548 81 L------PQHSsLSFPFTVEEVVAMGRAPHG--LSRAEDDALVAAALAQVDLAhLAG--RDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 432 ------LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFd 505
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL- 229
|
250 260
....*....|....*....|....
gi 2087084196 506 npqkpyTQALLAASLDPDPDVQAA 529
Cdd:PRK13548 230 ------TPETLRRVYGADVLVQPH 247
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
287-504 |
2.63e-28 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 119.03 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDLQMVFQDPT---- 362
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAEL---RARMALVPQDPVlfaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 ------QSLNPRMTVYQLISEAwiihpeilPKAKWRERVGEL-------LGQVGLSLehmgryphqfSGGQRQRIAIARA 429
Cdd:TIGR02204 429 svmeniRYGRPDATDEEVEAAA--------RAAHAHEFISALpegydtyLGERGVTL----------SGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVF 504
Cdd:TIGR02204 491 ILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-494 |
3.11e-28 |
|
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: 118.00 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMN-LIDMPPGKITSGEILLDGKDLlkmSA 83
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKS----TLMKiLSGVYPHGTWDGEIYWSGSPL---KA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EARREVNGRRIAMIFQD-----PLSHL------NPVYTVGWQMREALKTHgisttqaqaEALRLFKRVALPDAERALDKy 152
Cdd:TIGR02633 70 SNIRDTERAGIVIIHQEltlvpELSVAeniflgNEITLPGGRMAYNAMYL---------RAKNLLRELQLDADNVTRPV- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 153 pHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKG 232
Cdd:TIGR02633 140 -GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 233 QLVESGTVRDVyrnpqhaYTKKLIAAAPGKgEM-----HEPEAQGEPILSVKDARKSYGDFEALK---GVSFDLKQGETV 304
Cdd:TIGR02633 218 QHVATKDMSTM-------SEDDIITMMVGR-EItslypHEPHEIGDVILEARNLTCWDVINPHRKrvdDVSFSLRRGEIL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 305 AVVGESGSGKSTLARILLRLEEPD-GGTAHWKGKDLFTMSPGDlfKLRRDLQMVFQD-PTQSLNPRMTVYQLISEAwiih 382
Cdd:TIGR02633 290 GVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQ--AIRAGIAMVPEDrKRHGIVPILGVGKNITLS---- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 383 peILPKAKWRERVGEL--LGQVGLSLEHMG-RYPHQF------SGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQ 453
Cdd:TIGR02633 364 --VLKSFCFKMRIDAAaeLQIIGSAIQRLKvKTASPFlpigrlSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2087084196 454 VITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:TIGR02633 442 IYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-494 |
3.27e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 118.11 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSgksvsssaimnlidmppGKIT------------- 67
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGA-----------------GKSTlmkvlsgvyphgt 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 -SGEILLDGKDLlkmSAEARREVNGRRIAMIFQDPLshLNPVYTVGWQM---REALKTHGISTTQAQAEALRLFKRVALp 143
Cdd:PRK13549 60 yEGEIIFEGEEL---QASNIRDTERAGIAIIHQELA--LVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 daeralDKYPH----EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVV 219
Cdd:PRK13549 134 ------DINPAtpvgNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 220 SEVADRVVVMEKGQLVesGTvrdvyRNPQHAYTKKLIAAAPGKgEM-----HEPEAQGEPILSVKD---------ARKSY 285
Cdd:PRK13549 207 KAISDTICVIRDGRHI--GT-----RPAAGMTEDDIITMMVGR-ELtalypREPHTIGEVILEVRNltawdpvnpHIKRV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 286 GDfealkgVSFDLKQGETVAVVGESGSGKSTLARILL-----RLEepdgGTAHWKGKDLFTMSPGDlfKLRRDLQMVFQD 360
Cdd:PRK13549 279 DD------VSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgRWE----GEIFIDGKPVKIRNPQQ--AIAQGIAMVPED 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 361 -PTQSLNPRMTVYQLISEAwiihpeILPKAKWRERVGEL--LGQVGLSLEHMG-RYPHQF------SGGQRQRIAIARAL 430
Cdd:PRK13549 347 rKRDGIVPVMGVGKNITLA------ALDRFTGGSRIDDAaeLKTILESIQRLKvKTASPElaiarlSGGNQQKAVLAKCL 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-243 |
3.59e-28 |
|
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: 112.66 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVdfhTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSAEA 85
Cdd:cd03256 1 IEVENLSK---TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-----PTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREVNgRRIAMIFQDPlsHLNPVYTVgwqMREALktHG----ISTTQAqaeALRLFKRVALPDAERALDK-----YPH-- 154
Cdd:cd03256 73 LRQLR-RQIGMIFQQF--NLIERLSV---LENVL--SGrlgrRSTWRS---LFGLFPKEEKQRALAALERvglldKAYqr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 --EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKG 232
Cdd:cd03256 142 adQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
250
....*....|.
gi 2087084196 233 QLVESGTVRDV 243
Cdd:cd03256 222 RIVFDGPPAEL 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-233 |
3.95e-28 |
|
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: 109.64 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIdmppgKITSGEILLDGK 76
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALvgpngsgkstLLR----------AIAGLL-----KPTSGEILIDGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 77 DLLKMSAEARRevngRRIAMIFQdplshlnpvytvgwqmrealkthgisttqaqaealrlfkrvalpdaeraldkypheF 156
Cdd:cd00267 62 DIAKLPLEELR----RRIGYVPQ--------------------------------------------------------L 81
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:cd00267 82 SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
276-498 |
4.05e-28 |
|
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: 111.60 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKlrrdlq 355
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 mvFQDPTQSLNPRMTVY-QLISEAWIihpEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEP 434
Cdd:cd03269 74 --YLPEERGLYPKMKVIdQLVYLAQL---KGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-258 |
4.10e-28 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 112.20 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLiDMPpgkiTSGEILLDGKDLLKMSAEA 85
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL-EQP----DSGRIRLNGQDATRVHARD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrrIAMIFQD--PLSHLnpvyTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQR 163
Cdd:TIGR00968 72 RK------IGFVFQHyaLFKHL----TVRDNIAFGLEIRKHPKAKIKARVEELLELVQL---EGLGDRYPNQLSGGQRQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:TIGR00968 139 VALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
250
....*....|....*
gi 2087084196 244 YRNPQHAYTKKLIAA 258
Cdd:TIGR00968 219 YDHPANPFVMSFLGE 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-253 |
4.38e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.29 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 19 TGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMppgkiTSGEILLDGKDLLKMSAEARREVNGRRIAMIF 98
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP-----TRGQVLIDGVDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 99 QDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLI 178
Cdd:PRK10070 113 QS--FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 179 ADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTK 253
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-238 |
4.95e-28 |
|
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: 111.19 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAea 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE-----EPTSGRIYIGGRDVTDLPP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 rrevNGRRIAMIFQDplSHLNPVYTVGWQMREALKTHGISttqaQAEALRLFKRVA-LPDAERALDKYPHEFSGGQRQRV 164
Cdd:cd03301 70 ----KDRDIAMVFQN--YALYPHMTVYDNIAFGLKLRKVP----KDEIDERVREVAeLLQIEHLLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
65-246 |
7.77e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 7.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKMSA---EARREVngrriAMIFQDPLSHLNPvYTVGWQMREALKTHGISTTQAQAEALRLFKRVA 141
Cdd:PRK13637 58 KPTSGKIIIDGVDITDKKVklsDIRKKV-----GLVFQYPEYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 142 LpDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSE 221
Cdd:PRK13637 132 L-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAK 210
|
170 180
....*....|....*....|....*
gi 2087084196 222 VADRVVVMEKGQLVESGTVRDVYRN 246
Cdd:PRK13637 211 LADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-520 |
7.96e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 112.05 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDG-----GTAHWKGKDLFTMSPgDLF 348
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRV-NLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 KLRRDLQMVFqdPTQSLNPrMTVYQLISEAWII---HPEI---------LPKAKWRERVGELLGQVGLSLehmgryphqf 416
Cdd:PRK14258 85 RLRRQVSMVH--PKPNLFP-MSVYDNVAYGVKIvgwRPKLeiddivesaLKDADLWDEIKHKIHKSALDL---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 417 SGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQK----- 491
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenri 231
|
250 260
....*....|....*....|....*....
gi 2087084196 492 GEVVELGTVAQVFDNPQKPYTQALLAASL 520
Cdd:PRK14258 232 GQLVEFGLTKKIFNSPHDSRTREYVLSRL 260
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
287-504 |
1.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.49 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDLQMVFQDPTQSLn 366
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL---TAENVWNLRRKIGMVFQNPDNQF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 367 PRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSAL 446
Cdd:PRK13642 95 VGATVEDDV--AFGMENQGIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 447 DVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-240 |
1.08e-27 |
|
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: 110.54 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL-----KPTSGRATVAGHDVVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrRIAMIFQDPLshLNPVYTvGWQ-MREALKTHGISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQRV 164
Cdd:cd03265 72 RR-----RIGIVFQDLS--VDDELT-GWEnLYIHARLYGVPGAERRERIDELLDFVGLLEAA---DRLVKTYSGGMRRRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTV 240
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-259 |
1.11e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.60 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVrnlsVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAImNLIDMPpgkiTSGEILLDGKDL-- 78
Cdd:PRK10619 1 MSENKLNV----IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKP----SEGSIVVNGQTInl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 79 -------LKMSAEARREVNGRRIAMIFQ--DPLSHLNPVYTVgwqMREALKTHGISTTQAQAEALRLFKRVALpdAERAL 149
Cdd:PRK10619 72 vrdkdgqLKVADKNQLRLLRTRLTMVFQhfNLWSHMTVLENV---MEAPIQVLGLSKQEARERAVKYLAKVGI--DERAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 DKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFL 225
|
250 260 270
....*....|....*....|....*....|
gi 2087084196 230 EKGQLVESGTVRDVYRNPQHAYTKKLIAAA 259
Cdd:PRK10619 226 HQGKIEEEGAPEQLFGNPQSPRLQQFLKGS 255
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
146-488 |
1.12e-27 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 117.22 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVSEVADR 225
Cdd:PRK13409 203 ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 226 VVVM--EKGQLvesGTVRDVY--RNPQHAYTKKLIAAA-------PGKGEMHEP--EAQGEPILSVKDARKSYGDF--EA 290
Cdd:PRK13409 281 VHIAygEPGAY---GVVSKPKgvRVGINEYLKGYLPEEnmrirpePIEFEERPPrdESERETLVEYPDLTKKLGDFslEV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGvsfDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTahwkgkdlftmspgdlfklrrdlqmVFQDPTQSLNPR-- 368
Cdd:PRK13409 358 EGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-------------------------VDPELKISYKPQyi 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 369 -----MTVYQLISEAwiihPEILPKAKWRERVGEllgqvGLSLEH-MGRYPHQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:PRK13409 410 kpdydGTVEDLLRSI----TDDLGSSYYKSEIIK-----PLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2087084196 443 VSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMV 488
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
291-521 |
1.48e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGD--LFKLRRDLQMVFQDPTQslnpr 368
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGNknLKKLRKKVSLVFQFPEA----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 369 mtvyQLISEAWIIHPEILPK------AKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:PRK13641 97 ----QLFENTVLKDVEFGPKnfgfseDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 443 VSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP---QKPY----TQAL 515
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlKKHYldepATSR 251
|
....*.
gi 2087084196 516 LAASLD 521
Cdd:PRK13641 252 FASKLE 257
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
233-499 |
1.60e-27 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 116.97 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 233 QLVESGTVR--DVYRNPQHAYTKKLIAAAPGkgEMHEPEAQGEpiLSVKDARKSYGDFEA--LKGVSFDLKQGETVAVVG 308
Cdd:TIGR03796 437 QELEGDLNRldDVLRNPVDPLLEEPEGSAAT--SEPPRRLSGY--VELRNITFGYSPLEPplIENFSLTLQPGQRVALVG 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 309 ESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfKLRRDLQMVFQDPTQ---SLNPRMTVYQ-LISEAWI---- 380
Cdd:TIGR03796 513 GSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPRE---VLANSVAMVDQDIFLfegTVRDNLTLWDpTIPDADLvrac 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 381 ----IHPEILpkakwrERVGELLGQvglsLEHMGRyphQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVit 456
Cdd:TIGR03796 590 kdaaIHDVIT------SRPGGYDAE----LAEGGA---NLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII-- 654
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2087084196 457 lLDKLRKEmGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:TIGR03796 655 -DDNLRRR-GCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGT 694
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-251 |
2.39e-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: 110.07 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILgesgsgksvsssAIMNLIdmppgKITSGEILLDGKDLLKMS 82
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLgrngagkttllkAISGLL-----PPRSGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AE--ARR------EvnGRRIamiFqdplSHLnpvyTVgwqmREALkthgisttQAQAEALRLFKRVAlPDAERALDKYP- 153
Cdd:COG0410 72 PHriARLgigyvpE--GRRI---F----PSL----TV----EENL--------LLGAYARRDRAEVR-ADLERVYELFPr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 -HEF--------SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVAD 224
Cdd:COG0410 126 lKERrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIAD 204
|
250 260
....*....|....*....|....*....
gi 2087084196 225 RVVVMEKGQLVESGTVRDVYRNP--QHAY 251
Cdd:COG0410 205 RAYVLERGRIVLEGTAAELLADPevREAY 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
2.39e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.32 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTvtGTVhAVRNISYYLDRGETLAILGESGSGKSVSSSAiMNLIDMPpgkiTSGEILLDGKDlLKMSAE 84
Cdd:PRK13639 1 ILETRDLKYSYPD--GTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLH-FNGILKP----TSGEVLIKGEP-IKYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREVNgRRIAMIFQDPLSHL-NPvyTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERaldKYPHEFSGGQRQR 163
Cdd:PRK13639 72 SLLEVR-KTVGIVFQNPDDQLfAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFEN---KPPHHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
....*
gi 2087084196 244 YRNPQ 248
Cdd:PRK13639 225 FSDIE 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
273-504 |
2.66e-27 |
|
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: 110.17 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEP-DGGTAHWKGKDLFTMspgDLFKLR 351
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGE---DVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RDLQMVFQDPTQSLNPRMTVYQ-LISEAW---IIHPEILPKAkwRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIA 427
Cdd:COG1119 78 KRIGLVSPALQLRFPRDETVLDvVLSGFFdsiGLYREPTDEQ--RERARELLELLGLA-HLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
276-507 |
2.92e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.25 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT--------AHWKGKDLFTMSPG-- 345
Cdd:PRK13631 27 LYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdiyiGDKKNNHELITNPYsk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 346 ---DLFKLRRDLQMVFQDPTqslnprmtvYQLISEAwiIHPEIL--------PKAKWRERVGELLGQVGLSLEHMGRYPH 414
Cdd:PRK13631 107 kikNFKELRRRVSMVFQFPE---------YQLFKDT--IEKDIMfgpvalgvKKSEAKKLAKFYLNKMGLDDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 415 QFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLdKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
250
....*....|...
gi 2087084196 495 VELGTVAQVFDNP 507
Cdd:PRK13631 255 LKTGTPYEIFTDQ 267
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-475 |
3.17e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.34 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDF----EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftMSPGdlfk 349
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGPG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 350 lrRDLQMVFQDptQSLNPRMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARA 429
Cdd:COG4525 76 --ADRGVVFQK--DALLPWLNVLDNV--AFGLRLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHD 475
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
282-498 |
3.20e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 111.72 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 282 RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFK------------ 349
Cdd:PRK13651 14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEkvleklviqktr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 350 ---------LRRDLQMVFQdptqslnprMTVYQLISEAwiIHPEIL--------PKAKWRERVGELLGQVGLSLEHMGRY 412
Cdd:PRK13651 94 fkkikkikeIRRRVGVVFQ---------FAEYQLFEQT--IEKDIIfgpvsmgvSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 413 PHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKG 492
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
....*.
gi 2087084196 493 EVVELG 498
Cdd:PRK13651 242 KIIKDG 247
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
260-499 |
3.48e-27 |
|
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: 115.58 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 260 PGKGEMHEPEAQGEpiLSVKDARKSYG--DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK 337
Cdd:TIGR02203 317 KDTGTRAIERARGD--VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 338 DLFTMSpgdLFKLRRDLQMVFQ-----DPTQSLNPRMTVYQLISEAWIIhpEILPKAKWRERVGELlgQVGLSLEhMGRY 412
Cdd:TIGR02203 395 DLADYT---LASLRRQVALVSQdvvlfNDTIANNIAYGRTEQADRAEIE--RALAAAYAQDFVDKL--PLGLDTP-IGEN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 413 PHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKG 492
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDG 543
|
....*..
gi 2087084196 493 EVVELGT 499
Cdd:TIGR02203 544 RIVERGT 550
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
67-250 |
3.69e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.46 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngrrIAMIFQDP--LSHLNpVYT-VGWQMREALKthgISTTQAQ--AEALRlfkRVA 141
Cdd:COG3840 52 DSGRILWNGQDLTALPPAERP------VSMLFQENnlFPHLT-VAQnIGLGLRPGLK---LTAEQRAqvEQALE---RVG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 142 LPDAeraLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSE 221
Cdd:COG3840 119 LAGL---LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAAR 195
|
170 180
....*....|....*....|....*....
gi 2087084196 222 VADRVVVMEKGQLVESGTVRDVYRNPQHA 250
Cdd:COG3840 196 IADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
273-492 |
7.46e-27 |
|
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: 108.68 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSY-----GD--FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT---AHWKGK-DLFT 341
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvRHDGGWvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 342 MSPGDLFKLRRD-LQMVfqdpTQSLN--PRMTVYQLISEAWIIHPEilPKAKWRERVGELLGQVGLSLEHMGRYPHQFSG 418
Cdd:COG4778 82 ASPREILALRRRtIGYV----SQFLRviPRVSALDVVAEPLLERGV--DREEARARARELLARLNLPERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 419 GQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLrKEMGIAFIFIAHDLPLVRDFADYVMVMQKG 492
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
295-476 |
7.71e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.52 E-value: 7.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 295 SFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklRRDLQMVFQDptQSLNPRMTVYQL 374
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 375 IseAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQV 454
Cdd:PRK10771 92 I--GLGLNPGLKLNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|..
gi 2087084196 455 ITLLDKLRKEMGIAFIFIAHDL 476
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSL 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
276-496 |
1.00e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 107.69 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlftmSPGDLFKLRRDLQ 355
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK-----SYQKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPtqSLNPRMTVYqlisEAWIIHPEILPKAKwrERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03268 76 ALIEAP--GFYPNLTAR----ENLRLLARLLGIRK--KRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVE 496
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
296-498 |
1.09e-26 |
|
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: 107.64 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 296 FDL--KQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfkLRRDLQMVFQDptQSLNPRMTVYQ 373
Cdd:TIGR01277 17 FDLnvADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP-----YQRPVSMLFQE--NNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 374 LISEAwiIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQ 453
Cdd:TIGR01277 90 NIGLG--LHPGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087084196 454 VITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
289-499 |
1.18e-26 |
|
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: 107.50 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDLQMVFQDPT---QSL 365
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSSLTIIPQDPTlfsGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTVYQLISEAWIIhpEILpkakwreRVGEllgqVGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSA 445
Cdd:cd03369 99 RSNLDPFDEYSDEEIY--GAL-------RVSE----GGLNL----------SQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 446 LDVSVQAqvitLLDK-LRKEM-GIAFIFIAHDLPLVRDFaDYVMVMQKGEVVELGT 499
Cdd:cd03369 156 IDYATDA----LIQKtIREEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-261 |
1.22e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.78 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLKMSAEA 85
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RrEVNgRRIAMIFQ--DPLSHLnpvyTVGWQMREALKTHGISTTQAQAEALR--LFKRVALPD-AERALDKYPHEFSGGQ 160
Cdd:PRK14267 81 I-EVR-REVGMVFQypNPFPHL----TIYDNVAIGVKLNGLVKSKKELDERVewALKKAALWDeVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtgMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTV 240
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
250 260
....*....|....*....|.
gi 2087084196 241 RDVYRNPQHAYTKKLIAAAPG 261
Cdd:PRK14267 233 RKVFENPEHELTEKYVTGALG 253
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-240 |
1.31e-26 |
|
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: 107.59 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTvtGTVHAVRNISYYLDRGETLAILGEsgsgksvsssaimN------LIDMPPG--KITSGEILLDGKD 77
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGH-------------NgagkttTLKMLTGelRPTSGTAYINGYS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 78 LLKMSAEARRevngrRIAMIFQ-DPL-SHLNPvytvgwqmREALKTH----GISTTQAQAEALRLFKRVALPDAEralDK 151
Cdd:cd03263 66 IRTDRKAARQ-----SLGYCPQfDALfDELTV--------REHLRFYarlkGLPKSEIKEEVELLLRVLGLTDKA---NK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 152 YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETgmGVLIITHDLGVVSEVADRVVVMEK 231
Cdd:cd03263 130 RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSD 207
|
....*....
gi 2087084196 232 GQLVESGTV 240
Cdd:cd03263 208 GKLRCIGSP 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-247 |
1.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 4 HLLEVRNLSvdfHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKmsa 83
Cdd:PRK13652 2 HLIETRDLC---YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL-----KPTSGSVLIRGEPITK--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EARREVNgRRIAMIFQDPLSHL-NPvyTVGWQMREALKTHGISTtqaQAEALRLFKRVALPDAERALDKYPHEFSGGQRQ 162
Cdd:PRK13652 71 ENIREVR-KFVGLVFQNPDDQIfSP--TVEQDIAFGPINLGLDE---ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRD 242
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
....*
gi 2087084196 243 VYRNP 247
Cdd:PRK13652 225 IFLQP 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
271-507 |
1.77e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.70 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 271 QGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKL 350
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQdpTQSLNPRMTVYQLIseAWIIHPEI-LPKAKWRERVGELLGQVGL--SLEHMgryPHQFSGGQRQRIAIA 427
Cdd:PRK11831 83 RKRMSMLFQ--SGALFTDMNVFDNV--AYPLREHTqLPAPLLHSTVMMKLEAVGLrgAAKLM---PSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
123-248 |
1.96e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 123 GISTTQAQAEALRLFKRVALPdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQ 202
Cdd:PRK13634 115 GVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLH 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2087084196 203 RETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:PRK13634 193 KEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
277-508 |
2.34e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.50 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 277 SVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfklrRDLQM 356
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 357 VFQdpTQSLNPRMTVYQLIS----EAWIIHPEIlpkAKWRERVGELLgQVGLSLEhmgRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK11000 80 VFQ--SYALYPHLSVAENMSfglkLAGAKKEEI---NQRVNQVAEVL-QLAHLLD---RKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
67-239 |
2.53e-26 |
|
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: 113.39 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngRRIAMIFQDP----------LSHLNPVYTVGwQMREALKthgisttqaQAEALRL 136
Cdd:COG2274 528 TSGRILIDGIDLRQIDPASLR----RQIGVVLQDVflfsgtirenITLGDPDATDE-EIIEAAR---------LAGLHDF 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 137 FKRvaLPD------AERAldkypHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVL 210
Cdd:COG2274 594 IEA--LPMgydtvvGEGG-----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVI 664
|
170 180
....*....|....*....|....*....
gi 2087084196 211 IITHDLGVVsEVADRVVVMEKGQLVESGT 239
Cdd:COG2274 665 IIAHRLSTI-RLADRIIVLDKGRIVEDGT 692
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
67-256 |
2.73e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 109.02 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngRRIAMIFQDplSHLNPVYTV-----------GWqmrealkthgiSTTQAQAEALR 135
Cdd:COG1125 55 TSGRILIDGEDIRDLDPVELR----RRIGYVIQQ--IGLFPHMTVaeniatvprllGW-----------DKERIRARVDE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 136 LFKRVALpDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHD 215
Cdd:COG1125 118 LLELVGL-DPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2087084196 216 lgvVSE---VADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:COG1125 197 ---IDEalkLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
275-504 |
2.82e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.17 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPGDLFKLRRDL 354
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPTQSLnprmtVYQLISE--AWIIHPEILPKAKWRERVGELLGQVglSLEHMGRYPHQ-FSGGQRQRIAIARALA 431
Cdd:PRK13638 80 ATVFQDPEQQI-----FYTDIDSdiAFSLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
65-238 |
3.51e-26 |
|
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: 106.23 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKMSAEARREVNGRRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALrlfkrVALPD 144
Cdd:cd03297 48 KPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNVRENLAFGLKRKRNREDRISVDEL-----LDLLG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVAD 224
Cdd:cd03297 121 LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLAD 200
|
170
....*....|....
gi 2087084196 225 RVVVMEKGQLVESG 238
Cdd:cd03297 201 RIVVMEDGRLQYIG 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
68-256 |
3.95e-26 |
|
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: 109.12 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEaRREVNgrriaMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdAER 147
Cdd:TIGR01187 24 SGSIMLDGEDVTNVPPH-LRHIN-----MVFQS--YALFPHMTVEENVAFGLKMRKVPRAEIKPRVLEALRLVQL--EEF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 AlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVV 227
Cdd:TIGR01187 94 A-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIA 172
|
170 180
....*....|....*....|....*....
gi 2087084196 228 VMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:TIGR01187 173 IMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
289-499 |
4.69e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 112.53 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfKLRRDLQMVFQDP---TQSL 365
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA---WLRRQMGVVLQENvlfSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 -------NPRMtvyqliSEAWIIHPEILPKA-----KWRERVGELLGQVGLSLehmgryphqfSGGQRQRIAIARALALE 433
Cdd:TIGR01846 548 rdnialcNPGA------PFEHVIHAAKLAGAhdfisELPQGYNTEVGEKGANL----------SGGQRQRIAIARALVGN 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGT 499
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGR 674
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
275-515 |
6.19e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.13 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGD-FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRD 353
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTQSLNPrMTVYQLIseAWIIHPEILPKAKWRERVGELLGQVGL-SLEHmgRYPHQFSGGQRQRIAIARALAL 432
Cdd:PRK13647 81 VGLVFQDPDDQVFS-STVWDDV--AFGPVNMGLDKDEVERRVEEALKAVRMwDFRD--KPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVV----------------- 495
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLaegdkslltdediveqa 234
|
250 260
....*....|....*....|..
gi 2087084196 496 --ELGTVAQVFDNPQKPYTQAL 515
Cdd:PRK13647 235 glRLPLVAQIFEDLPELGQSKL 256
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
69-247 |
6.98e-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: 108.66 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGKDLLKMSAEARREVNGRRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALrlfkrVALPDAERA 148
Cdd:TIGR02142 52 GEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVRGNLRYGMKRARPSERRISFERV-----IELLGIGHL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 149 LDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVV 228
Cdd:TIGR02142 125 LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVV 204
|
170
....*....|....*....
gi 2087084196 229 MEKGQLVESGTVRDVYRNP 247
Cdd:TIGR02142 205 LEDGRVAAAGPIAEVWASP 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
131-494 |
7.30e-26 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 110.86 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRLFKRVALPDAERALdkyPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVL 210
Cdd:PRK10762 120 AEADKLLARLNLRFSSDKL---VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 211 IITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNpqhaytkKLIAAAPG-KGEMHEP---EAQGEPILSVKDARKSyg 286
Cdd:PRK10762 196 YISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED-------SLIEMMVGrKLEDQYPrldKAPGEVRLKVDNLSGP-- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 dfeALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFK---------LRRD---L 354
Cdd:PRK10762 267 ---GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAngivyisedRKRDglvL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDptqslNPRMTVYQLISEAWIihpeILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEP 434
Cdd:PRK10762 344 GMSVKE-----NMSLTALRYFSRAGG----SLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
65-247 |
7.58e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 7.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKmsaearREVNGRRIAMIFQdplSH-LNPVYTVGWQMREALKTHGISTT---QAQAEALrlfkrv 140
Cdd:PRK11432 57 KPTEGQIFIDGEDVTH------RSIQQRDICMVFQ---SYaLFPHMSLGENVGYGLKMLGVPKEerkQRVKEAL------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 141 ALPDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVS 220
Cdd:PRK11432 122 ELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAF 201
|
170 180
....*....|....*....|....*..
gi 2087084196 221 EVADRVVVMEKGQLVESGTVRDVYRNP 247
Cdd:PRK11432 202 AVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-243 |
9.55e-26 |
|
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: 105.21 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL-----PPRSGSIRFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RrevNGRRIAMIFQDPlsHLNPVYTVGWQMREALKTHGISTTQAQ-AEALRLFKRVAlpdaERaLDKYPHEFSGGQRQRV 164
Cdd:cd03224 72 R---ARAGIGYVPEGR--RIFPELTVEENLLLGAYARRRAKRKARlERVYELFPRLK----ER-RKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
273-478 |
1.11e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 105.25 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEA----LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLF 348
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHelsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 KLR-RDLQMVFQD----PTqsLNPRMTVyQLiseawiihPEIL---PKAKWRERVGELLGQVGLS--LEHMgryPHQFSG 418
Cdd:PRK10584 84 KLRaKHVGFVFQSfmliPT--LNALENV-EL--------PALLrgeSSRQSRNGAKALLEQLGLGkrLDHL---PAQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 419 GQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPL 478
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-235 |
1.36e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 104.26 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSVDFHTVTgtvHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLlkmSAEAR 86
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI-----KESSGSILLNGKPI---KAKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 87 RevngRRIAMIFQDPLSHLNPVyTVGWQMREALKthGISTTQAQAEALrlFKRVALPDAEralDKYPHEFSGGQRQRVMI 166
Cdd:cd03226 70 R----KSIGYVMQDVDYQLFTD-SVREELLLGLK--ELDAGNEQAETV--LKDLDLYALK---ERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 167 AMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
281-506 |
1.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.63 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 281 ARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARI---LLRLEEPDGGTAHWKgkdlftmSPGDLFK------LR 351
Cdd:PRK13645 17 AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngLIISETGQTIVGDYA-------IPANLKKikevkrLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RDLQMVFQDPTqslnprmtvYQLISEAwiIHPEIL--------PKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQR 423
Cdd:PRK13645 90 KEIGLVFQFPE---------YQLFQET--IEKDIAfgpvnlgeNKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
...
gi 2087084196 504 FDN 506
Cdd:PRK13645 239 FSN 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-233 |
1.64e-25 |
|
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: 102.85 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNlsVDFHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIDmppgkITSGEILLDG 75
Cdd:cd03228 1 IEFKN--VSFSYPGRPKPVLKDVSLTIKPGEKVAIvgpsgsgkstLLK----------LLLRLYD-----PTSGEILIDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 76 KDLLKMSAEARRevngRRIAMIFQDPLshlnpvytvgwqmrealkthgisttqaqaealrLFKR-VAlpdaeraldkyph 154
Cdd:cd03228 64 VDLRDLDLESLR----KNIAYVPQDPF---------------------------------LFSGtIR------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 E--FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVsEVADRVVVMEKG 232
Cdd:cd03228 94 EniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
.
gi 2087084196 233 Q 233
Cdd:cd03228 171 R 171
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-494 |
2.34e-25 |
|
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: 102.90 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 272 GEPILSVKDARKSYgdfeALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfkLR 351
Cdd:cd03215 1 GEPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RDLQMVFQDP-TQSLNPRMTVYQLISeawiihpeilpkakwrervgellgqvglslehmgrYPHQFSGGQRQRIAIARAL 430
Cdd:cd03215 75 AGIAYVPEDRkREGLVLDLSVAENIA-----------------------------------LSSLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
2.47e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSvdFHTVTGTvHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLlK 80
Cdd:PRK13636 1 MEDYILKVEELN--YNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL-----KPSSGRILFDGKPI-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEARREVNgRRIAMIFQDPLSHLNPVyTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaERALDKYPHEFSGGQ 160
Cdd:PRK13636 72 YSRKGLMKLR-ESVGMVFQDPDNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI---EHLKDKPTHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTV 240
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
....
gi 2087084196 241 RDVY 244
Cdd:PRK13636 227 KEVF 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
287-494 |
3.36e-25 |
|
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: 103.70 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRDLQMVFQDPT---Q 363
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHSKVSLVGQEPVlfaR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 SLNPRMTvYQLISEAWIIHPEILPKAKWRERVGELlgQVGLSLEhMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAV 443
Cdd:cd03248 103 SLQDNIA-YGLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTE-VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 444 SALDVSVQAQVITLL-DKLRKEmgiAFIFIAHDLPLVRDfADYVMVMQKGEV 494
Cdd:cd03248 179 SALDAESEQQVQQALyDWPERR---TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
283-495 |
3.58e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.42 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 283 KSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRRDLQMVFQDp 361
Cdd:PRK10908 9 KAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 362 tQSLNPRMTVYQLISEAWIIHPEilPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDE 441
Cdd:PRK10908 88 -HHLLMDRTVYDNVAIPLIIAGA--SGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 442 AVSALDVSVQAQVITLLDKLRKeMGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-248 |
3.79e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.56 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLID--MPPgkiTSGEILLDGKDLLKMSA 83
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIAgfLAP---SSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EarREVngrriamIFQDplsH-LNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERAldkYPHEFSGGQRQ 162
Cdd:COG4525 77 D--RGV-------VFQK---DaLLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARR---RIWQLSGGMRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDlgvVSE---VADRVVVMEKG------- 232
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVMSPGpgriver 218
|
250 260
....*....|....*....|...
gi 2087084196 233 -------QLVESGTVRDVYRNPQ 248
Cdd:COG4525 219 leldfsrRFLAGEDARAIKSDPA 241
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
289-495 |
4.44e-25 |
|
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: 103.05 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfkLRRDLQMVFQDPT---QSL 365
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRNIGYVPQDVTlfyGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTV-YQLISEAwiihpEILPKAKwRERVGELLGQVGLSLEHM-GRYPHQFSGGQRQRIAIARALALEPQLIVCDEAV 443
Cdd:cd03245 95 RDNITLgAPLADDE-----RILRAAE-LAGVTDFVNKHPNGLDLQiGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 444 SALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVrDFADYVMVMQKGEVV 495
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
65-248 |
6.03e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.53 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDL-LKMSAEARREVNgRRIAMIFQDPLSHLNPvYTVGWQMREALKTHGISTTQAQAEALRLFKRVALP 143
Cdd:PRK13641 58 KPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQLFE-NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 daERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVA 223
Cdd:PRK13641 136 --EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYA 212
|
170 180
....*....|....*....|....*
gi 2087084196 224 DRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:PRK13641 213 DDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
267-514 |
6.07e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.09 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 267 EPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEE--PDG---GTAHWKGKDLFT 341
Cdd:PRK14243 2 STLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 342 mSPGDLFKLRRDLQMVFQDPTQ---------SLNPRMTVYQL-ISEawIIHPEILPKAKWRErVGELLGQVGLSLehmgr 411
Cdd:PRK14243 82 -PDVDPVEVRRRIGMVFQKPNPfpksiydniAYGARINGYKGdMDE--LVERSLRQAALWDE-VKDKLKQSGLSL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 412 yphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVM-- 489
Cdd:PRK14243 153 -----SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFnv 225
|
250 260 270
....*....|....*....|....*....|..
gi 2087084196 490 -------QKGEVVELGTVAQVFDNPQKPYTQA 514
Cdd:PRK14243 226 eltegggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
290-504 |
6.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.82 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAhwKGKDLFTMSPG---DLFKLRRDLQMVFQDPTQSLN 366
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSkqkEIKPVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 367 PRMTVYQLiseAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSAL 446
Cdd:PRK13643 99 EETVLKDV---AFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 447 DVSVQAQVITLLDKLRkEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13643 176 DPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-233 |
6.91e-25 |
|
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: 102.33 E-value: 6.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 13 VDFHTVT----GTVHAVRNISYYLDRGETLAIlgesGSGKSVSSSAIMNLIDM--PPgkiTSGEILLDGKDLLKMSaeaR 86
Cdd:TIGR02673 2 IEFHNVSkaypGGVAALHDVSLHIRKGEFLFL----TGPSGAGKTTLLKLLYGalTP---SRGQVRIAGEDVNRLR---G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 87 REVNG--RRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAeraLDKYPHEFSGGQRQRV 164
Cdd:TIGR02673 72 RQLPLlrRRIGVVFQD--FRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHK---ADAFPEQLSGGEQQRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:TIGR02673 147 AIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-233 |
7.06e-25 |
|
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: 102.90 E-value: 7.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 4 HLLEVRNLSVDF--HTVTG-TVHAVRNISYYLDRGETLAIlgesgsgksvsssaimnliDMPPG--------------KI 66
Cdd:COG4778 3 TLLEVENLSKTFtlHLQGGkRLPVLDGVSFSVAAGECVAL-------------------TGPSGagkstllkciygnyLP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGK----DLLkmSAEARREVNGRRiamifqdplshlnpvYTVGW--Q-------------MREALKTHGISTT 127
Cdd:COG4778 64 DSGSILVRHDggwvDLA--QASPREILALRR---------------RTIGYvsQflrviprvsaldvVAEPLLERGVDRE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 128 QAQAEALRLFKRVALPdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGM 207
Cdd:COG4778 127 EARARARELLARLNLP--ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GT 203
|
250 260
....*....|....*....|....*.
gi 2087084196 208 GVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:COG4778 204 AIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-245 |
8.83e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.09 E-value: 8.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 11 LSVDFHTVT-----GTVH---AVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLKMS 82
Cdd:PRK13646 1 MTIRFDNVSytyqkGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARRevngrRIAMIFQDPLSHLNPvYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPdaERALDKYPHEFSGGQRQ 162
Cdd:PRK13646 81 RPVRK-----RIGMVFQFPESQLFE-DTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRD 242
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
...
gi 2087084196 243 VYR 245
Cdd:PRK13646 233 LFK 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
288-504 |
1.28e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 288 FE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPG-DLFKLRRDLQMVFQDPTQS 364
Cdd:PRK13649 18 FEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQIRKKVGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 365 LNPRmTVYQLIS---EAWIIHPEilpKAKWRERvgELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDE 441
Cdd:PRK13649 98 LFEE-TVLKDVAfgpQNFGVSQE---EAEALAR--EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 442 AVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-235 |
1.46e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.81 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaiMN------LIDMPPG--KITSGEILLDGKD 77
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLG-------------ENgagkstLMKILSGlyKPDSGEILVDGKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 78 LLKMS-AEARRevngRRIAMIFQdplshlnpvytvgwqmrealkthgisttqaqaealrlfkrvalpdaeraldkypheF 156
Cdd:cd03216 64 VSFASpRDARR----AGIAMVYQ--------------------------------------------------------L 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
276-498 |
1.83e-24 |
|
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: 101.12 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETvAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmsPGDLFKLRRDLQ 355
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTqsLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03264 76 YLPQEFG--VYPNFTVREFLDYIAWLKG--IPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMgiAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-248 |
1.86e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSvdFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLlkmSAEAR 86
Cdd:PRK13632 9 KVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL-----KPQSGEIKIDGITI---SKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 87 REVNGRrIAMIFQDPLSHLnpvytVGWQMRE----ALKTHGISTTQAQAEALRLFKRValpDAERALDKYPHEFSGGQRQ 162
Cdd:PRK13632 79 KEIRKK-IGIIFQNPDNQF-----IGATVEDdiafGLENKKVPPKKMKDIIDDLAKKV---GMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLgvvSEV--ADRVVVMEKGQLVESGTV 240
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM---DEAilADKVIVFSEGKLIAQGKP 226
|
....*...
gi 2087084196 241 RDVYRNPQ 248
Cdd:PRK13632 227 KEILNNKE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-260 |
1.90e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.16 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNLSVDFHTVT-GTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLK 80
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEAR--REVNG-----RRIAMIFQDPLSHL-----------NPVytvgwqmreALkthGISTTQAQAEALRLFKRVAL 142
Cdd:PRK13631 98 ELITNPysKKIKNfkelrRRVSMVFQFPEYQLfkdtiekdimfGPV---------AL---GVKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PDAerALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEV 222
Cdd:PRK13631 166 DDS--YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEV 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 2087084196 223 ADRVVVMEKGQLVESGTVRDVYRNpQHAYTKKLIAAAP 260
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTD-QHIINSTSIQVPR 279
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-246 |
1.96e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.86 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSVDFHTVTGTVH--AVRNISYYLDRGETLAILGESGSGKSVSSSAiMNLIDMPpgkiTSGEILLDGKDLLK 80
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKH-MNALLIP----SEGKVYVDGLDTSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSA--EARRevngrRIAMIFQDPLSHLnpVYTVgwqmREALKTHGISTTQAQAEALRlfKRValPDAERALDKY------ 152
Cdd:PRK13633 77 EENlwDIRN-----KAGMVFQNPDNQI--VATI----VEEDVAFGPENLGIPPEEIR--ERV--DESLKKVGMYeyrrha 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 153 PHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvADRVVVMEKG 232
Cdd:PRK13633 142 PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSG 220
|
250
....*....|....
gi 2087084196 233 QLVESGTVRDVYRN 246
Cdd:PRK13633 221 KVVMEGTPKEIFKE 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-498 |
2.06e-24 |
|
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: 101.29 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGD----FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKL 350
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMVFQdpTQSLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:cd03266 77 RRRLGFVSD--STGLYDRLTARENLEYFAGLYG--LKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
270-499 |
2.17e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.03 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 270 AQGEpiLSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDL--FTMSpg 345
Cdd:PRK11176 338 AKGD--IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLA-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 346 dlfKLRRDLQMV------FQDpTQSLNPRMTVYQLISEAWIIHPEILPKA-----KWRERVGELLGQVGLSLehmgryph 414
Cdd:PRK11176 414 ---SLRNQVALVsqnvhlFND-TIANNIAYARTEQYSREQIEEAARMAYAmdfinKMDNGLDTVIGENGVLL-------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 415 qfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDfADYVMVMQKGEV 494
Cdd:PRK11176 482 --SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEI 556
|
....*
gi 2087084196 495 VELGT 499
Cdd:PRK11176 557 VERGT 561
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
281-498 |
3.11e-24 |
|
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: 101.07 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 281 ARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKD--LFTMSPGdlfklrrdlqmvf 358
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssLLGLGGG------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 qdptqsLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGEL-----LGQVGlsLEHMGRYphqfSGGQRQRIAIARALALE 433
Cdd:cd03220 95 ------FNPELTGRENIYLNGRLLG--LSRKEIDEKIDEIiefseLGDFI--DLPVKTY----SSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIaFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-256 |
3.57e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 25 VRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKI-TSGEILLDGKDLLKMSAEARRevngRRIAMIFQ--DP 101
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQqpNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 102 LSHLNPVYTVGWqmreALKTHGISTTQAQAEALR-LFKRVAL-PDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIA 179
Cdd:PRK14246 102 FPHLSIYDNIAY----PLKSHGIKEKREIKKIVEeCLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 180 DEPTTALDVTVQAEVLALLKELQREtgMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
276-494 |
4.15e-24 |
|
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: 99.21 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEA--LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRD 353
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPtqslnprmtvyQLISeawiihpeilpkakwrervGELLGQVglslehmgryphqFSGGQRQRIAIARALALE 433
Cdd:cd03246 78 VGYLPQDD-----------ELFS-------------------GSIAENI-------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDfADYVMVMQKGEV 494
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-498 |
4.16e-24 |
|
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: 99.91 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLE--EPDGGTAHWKGKDLFTMSPGDlfKLRRD 353
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE--RARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPtqslnprmtvyqliseawiihPEIlpkakwrervgellgqVGLSLEHMGRYPHQ-FSGGQRQRIAIARALAL 432
Cdd:cd03217 79 IFLAFQYP---------------------PEI----------------PGVKNADFLRYVNEgFSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHD---LPLVRdfADYVMVMQKGEVVELG 498
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSG 187
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-239 |
5.12e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.02 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVT----GTVHAVRNISYYLDRGETLAI-------------LgesgsgksvsssaIMNLIDmppgkITS 68
Cdd:COG1132 333 LPPVRGEIEFENVSfsypGDRPVLKDISLTIPPGETVALvgpsgsgkstlvnL-------------LLRFYD-----PTS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGKDLLKMSAEARRevngRRIAMIFQDPlsHL------------NPVYTVGwQMREALKthgisttqaQAEALRL 136
Cdd:COG1132 395 GRILIDGVDIRDLTLESLR----RQIGVVPQDT--FLfsgtirenirygRPDATDE-EVEEAAK---------AAQAHEF 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 137 FKRvaLPD------AERAldkypHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVL 210
Cdd:COG1132 459 IEA--LPDgydtvvGERG-----VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTI 529
|
250 260
....*....|....*....|....*....
gi 2087084196 211 IITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:COG1132 530 VIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
67-256 |
5.49e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEaRREVNgrriaMIFQdplSH-LNPVYTV------GWQMRealKTHGISTTQAQAEALRLfkr 139
Cdd:PRK09452 67 DSGRIMLDGQDITHVPAE-NRHVN-----TVFQ---SYaLFPHMTVfenvafGLRMQ---KTPAAEITPRVMEALRM--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 140 VALPD-AERAldkyPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGV 218
Cdd:PRK09452 132 VQLEEfAQRK----PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEE 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 2087084196 219 VSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:PRK09452 208 ALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-244 |
6.39e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSVDFHTVTgTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMS 82
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQ-EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL-----EAESGQIIIDGDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARRevngRRIAMIFQDPLSHLNPVyTVGWQMREALKTHGISTTQAQA---EALRLfkrVALPDAEralDKYPHEFSGG 159
Cdd:PRK13650 76 VWDIR----HKIGMVFQNPDNQFVGA-TVEDDVAFGLENKGIPHEEMKErvnEALEL---VGMQDFK---EREPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 160 QRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLgvvSEVA--DRVVVMEKGQLVES 237
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL---DEVAlsDRVLVMKNGQVEST 221
|
....*..
gi 2087084196 238 GTVRDVY 244
Cdd:PRK13650 222 STPRELF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
265-506 |
8.68e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.75 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 265 MHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSP 344
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 GDLFKLrrDLQMVFQDPTqsLNPRMTVYQLISEAwiihpeiLPK-AKWRERVGELLGQVGLSLEhmgryPHQFSG----G 419
Cdd:PRK15439 81 AKAHQL--GIYLVPQEPL--LFPNLSVKENILFG-------LPKrQASMQKMKQLLAALGCQLD-----LDSSAGslevA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 420 QRQRIAIARALALEPQLIVCDEAVSALdvsVQAQVITLLDKLRK--EMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVEL 497
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
|
....*....
gi 2087084196 498 GTVAQVFDN 506
Cdd:PRK15439 222 GKTADLSTD 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
284-524 |
1.23e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 284 SYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfKLRRDLQMVfqdPTQ 363
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR---QLARRLALL---PQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 SLNPR-MTVYQLIS---EAWIIHPEILpKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVC 439
Cdd:PRK11231 85 HLTPEgITVRELVAygrSPWLSLWGRL-SAEDNARVNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 440 DEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFdnpqkpyTQALLA-- 517
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-------TPGLLRtv 234
|
250
....*....|.
gi 2087084196 518 ----ASLDPDP 524
Cdd:PRK11231 235 fdveAEIHPEP 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
60-243 |
1.32e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 60 DMPPgkiTSGEILLDGKDLLKMSAEARrevnGRRIAMIFQDplSHLNPVYTVgwqmRE----ALKTHGISTTQAQAEALR 135
Cdd:PRK13548 51 ELSP---DSGEVRLNGRPLADWSPAEL----ARRRAVLPQH--SSLSFPFTV----EEvvamGRAPHGLSRAEDDALVAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 136 LFKRVALPD-AERAldkYPhEFSGGQRQRVMIAMALA------LKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMG 208
Cdd:PRK13548 118 ALAQVDLAHlAGRD---YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLA 193
|
170 180 190
....*....|....*....|....*....|....*
gi 2087084196 209 VLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:PRK13548 194 VIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-251 |
2.08e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.42 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVdfhtVTGTVHAVRNISYYLDRGETLAI----------LgesgsgksvsssaiMNLI--DMPPgkiTSGEIL 72
Cdd:COG4559 1 MLEAENLSV----RLGGRTLLDDVSLTLRPGELTAIigpngagkstL--------------LKLLtgELTP---SSGEVR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 LDGKDLLKMSAEARrevnGRRIAMIFQDplSHLNPVYTVgwqmRE----ALKTHGISTTQAQAEALRLFKRVALPD-AER 147
Cdd:COG4559 60 LNGRPLAAWSPWEL----ARRRAVLPQH--SSLAFPFTV----EEvvalGRAPHGSSAAQDRQIVREALALVGLAHlAGR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 AldkYPhEFSGGQRQRVMIAMALA-------LKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVS 220
Cdd:COG4559 130 S---YQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAA 204
|
250 260 270
....*....|....*....|....*....|...
gi 2087084196 221 EVADRVVVMEKGQLVESGTVRDVYRNP--QHAY 251
Cdd:COG4559 205 QYADRILLLHQGRLVAQGTPEEVLTDEllERVY 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
67-238 |
2.23e-23 |
|
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: 98.03 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngrRIAMIFQDPLSHlnPVYTVgwqmREALKT----HGISTTQAQAEALRLFKRVAL 142
Cdd:cd03264 52 SSGTIRIDGQDVLKQPQKLRR-----RIGYLPQEFGVY--PNFTV----REFLDYiawlKGIPSKEVKARVDEVLELVNL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PDAEralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETgmGVLIITHDLGVVSEV 222
Cdd:cd03264 121 GDRA---KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESL 195
|
170
....*....|....*.
gi 2087084196 223 ADRVVVMEKGQLVESG 238
Cdd:cd03264 196 CNQVAVLNKGKLVFEG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-259 |
2.40e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVtgtvHAVRNISYYLDRGETLAILGESGSGKSvsssaimNLIDMPPG--KITSGEILLDGKDLLKMS 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS-------TLLRMLAGfeQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARRevngrrIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAealRLFKRVALPDAERALDKYPHEFSGGQRQ 162
Cdd:PRK11607 88 PYQRP------INMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIAS---RVNEMLGLVHMQEFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTV----QAEVLALLKELqretGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250 260
....*....|....*....|.
gi 2087084196 239 TVRDVYRNPQHAYTKKLIAAA 259
Cdd:PRK11607 233 EPEEIYEHPTTRYSAEFIGSV 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
285-476 |
2.53e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.39 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 285 YGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftMSPGdlfklrRDLQMVFQDptQS 364
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGPG------AERGVVFQN--EG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 365 LNPRMTVyqLISEAWIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVS 444
Cdd:PRK11248 81 LLPWRNV--QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|..
gi 2087084196 445 ALDVSVQAQVITLLDKLRKEMGIAFIFIAHDL 476
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
55-227 |
2.96e-23 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 97.69 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 55 IMNLIDmppgKITSGEILLDGKDLLKMSAEARREVNGRRIAMIFQDPLshLNPVYTVGWQMREALKTHGISTTQAQAEAL 134
Cdd:TIGR03608 43 IIGLLE----KFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFA--LIENETVEENLDLGLKYKKLSKKEKREKKK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 135 RLFKRVALpdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITH 214
Cdd:TIGR03608 117 EALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTH 192
|
170
....*....|...
gi 2087084196 215 DLgVVSEVADRVV 227
Cdd:TIGR03608 193 DP-EVAKQADRVI 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
276-507 |
3.13e-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: 98.38 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPgdLFKlRRDLQ 355
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLP--MHK-RARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVF--QDPtqSLNPRMTVYQLISEAWIIHPeiLPKAKWRERVGELLGQvgLSLEHM-GRYPHQFSGGQRQRIAIARALAL 432
Cdd:cd03218 77 IGYlpQEA--SIFRKLTVEENILAVLEIRG--LSKKEREEKLEELLEE--FHITHLrKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 433 EPQLIVCDEAVSALD-VSVQ--AQVITLLdklrKEMGIAfIFIA-HDlplVR---DFADYVMVMQKGEVVELGTVAQVFD 505
Cdd:cd03218 151 NPKFLLLDEPFAGVDpIAVQdiQKIIKIL----KDRGIG-VLITdHN---VRetlSITDRAYIIYEGKVLAEGTPEEIAA 222
|
..
gi 2087084196 506 NP 507
Cdd:cd03218 223 NE 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
67-246 |
3.28e-23 |
|
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: 103.30 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPlsHL------------NPVYTvGWQMREALKthgisttqaQAEAL 134
Cdd:COG4988 390 YSGSILINGVDLSDLDPASWR----RQIAWVPQNP--YLfagtirenlrlgRPDAS-DEELEAALE---------AAGLD 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 135 RLFKRvaLPD------AERAldkypHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRE-Tgm 207
Cdd:COG4988 454 EFVAA--LPDgldtplGEGG-----RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrT-- 524
|
170 180 190
....*....|....*....|....*....|....*....
gi 2087084196 208 gVLIITHDLGVVSEvADRVVVMEKGQLVESGTVRDVYRN 246
Cdd:COG4988 525 -VILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-238 |
3.66e-23 |
|
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: 97.29 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI-----KPDSGEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrrIAMIFQDPLshLNPVYTVgwqmREALKTHGISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQRVM 165
Cdd:cd03268 72 RR------IGALIEAPG--FYPNLTA----RENLRLLARLLGIRKKRIDEVLDVVGLKDSA---KKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 166 IAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-243 |
6.39e-23 |
|
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: 97.21 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:TIGR03410 1 LEVSNLNVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLL-----PVKSGSIRLDGEDITKLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREvngRRIA------MIFqdplshlnPVYTVgwqmREALKThgisttqaQAEALRLFKRvALPDaeRALDKYP--HEF- 156
Cdd:TIGR03410 72 RAR---AGIAyvpqgrEIF--------PRLTV----EENLLT--------GLAALPRRSR-KIPD--EIYELFPvlKEMl 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 -------SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:TIGR03410 126 grrggdlSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVM 205
|
250
....*....|....
gi 2087084196 230 EKGQLVESGTVRDV 243
Cdd:TIGR03410 206 ERGRVVASGAGDEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-243 |
7.35e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHtvtGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIdmppgKITSGEILLD 74
Cdd:COG3845 257 VLEVENLSVRDD---RGVPALKDVSLEVRAGEILGIagvagngqseLAE----------ALAGLR-----PPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEARREvngRRIAMIFQDPLSH-LNPVYTV------GWQMREALKTHG-ISTTQAQAEALRLFKR--VALPD 144
Cdd:COG3845 319 GEDITGLSPRERRR---LGVAYIPEDRLGRgLVPDMSVaenlilGRYRRPPFSRGGfLDRKAIRAFAEELIEEfdVRTPG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AE---RALdkyphefSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSE 221
Cdd:COG3845 396 PDtpaRSL-------SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILA 467
|
250 260
....*....|....*....|..
gi 2087084196 222 VADRVVVMEKGQLVESGTVRDV 243
Cdd:COG3845 468 LSDRIAVMYEGRIVGEVPAAEA 489
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-243 |
1.00e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAea 85
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL-----TPQSGTVFLGDKPISMLSS-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 rREVnGRRIAMIfqdPLSHLNPvytVGWQMREaLKTHGISTTqaqaeaLRLFKRVALPD----------------AERAL 149
Cdd:PRK11231 72 -RQL-ARRLALL---PQHHLTP---EGITVRE-LVAYGRSPW------LSLWGRLSAEDnarvnqameqtrinhlADRRL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 DkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:PRK11231 137 T----DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVL 211
|
250
....*....|....
gi 2087084196 230 EKGQLVESGTVRDV 243
Cdd:PRK11231 212 ANGHVMAQGTPEEV 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
67-245 |
1.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARREVNGRRIAMIFQDPLSHLNPvYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdAE 146
Cdd:PRK13649 60 TQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFE-ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGI--SE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHDLGVVSEVADRV 226
Cdd:PRK13649 137 SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFV 215
|
170
....*....|....*....
gi 2087084196 227 VVMEKGQLVESGTVRDVYR 245
Cdd:PRK13649 216 YVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-238 |
1.10e-22 |
|
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: 96.20 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPgkiTSGEILLDGKdllKMSAEA 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII--LP---DSGEVLFDGK---PLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngrRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPD-AERALDkyphEFSGGQRQRV 164
Cdd:cd03269 69 RN-----RIGYLPEE--RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
253-504 |
1.16e-22 |
|
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: 101.75 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 253 KKLIAAAPGKGE-MHEPEAQGEpiLSVKD--ARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDG 329
Cdd:COG4618 309 NELLAAVPAEPErMPLPRPKGR--LSVENltVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 330 GTAHWKGKDLFTMSPGDLFK----LRRDLQMV----------FQDPTQslnprmtvyQLISEA--------WIIHpeiLP 387
Cdd:COG4618 387 GSVRLDGADLSQWDREELGRhigyLPQDVELFdgtiaeniarFGDADP---------EKVVAAaklagvheMILR---LP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 388 KakwrervG--ELLGQVGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLrKEM 465
Cdd:COG4618 455 D-------GydTRIGEGGARL----------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KAR 516
|
250 260 270
....*....|....*....|....*....|....*....
gi 2087084196 466 GIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVF 504
Cdd:COG4618 517 GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
273-508 |
1.20e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLfTMSPgdLFK-LR 351
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLP--MHKrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RDLQMVFQDPtqSLNPRMTVYQ---LISEawiIHPeiLPKAKWRERVGELLGQvgLSLEHMGRYP-HQFSGGQRQRIAIA 427
Cdd:COG1137 78 LGIGYLPQEA--SIFRKLTVEDnilAVLE---LRK--LSKKEREERLEELLEE--FGITHLRKSKaYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALD-VSV---QAQVITLldklrKEMGIAfIFIA-HDlplVR---DFADYVMVMQKGEVVELGT 499
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDpIAVadiQKIIRHL-----KERGIG-VLITdHN---VRetlGICDRAYIISEGKVLAEGT 219
|
....*....
gi 2087084196 500 VAQVFDNPQ 508
Cdd:COG1137 220 PEEILNNPL 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
8-259 |
1.74e-22 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 98.91 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 8 VRNLSVDFHTVTgtvhAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmPPGkiTSGEILLDGKDLLKMSAEARR 87
Cdd:TIGR03258 8 IDHLRVAYGANT----VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVK-AAG--LTGRIAIADRDLTHAPPHKRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 88 evngrrIAMIFQD--PLSHLNPVYTVGWQMReALKTHGISTTQAQAEALRLfkrVALPDAERaldKYPHEFSGGQRQRVM 165
Cdd:TIGR03258 81 ------LALLFQNyaLFPHLKVEDNVAFGLR-AQKMPKADIAERVADALKL---VGLGDAAA---HLPAQLSGGMQQRIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 166 IAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRE-TGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVY 244
Cdd:TIGR03258 148 IARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALY 227
|
250
....*....|....*
gi 2087084196 245 RNPQHAYTKKLIAAA 259
Cdd:TIGR03258 228 DAPADGFAAEFLGAA 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-253 |
2.00e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.49 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILgesgsgksvsssaIMNLIDmppgkITSGEILLDGKdllKMSAEA 85
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLgpngagktttiriILGILA-----PDSGEVLWDGE---PLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREVnG-----RRiamifqdplshLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDaeRALDKYpHEFSGGQ 160
Cdd:COG4152 70 RRRI-GylpeeRG-----------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGD--RANKKV-EELSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVtVQAEVLA-LLKELQREtgmGVLII--THDLGVVSEVADRVVVMEKGQLVES 237
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLKdVIRELAAK---GTTVIfsSHQMELVEELCDRIVIINKGRKVLS 210
|
250
....*....|....*.
gi 2087084196 238 GTVRDVYRnpQHAYTK 253
Cdd:COG4152 211 GSVDEIRR--QFGRNT 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
274-475 |
2.03e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfKLRRD 353
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTQSLNprmTVYQLISEAWII---HPEilPKAKWRErvgelLGQVGLSLEHMGRYPHQFSGGQRQRIAIARAL 430
Cdd:PRK10247 83 VSYCAQTPTLFGD---TVYDNLIFPWQIrnqQPD--PAIFLDD-----LERFALPDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHD 475
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-238 |
2.57e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 95.13 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAE 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL-----EPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARRevngrRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRValpDAERALDKYPHEFSGGQRQRV 164
Cdd:cd03266 76 ARR-----RLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRL---GMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 165 MIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
282-495 |
2.71e-22 |
|
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: 95.86 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 282 RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfKLRRDLQMVFQDP 361
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK----KFLRRIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 362 TQ---SLNPRMTVYqliseawiIHPEI--LPKAKWRERVGELLGQvgLSLEHMGRYP-HQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03267 104 TQlwwDLPVIDSFY--------LLAAIydLPPARFKKRLDELSEL--LDLEELLDTPvRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-247 |
2.78e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMppgkiTSGEILLDGKDLLKMSAea 85
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ-----TSGHIRFHGTDVSRLHA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 rREvngRRIAMIFQD--PLSHLNPVYTVGWQM-----REALKTHGISttqaqAEALRLFKRVALpdaERALDKYPHEFSG 158
Cdd:PRK10851 72 -RD---RKVGFVFQHyaLFRHMTVFDNIAFGLtvlprRERPNAAAIK-----AKVTQLLEMVQL---AHLADRYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 159 GQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
....*....
gi 2087084196 239 TVRDVYRNP 247
Cdd:PRK10851 220 TPDQVWREP 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-234 |
3.03e-22 |
|
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: 94.04 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDfhtvtgtvHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAE 84
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR-----PPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREvngRRIAMIFQDPLSH-LNPVYTVGWQMrealkthgisttqaqaeALRLFkrvalpdaeraldkypheFSGGQRQR 163
Cdd:cd03215 71 DAIR---AGIAYVPEDRKREgLVLDLSVAENI-----------------ALSSL------------------LSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
68-248 |
4.01e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 97.64 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARREVNGRRIAMIFQDplSHLNPVYTVgwqmREALKtHGIS-TTQAQAEALrlfkrVALPDAE 146
Cdd:PRK11144 52 KGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQD--ARLFPHYKV----RGNLR-YGMAkSMVAQFDKI-----VALLGIE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRV 226
Cdd:PRK11144 120 PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRV 199
|
170 180
....*....|....*....|..
gi 2087084196 227 VVMEKGQLVESGTVRDVYRNPQ 248
Cdd:PRK11144 200 VVLEQGKVKAFGPLEEVWASSA 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-239 |
7.06e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 7.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVdfhTVTGTVhAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLidmpPG-KITSGEILLD 74
Cdd:COG0396 1 LEIKNLHV---SVEGKE-ILKGVNLTIKPGEVHAImgpngsgkstLAK----------VLMGH----PKyEVTSGSILLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 75 GKDLLKMSAEAR-REvnGrrIAMIFQDP-------LSHLnpvytvgwqMREALKTHG---ISTTQAQAEALRLFKRVALP 143
Cdd:COG0396 63 GEDILELSPDERaRA--G--IFLAFQYPveipgvsVSNF---------LRTALNARRgeeLSAREFLKLLKEKMKELGLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 DAerALDKYPHE-FSGGQRQRVMIAMALALKPDLLIADEPTTALDV----TVqAEVLALLkelqRETGMGVLIITHDLGV 218
Cdd:COG0396 130 ED--FLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalrIV-AEGVNKL----RSPDRGILIITHYQRI 202
|
250 260
....*....|....*....|..
gi 2087084196 219 VSEV-ADRVVVMEKGQLVESGT 239
Cdd:COG0396 203 LDYIkPDFVHVLVDGRIVKSGG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
273-507 |
8.45e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.67 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMsPGDLFKlRR 352
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIA-RM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDptQSLNPRMTVYQ--LISEAWIIHPEILP-----------KAKWRERVGELLGQVGLsLEHMGRYPHQFSGG 419
Cdd:PRK11300 81 GVVRTFQH--VRLFREMTVIEnlLVAQHQQLKTGLFSgllktpafrraESEALDRAATWLERVGL-LEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 420 QRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGT 499
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
....*...
gi 2087084196 500 VAQVFDNP 507
Cdd:PRK11300 238 PEEIRNNP 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
255-476 |
8.51e-22 |
|
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: 98.59 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 255 LIAAAPGKGEMHEPEAQ----GEPILSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDG 329
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGavglGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 330 GTAHWKGKDLFTMSPGDlfkLRRDLQMVFQDP-----TQSLNPRmtvyqliseawIIHPEILPKAKWR--ERVG------ 396
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDE---VRRRVSVCAQDAhlfdtTVRENLR-----------LARPDATDEELWAalERVGladwlr 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 397 ELLGQVGLSLEHMGRyphQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLdkLRKEMGIAFIFIAHDL 476
Cdd:TIGR02868 456 ALPDGLDTVLGEGGA---RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
238-503 |
1.25e-21 |
|
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: 98.19 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 238 GTVRDVYRNpqhayTKKLIAAAPGKGE-MHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKST 316
Cdd:TIGR01842 285 SGARQAYKR-----LNELLANYPSRDPaMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 317 LARILLRLEEPDGGTAHWKGKDLFTMSPGDLFK----LRRDLQMV----------FQDPTQSlnprmtvyQLISEAWII- 381
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKhigyLPQDVELFpgtvaeniarFGENADP--------EKIIEAAKLa 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 382 --HPEILPKAKWRERVgelLGQVGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLD 459
Cdd:TIGR01842 432 gvHELILRLPDGYDTV---IGPGGATL----------SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK 498
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2087084196 460 KLRKEmGIAFIFIAHDlPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:TIGR01842 499 ALKAR-GITVVVITHR-PSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
123-246 |
1.54e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.15 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 123 GISTTQAQAEALRLFKRVALPdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQ 202
Cdd:PRK13651 135 GVSKEEAKKRAAKYIELVGLD--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2087084196 203 REtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRN 246
Cdd:PRK13651 213 KQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-495 |
2.21e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.61 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYG-----DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlFK 349
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE---YK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 350 LRRDLQMVFQDPTQSLNPRMTVYQLISEAWI------IHPEIlpKAKWRERVGELLGQVGLSLEH-----MGryphQFSG 418
Cdd:COG1101 78 RAKYIGRVFQDPMMGTAPSMTIEENLALAYRrgkrrgLRRGL--TKKRRELFRELLATLGLGLENrldtkVG----LLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 419 GQRQriaiarALAL------EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLplvRDFADY----VMv 488
Cdd:COG1101 152 GQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM---EQALDYgnrlIM- 221
|
....*..
gi 2087084196 489 MQKGEVV 495
Cdd:COG1101 222 MHEGRII 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
60-230 |
2.65e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.16 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 60 DMPPGKITSGEILLDGKDLLKMSAEARRevngrrIAMIFQDPLshLNPVYTVGWQMREALkTHGISTTQAQAEALRLFKR 139
Cdd:COG4136 50 TLSPAFSASGEVLLNGRRLTALPAEQRR------IGILFQDDL--LFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 140 VALPDAEralDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVV 219
Cdd:COG4136 121 AGLAGFA---DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA 197
|
170
....*....|.
gi 2087084196 220 sEVADRVVVME 230
Cdd:COG4136 198 -PAAGRVLDLG 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
274-500 |
3.18e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 93.17 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILlrLEEPD----GGTAHWKGKDLFTMSPGDlfK 349
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEE--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 350 LRRDLQMVFQDPTQ------------SLNPRMTVYQLiseawiihPEILPkAKWRERVGELLGQVGLSLEHMGRYPHQ-F 416
Cdd:CHL00131 82 AHLGIFLAFQYPIEipgvsnadflrlAYNSKRKFQGL--------PELDP-LEFLEIINEKLKLVGMDPSFLSRNVNEgF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 417 SGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVrDF--ADYVMVMQKGEV 494
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLL-DYikPDYVHVMQNGKI 230
|
....*.
gi 2087084196 495 VELGTV 500
Cdd:CHL00131 231 IKTGDA 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
67-519 |
3.25e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.90 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAearREVNGRRIAMIFQDplSHLNPVYTV-------------GWQMREALKthgisttqaqAEA 133
Cdd:PRK11288 57 DAGSILIDGQEMRFAST---TAALAAGVAIIYQE--LHLVPEMTVaenlylgqlphkgGIVNRRLLN----------YEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 134 LRLFKRVAL---PDAERAldkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVL 210
Cdd:PRK11288 122 REQLEHLGVdidPDTPLK------YLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVIL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 211 IITHDLGVVSEVADRVVVMEKGQLVES-GTVRDVYRNpqhaytkKLIAAAPGKgEM-----HEPEAQGEPILSVKDarks 284
Cdd:PRK11288 195 YVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRD-------QLVQAMVGR-EIgdiygYRPRPLGEVRLRLDG---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 285 ygdfeaLKG------VSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfKLRRDLQMVF 358
Cdd:PRK11288 263 ------LKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRAGIMLCP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 QD-------PTQSLNPRMTvyqlISE-------AWIIHPeilpkaKWRERVGELLGQvglSLEHMGRYPHQ----FSGGQ 420
Cdd:PRK11288 335 EDrkaegiiPVHSVADNIN----ISArrhhlraGCLINN------RWEAENADRFIR---SLNIKTPSREQlimnLSGGN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 421 RQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLrKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVelGTV 500
Cdd:PRK11288 402 QQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GEL 478
|
490
....*....|....*....
gi 2087084196 501 AQVFDNPQKPYTQALLAAS 519
Cdd:PRK11288 479 AREQATERQALSLALPRTS 497
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
131-486 |
3.75e-21 |
|
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: 96.93 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRLfkrvalPDAERALDKypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDvtvqAEVLALLKE-LQRETGMgV 209
Cdd:TIGR03719 147 MDALRC------PPWDADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPGT-V 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 210 LIITHDLGVVSEVADRVVVMEKGQLV-----------------------ESGTVRDVYR-------NP--QHAYTKKLIA 257
Cdd:TIGR03719 212 VAVTHDRYFLDNVAGWILELDRGRGIpwegnysswleqkqkrleqeekeESARQKTLKRelewvrqSPkgRQAKSKARLA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 258 A-----------APGKGEMHEPEAQ--GEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRL 324
Cdd:TIGR03719 292 RyeellsqefqkRNETAEIYIPPGPrlGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 325 EEPDGGtahwkgkdlfTMSPGDLFKL-----RRDlqmvfqdptqSLNPRMTVYQLISEAwiihPEILPKAKWRERVGELL 399
Cdd:TIGR03719 372 EQPDSG----------TIEIGETVKLayvdqSRD----------ALDPNKTVWEEISGG----LDIIKLGKREIPSRAYV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 400 GQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV-SVQAqvitLLDKLRKEMGIAFIfIAHDlpl 478
Cdd:TIGR03719 428 GRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA----LEEALLNFAGCAVV-ISHD--- 499
|
....*...
gi 2087084196 479 vRDFADYV 486
Cdd:TIGR03719 500 -RWFLDRI 506
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-248 |
4.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.33 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSvdFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLID--MPPGKITSGEILLDGKDL 78
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKS----TISKLINglLLPDDNPNSKITVDGITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 79 LKMSAEARREvngrRIAMIFQDPLSHLNPVyTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAeraLDKYPHEFSG 158
Cdd:PRK13640 75 TAKTVWDIRE----KVGIVFQNPDNQFVGA-TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDY---IDSEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 159 GQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGvVSEVADRVVVMEKGQLVESG 238
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQG 225
|
250
....*....|
gi 2087084196 239 TVRDVYRNPQ 248
Cdd:PRK13640 226 SPVEIFSKVE 235
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
5-229 |
4.84e-21 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 91.68 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDF--HTVTGTV-HAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITS---GEILldgkDL 78
Cdd:TIGR02324 1 LLEVEDLSKTFtlHQQGGVRlPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVrheGAWV----DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 79 LKmsAEARREVNGRRIAMIFQDPLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPdaERALDKYPHEFSG 158
Cdd:TIGR02324 77 AQ--ASPREVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIP--ERLWHLPPATFSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 159 GQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:TIGR02324 153 GEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDV 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
65-243 |
4.98e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.45 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKMSAEARrevnGRRIAMIFQDPlsHLNPVYTVgwqmREALK------THGISTTQAQA---EALR 135
Cdd:COG4604 52 PPDSGEVLVDGLDVATTPSREL----AKRLAILRQEN--HINSRLTV----RELVAfgrfpySKGRLTAEDREiidEAIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 136 LFKRVALpdAERALDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHD 215
Cdd:COG4604 122 YLDLEDL--ADRYLD----ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
170 180
....*....|....*....|....*...
gi 2087084196 216 LGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:COG4604 196 INFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
55-238 |
6.72e-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: 91.02 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 55 IMNLI---DMPpgkiTSGEILLDGKDLLKMsaearrEVNGRRIAMIFQDP--LSHLNPVYTVGWQMREALKTHGISTtQA 129
Cdd:cd03298 40 LLNLIagfETP----QSGRVLINGVDVTAA------PPADRPVSMLFQENnlFAHLTVEQNVGLGLSPGLKLTAEDR-QA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 130 QAEALRlfkRVALPDAERALdkyPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGV 209
Cdd:cd03298 109 IEVALA---RVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTV 182
|
170 180
....*....|....*....|....*....
gi 2087084196 210 LIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03298 183 LMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-234 |
7.55e-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: 90.93 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 13 VDFHTVT----GTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLIdMPPGKITSGEILLDGKDLLKMSAEARRE 88
Cdd:cd03292 1 IEFINVTktypNGTAALDGINISISAGEFVFLVGPSGAGKS----TLLKLI-YKEELPTSGTIRVNGQDVSDLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 89 VNgRRIAMIFQDP--LSHLNPVYTVGWqmreALKTHGISTTQAQAEALRLFKRVALPDAERAldkYPHEFSGGQRQRVMI 166
Cdd:cd03292 76 LR-RKIGVVFQDFrlLPDRNVYENVAF----ALEVTGVPPREIRKRVPAALELVGLSHKHRA---LPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 167 AMALALKPDLLIADEPTTALDVTVQAEVLALLKELQReTGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-256 |
8.14e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 8.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLK 80
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSA---EARREvngrrIAMIFQDPlshlNPV-YTVGWQMREALKTHGISTTQAQAEAL-RLFKRVALPDAERalDKYpHE 155
Cdd:PRK14239 77 PRTdtvDLRKE-----IGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQVLDEAVeKSLKGASIWDEVK--DRL-HD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 ----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgvLIITHDLGVVSEVADRVVVMEK 231
Cdd:PRK14239 145 salgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLD 222
|
250 260
....*....|....*....|....*
gi 2087084196 232 GQLVESGTVRDVYRNPQHAYTKKLI 256
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
274-487 |
1.19e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.33 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTahwkgkdlftmspgdlfkLRRD 353
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV------------------IKRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTQSLNPRMTVYQLISEAWIIHP-----EILPKAKwRERVGELLGQvglslehmgryPHQ-FSGGQRQRIAIA 427
Cdd:PRK09544 65 GKLRIGYVPQKLYLDTTLPLTVNRFLRLRPgtkkeDILPALK-RVQAGHLIDA-----------PMQkLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVM 487
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
65-244 |
1.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.74 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGkdlLKMSAEARREVNgRRIAMIFQDPLSHLNPVyTVGWQMREALKTHGISTTQAQAEALRLFKRVALPD 144
Cdd:PRK13648 60 KVKSGEIFYNN---QAITDDNFEKLR-KHIGIVFQNPDNQFVGS-IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 aeRAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvAD 224
Cdd:PRK13648 135 --RA-DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-AD 210
|
170 180
....*....|....*....|
gi 2087084196 225 RVVVMEKGQLVESGTVRDVY 244
Cdd:PRK13648 211 HVIVMNKGTVYKEGTPTEIF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-251 |
1.45e-20 |
|
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: 95.22 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNLSvdFHTVTGTVHAVRNISYYLDRGETLAI----------LGEsgsgksvsssAIMNLIDmppgkITSGEI 71
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIvgpsgsgkstLLA----------LLLRFLD-----PQSGSI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 72 LLDGKDLLKMSAEARRevngRRIAMIFQDPlsHLnpvytvgwqmrealkthgISTTQAQ-----------AEALRLFKRV 140
Cdd:COG4987 393 TLGGVDLRDLDEDDLR----RRIAVVPQRP--HL------------------FDTTLREnlrlarpdatdEELWAALERV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 141 ALPDAERALDK--------YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLII 212
Cdd:COG4987 449 GLGDWLAALPDgldtwlgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLI 526
|
250 260 270
....*....|....*....|....*....|....*....
gi 2087084196 213 THDLGVVsEVADRVVVMEKGQLVESGTVRDVYRNPQHAY 251
Cdd:COG4987 527 THRLAGL-ERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-235 |
1.77e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLI---DMPpgkiTSGEILLDGKDLLKM 81
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILgclDKP----TSGTYRVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 82 SAEA----RREVNGrriaMIFQ--DPLSHLNPVYTVGWQMREAlkthGISTTQAQAEALRLFKRVALpdAERaLDKYPHE 155
Cdd:PRK10535 76 DADAlaqlRREHFG----FIFQryHLLSHLTAAQNVEVPAVYA----GLERKQRLLRAQELLQRLGL--EDR-VEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEvADRVVVMEKGQLV 235
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
289-489 |
1.91e-20 |
|
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: 94.66 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 289 EALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDLQMVFQDPT---QSL 365
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFlfaGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTVYQliSEAwiiHPEILPKAKWRERVGELLGQVGLSLEHM-GRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVS 444
Cdd:TIGR02857 413 AENIRLAR--PDA---SDAEIREALERAGLDEFVAALPQGLDTPiGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087084196 445 ALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDfADYVMVM 489
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-261 |
2.32e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 60 DMPPGKITSGEILLDGKDLLKMS--AEARRevngrRIAMIFQDPlshlNPV-YTVGWQMREALKTHG-ISTTQAQAEALR 135
Cdd:PRK14271 72 DKVSGYRYSGDVLLGGRSIFNYRdvLEFRR-----RVGMLFQRP----NPFpMSIMDNVLAGVRAHKlVPRKEFRGVAQA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 136 LFKRVALPDAER-ALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtgMGVLIITH 214
Cdd:PRK14271 143 RLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTH 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2087084196 215 DLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLIAAAPG 261
Cdd:PRK14271 221 NLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
77-245 |
2.91e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 77 DLLKMSAEARREVNG--RRIAMIFQDPLSHLNPvYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdAERALDKYPH 154
Cdd:PRK13643 67 DIVVSSTSKQKEIKPvrKKVGVVFQFPESQLFE-ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:PRK13643 144 ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
170
....*....|.
gi 2087084196 235 VESGTVRDVYR 245
Cdd:PRK13643 223 ISCGTPSDVFQ 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
276-498 |
2.98e-20 |
|
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: 88.14 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFE--ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDlftmsPGDLFKLRRD 353
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----VSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVfqdptqsLNPRMTVYQliseawiihpeilpkAKWRERVGEllgqvglslehmgryphQFSGGQRQRIAIARALALE 433
Cdd:cd03247 76 LISV-------LNQRPYLFD---------------TTLRNNLGR-----------------RFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFaDYVMVMQKGEVVELG 498
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
275-495 |
3.11e-20 |
|
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: 93.74 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLeEPDG---GTAHWKGKDLFTMSPGDlfKLR 351
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRD--TER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 352 RDLQMVFQDPTqsLNPRMTVYQLI---SEawIIHP-EILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIA 427
Cdd:TIGR02633 78 AGIVIIHQELT--LVPELSVAENIflgNE--ITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 428 RALALEPQLIVCDEAVSALdvsVQAQVITLLDKLR--KEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL---TEKETEILLDIIRdlKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
300-508 |
5.92e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.47 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 300 QGETvAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPG-DLFKLRRDLQMVFQDptQSLNPRMTV-----YQ 373
Cdd:PRK11144 24 QGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLPPEKRRIGYVFQD--ARLFPHYKVrgnlrYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 374 LiseawiihpeilpKAKWRE---RVGELLGqvglsLEH-MGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVS 449
Cdd:PRK11144 101 M-------------AKSMVAqfdKIVALLG-----IEPlLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 450 VQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-235 |
6.04e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTvtGTV---HAVRNISYYLDRGE-------------TLailgesgsgksvsssaiMNLI--DMPPgkiT 67
Cdd:COG1101 2 LELKNLSKTFNP--GTVnekRALDGLNLTIEEGDfvtvigsngagksTL-----------------LNAIagSLPP---D 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARrevnGRRIAMIFQDPLSHLNPVYTVGWQMREAL---KTHG--ISTTQAQAEAL-------- 134
Cdd:COG1101 60 SGSILIDGKDVTKLPEYKR----AKYIGRVFQDPMMGTAPSMTIEENLALAYrrgKRRGlrRGLTKKRRELFrellatlg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 135 -----RLFKRVALpdaeraldkypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGV 209
Cdd:COG1101 136 lglenRLDTKVGL-------------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTT 202
|
250 260
....*....|....*....|....*.
gi 2087084196 210 LIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:COG1101 203 LMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
291-498 |
7.75e-20 |
|
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: 87.61 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILL-RLEEPdggtaHWKGKDLFTMSPGDLFKLRRDLQMVFQDptQSLNPRM 369
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGL-----GVSGEVLINGRPLDKRSFRKIIGYVPQD--DILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 370 TVYQLISEAwiihpeilpkAKWRervgellgqvGLSlehmgryphqfsGGQRQRIAIARALALEPQLIVCDEAVSALDVS 449
Cdd:cd03213 98 TVRETLMFA----------AKLR----------GLS------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087084196 450 VQAQVITLLDKLRKeMGIAFIFIAHDLP-LVRDFADYVMVMQKGEVVELG 498
Cdd:cd03213 146 SALQVMSLLRRLAD-TGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-216 |
1.04e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLID--MPPGkitSGEILLDGKDLLKMS 82
Cdd:PRK11248 1 MLQISHLYADY----GGKPALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAgfVPYQ---HGSITLDGKPVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEarREVngrriamIFQDP--LSHLNPVYTVGWQMREAlkthGISTTQAQAEALRLFKRVALPDAERaldKYPHEFSGGQ 160
Cdd:PRK11248 70 AE--RGV-------VFQNEglLPWRNVQDNVAFGLQLA----GVEKMQRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDL 216
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
250-533 |
1.08e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.47 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 250 AYTK--KLIAAAP--GKGEMHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLE 325
Cdd:PRK10789 286 AYSRirAMLAEAPvvKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 326 EPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDP-----TQSLN-----PRMTVYQLISEAWI--IHPEIL--PKAkW 391
Cdd:PRK10789 366 DVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPflfsdTVANNialgrPDATQQEIEHVARLasVHDDILrlPQG-Y 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 392 RERVGELlgqvGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIF 471
Cdd:PRK10789 442 DTEVGER----GVML----------SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTV--II 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 472 IAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDNP---QKPYTQALLAASLDPDPDVQAANRNA 533
Cdd:PRK10789 506 SAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQSgwyRDMYRYQQLEAALDDAPEIREEAVDA 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
276-505 |
2.81e-19 |
|
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: 91.34 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYG-DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMspgDLFKLRRDL 354
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDP---TQSL--NPRMTVYQLISEAWIIhpEILPKAKWRERVGEL-LG-QVGLSLEHMgryphQFSGGQRQRIAIA 427
Cdd:TIGR01193 551 NYLPQEPyifSGSIleNLLLGAKENVSQDEIW--AACEIAEIKDDIENMpLGyQTELSEEGS-----SISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 428 RALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmgiAFIFIAHDLPlVRDFADYVMVMQKGEVVELGTVAQVFD 505
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
124-495 |
3.47e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 124 ISTTQAQAEALRLFKRVALPDAERALDKyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqR 203
Cdd:NF040905 111 IDWNETNRRARELLAKVGLDESPDTLVT---DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-K 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 204 ETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRD------------VYRNPQHAYTKkliaaapgkgemHEPEAq 271
Cdd:NF040905 187 AQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRAdevtedriirgmVGRDLEDRYPE------------RTPKI- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 272 GEPILSVKD---------ARKsygdfeALKGVSFDLKQGETVAVVGESGSGKSTLA----------RIllrleepdGGTA 332
Cdd:NF040905 254 GEVVFEVKNwtvyhplhpERK------VVDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgrsygrNI--------SGTV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 333 HWKGKDLFTMSPGDLFKL--------RRDLQMVFQDPTQSlNPRMTVYQLISEAWII--HPEILPKAKWRER-------- 394
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAglayvtedRKGYGLNLIDDIKR-NITLANLGKVSRRGVIdeNEEIKVAEEYRKKmniktpsv 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 395 ---VGELlgqvglslehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIF 471
Cdd:NF040905 399 fqkVGNL------------------SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIV 459
|
410 420
....*....|....*....|....
gi 2087084196 472 IAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:NF040905 460 ISSELPELLGMCDRIYVMNEGRIT 483
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
4.23e-19 |
|
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: 85.61 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 4 HLLEVRNLSVDFHTVTgtvhAVRNISYYLDRGETLAI-----------LGesgsgksvsssAIMNLIdmPPgkiTSGEIL 72
Cdd:COG4133 1 MMLEAENLSCRRGERL----LFSGLSFTLAAGEALALtgpngsgkttlLR-----------ILAGLL--PP---SAGEVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 LDGKDLLKMSAEARRevngrRIAMIFQDPlsHLNPVYTVgwqmREAL----KTHGISTTQAQAEALrlFKRVALPDAEra 148
Cdd:COG4133 61 WNGEPIRDAREDYRR-----RLAYLGHAD--GLKPELTV----RENLrfwaALYGLRADREAIDEA--LEAVGLAGLA-- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 149 lDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgVLIITHD 215
Cdd:COG4133 126 -DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
66-239 |
4.40e-19 |
|
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: 86.52 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 66 ITSGEILLDGKDLLKMSAEARRevngRRIAMIFQD-PLSHLNPVYTVGW--------QMREALKTHGISTtqaqaealrl 136
Cdd:cd03253 53 VSSGSILIDGQDIREVTLDSLR----RAIGVVPQDtVLFNDTIGYNIRYgrpdatdeEVIEAAKAAQIHD---------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 137 fKRVALPDA------ERALdkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQreTGMGVL 210
Cdd:cd03253 119 -KIMRFPDGydtivgERGL-----KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTI 190
|
170 180
....*....|....*....|....*....
gi 2087084196 211 IITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:cd03253 191 VIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-242 |
7.57e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 7 EVRNLSVDFH----------TVTG-------TVHAVRNISYYLDRGETLAILGEsgsgksvsssaimN------LIDMPP 63
Cdd:COG4586 3 EVENLSKTYRvyekepglkgALKGlfrreyrEVEAVDDISFTIEPGEIVGFIGP-------------NgagkstTIKMLT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 64 GKI--TSGEILLDGKDLLKmsaeaRREVNGRRIAMIF-QDplSHLN---PVYtvgwqmrealkthgisttqaqaEALRLF 137
Cdd:COG4586 70 GILvpTSGEVRVLGYVPFK-----RRKEFARRIGVVFgQR--SQLWwdlPAI----------------------DSFRLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 138 KRV-ALPDAE--RALDKYPHEF-------------SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKEL 201
Cdd:COG4586 121 KAIyRIPDAEykKRLDELVELLdlgelldtpvrqlSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2087084196 202 QRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRD 242
Cdd:COG4586 201 NRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
274-507 |
9.35e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfkLRRD 353
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDPTQSLNprMTVYQLISEAWiiHPEILPKAKW----RERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARA 429
Cdd:PRK09536 79 VASVPQDTSLSFE--FDVRQVVEMGR--TPHRSRFDTWtetdRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNP 507
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
68-234 |
1.10e-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: 84.91 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKmSAEARREVngrriAMIFQDP--LSHLNPVYTVGWQMREALKTHGISTTQAQAEAlrlfKRVALPDA 145
Cdd:TIGR01277 52 SGSIKVNDQSHTG-LAPYQRPV-----SMLFQENnlFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAA----QQVGIADY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 eraLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADR 225
Cdd:TIGR01277 122 ---LDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQ 198
|
....*....
gi 2087084196 226 VVVMEKGQL 234
Cdd:TIGR01277 199 IAVVSQGKI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
278-484 |
1.12e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 278 VKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHwkgkdlftmspgdlfkLRRDLQMV 357
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS----------------IPKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 F--QDPTqsLNPRMTVYQLISEAwiiHPEILP-KAKWRE--------------------------------RVGELLGQV 402
Cdd:COG0488 65 YlpQEPP--LDDDLTVLDTVLDG---DAELRAlEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 403 GLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDvsvqAQVITLLDKLRKEMGIAFIFIAHDlplvRDF 482
Cdd:COG0488 140 GFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHD----RYF 211
|
..
gi 2087084196 483 AD 484
Cdd:COG0488 212 LD 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
273-506 |
1.43e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPD----------GGTAHWKGKdlftm 342
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellGRTVQREGR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 343 SPGDLFKLRRDLQMVFQDptQSLNPRMTVYQ-LISEAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQ----FS 417
Cdd:PRK09984 77 LARDIRKSRANTGYIFQQ--FNLVNRLSVLEnVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQrvstLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 418 GGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVEL 497
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*....
gi 2087084196 498 GTvAQVFDN 506
Cdd:PRK09984 235 GS-SQQFDN 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-238 |
1.57e-18 |
|
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: 83.73 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVdfhtVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidmPPGKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03217 1 LEIKDLHV----SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH---PKYEVTEGEILFKGEDITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RrevnGRR-IAMIFQDPLshlnpvytvgwqmrealKTHGISTtqaqAEALRlfkrvalpdaeraldkYPHE-FSGGQRQR 163
Cdd:cd03217 74 R----ARLgIFLAFQYPP-----------------EIPGVKN----ADFLR----------------YVNEgFSGGEKKR 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEV-ADRVVVMEKGQLVESG 238
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
66-247 |
1.72e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.21 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 66 ITSGEILLDGkdllkmsaearREVNG-----RRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQaealrlfKRV 140
Cdd:PRK11650 56 ITSGEIWIGG-----------RVVNElepadRDIAMVFQN--YALYPHMSVRENMAYGLKIRGMPKAEIE-------ERV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 141 AlpDAERA------LDKYPHEFSGGQRQRVmiAMALAL--KPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLII 212
Cdd:PRK11650 116 A--EAARIleleplLDRKPRELSGGQRQRV--AMGRAIvrEPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYV 191
|
170 180 190
....*....|....*....|....*....|....*
gi 2087084196 213 THDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNP 247
Cdd:PRK11650 192 THDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-531 |
1.82e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.53 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAH-----WKGKDLFTMSpgDLF 348
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYR--DVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 KLRRDLQMVFQDPtqslNP-RMTVYQLISEAWIIHpEILPKAKWRERVGELLGQVGL---SLEHMGRYPHQFSGGQRQRI 424
Cdd:PRK14271 98 EFRRRVGMLFQRP----NPfPMSIMDNVLAGVRAH-KLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 425 AIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIafIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
250 260
....*....|....*....|....*..
gi 2087084196 505 DNPQKPYTQALLAASldpDPDVQAANR 531
Cdd:PRK14271 251 SSPKHAETARYVAGL---SGDVKDAKR 274
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
113-229 |
2.28e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 113 WQMREALKTHGISTTQAQAEALRlfkRVALPD-AERALDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQ 191
Cdd:NF040873 83 WARRGLWRRLTRDDRAAVDDALE---RVGLADlAGRQLG----ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
90 100 110
....*....|....*....|....*....|....*...
gi 2087084196 192 AEVLALLKELqRETGMGVLIITHDLGVVSEvADRVVVM 229
Cdd:NF040873 156 ERIIALLAEE-HARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-238 |
2.76e-18 |
|
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: 84.31 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 15 FHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSvsssaimNLIDMPPGKI--TSGEILLDGKDLLKmsaeaRREVNGR 92
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKT-------TTLKILSGLLqpTSGEVRVAGLVPWK-----RRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 93 RIAMIFQDPlshlnpvYTVGWQM--REALKTH----GISTTQAQAealRLFKRVALPDAERALDKYPHEFSGGQRQRVMI 166
Cdd:cd03267 95 RIGVVFGQK-------TQLWWDLpvIDSFYLLaaiyDLPPARFKK---RLDELSELLDLEELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 167 AMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
69-258 |
3.01e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGK-DLLKMSAEARReVN----GRRIAMIFQDPlsHLNP----------VYTVGWqmREALKTHGISTTQAQAEA 133
Cdd:PRK14258 61 SEVRVEGRvEFFNQNIYERR-VNlnrlRRQVSMVHPKP--NLFPmsvydnvaygVKIVGW--RPKLEIDDIVESALKDAD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 134 LrlfkrvaLPDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIIT 213
Cdd:PRK14258 136 L-------WDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVS 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087084196 214 HDLGVVSEVADRVVVMEK-----GQLVESGTVRDVYRNPQHAYTKKLIAA 258
Cdd:PRK14258 209 HNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
285-503 |
3.12e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 285 YGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDLQMVFQDPTQS 364
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV---ARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 365 LNprMTVYQLISEAWIIHPEILpkAKWR----ERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCD 440
Cdd:PRK10253 94 GD--ITVQELVARGRYPHQPLF--TRWRkedeEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 441 EAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-239 |
4.32e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 4 HLLEVRNLS--VDFHTVT----GTVHAVRNISYYLDRGETLAILGESGSgksvsssaimnlidmppGKIT---------- 67
Cdd:PRK13657 324 GAIDLGRVKgaVEFDDVSfsydNSRQGVEDVSFEAKPGQTVAIVGPTGA-----------------GKSTlinllqrvfd 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 --SGEILLDGKDLLKMSAEARRevngRRIAMIFQDPLShLNPvytvgwQMREALKTHGISTTQAqaEALRLFKRVALPD- 144
Cdd:PRK13657 387 pqSGRILIDGTDIRTVTRASLR----RNIAVVFQDAGL-FNR------SIEDNIRVGRPDATDE--EMRAAAERAQAHDf 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERALDKYP-------HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLG 217
Cdd:PRK13657 454 IERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS 531
|
250 260
....*....|....*....|..
gi 2087084196 218 VVSEvADRVVVMEKGQLVESGT 239
Cdd:PRK13657 532 TVRN-ADRILVFDNGRVVESGS 552
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
67-235 |
4.91e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSaeaRREVN--GRRIAMIFQDplSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALPD 144
Cdd:PRK10908 55 SAGKIWFSGHDITRLK---NREVPflRRQIGMIFQD--HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERaldKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQReTGMGVLIITHDLGVVSEVAD 224
Cdd:PRK10908 130 KAK---NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSY 205
|
170
....*....|.
gi 2087084196 225 RVVVMEKGQLV 235
Cdd:PRK10908 206 RMLTLSDGHLH 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
272-504 |
5.43e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.08 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 272 GEPILSVKDA-RKSYGDFE--------ALKGVSFDLKQGETV--------------AVVGESGSGKSTLARILLRLEEPD 328
Cdd:PRK10790 315 GERVFELMDGpRQQYGNDDrplqsgriDIDNVSFAYRDDNLVlqninlsvpsrgfvALVGHTGSGKSTLASLLMGYYPLT 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 329 GGTAHWKGKDLFTMSPGdlfKLRRDLQMVFQDP---TQSLNPRMTVYQLISEawiihpeilpkakwrERVGELLGQVGLS 405
Cdd:PRK10790 395 EGEIRLDGRPLSSLSHS---VLRQGVAMVQQDPvvlADTFLANVTLGRDISE---------------EQVWQALETVQLA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 406 L----------EHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMgiAFIFIAHD 475
Cdd:PRK10790 457 ElarslpdglyTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHR 534
|
250 260
....*....|....*....|....*....
gi 2087084196 476 LPLVRDfADYVMVMQKGEVVELGTVAQVF 504
Cdd:PRK10790 535 LSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-245 |
6.49e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.78 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSVDFHTVT-GTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPgkiTSGEI-LLDGKDLLK 80
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVL--EP---TSGEVnVRVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSaEARREVNGRR---IAMIFQDplSHLNPVYTVGWQMREALKTHgISTTQAQAEALRLFKRVALPD--AERALDKYPHE 155
Cdd:TIGR03269 352 MT-KPGPDGRGRAkryIGILHQE--YDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEekAEEILDKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|
gi 2087084196 236 ESGTVRDVYR 245
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
290-504 |
6.69e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 290 ALKGVSFDLKQGETVAVVGESGSGKSTLARILLrleepdgGTAHWKGKDLFTMSPGDLFKLRRDL-QMVFQDPTQSLNPR 368
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLASGKISILGQPTRQALQKNLvAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 369 MTVYQLISEAWIIHPEIL--PKAKWRERVGELLGQVGLsLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSAL 446
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLrrAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 447 DVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVmVMQKGEVVELGTVAQVF 504
Cdd:PRK15056 174 DVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTF 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
67-234 |
7.05e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEiLLDGKDLLkmsAEARREvngrrIAMIFQDplSHLNPVYTVGWQMREALKTHGisttqaQAEALRLFKRVALpdAE 146
Cdd:PRK11247 65 SAGE-LLAGTAPL---AEARED-----TRLMFQD--ARLLPWKKVIDNVGLGLKGQW------RDAALQALAAVGL--AD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RALDkYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDlgvVSE---VA 223
Cdd:PRK11247 126 RANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD---VSEavaMA 201
|
170
....*....|.
gi 2087084196 224 DRVVVMEKGQL 234
Cdd:PRK11247 202 DRVLLIEEGKI 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
288-496 |
7.39e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.70 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 288 FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmspgdlfklrrdlqmvfqdptqslnp 367
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN---------------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 368 rmtvyQLISEAWIIhpEILPKAKWRERVGELLGQVGLS---LehMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVS 444
Cdd:COG2401 95 -----QFGREASLI--DAIGRKGDFKDAVELLNAVGLSdavL--WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 445 ALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFA-DYVMVMQKGEVVE 496
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-248 |
7.60e-18 |
|
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: 82.59 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 32 LDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDllkmSAEARREVN--GRRIAMIFQDPLSHLNPVY 109
Cdd:TIGR03771 3 ADKGELLGLLGPNGAGKTTLLRAILGLI-----PPAKGTVKVAGAS----PGKGWRHIGyvPQRHEFAWDFPISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 110 T-----VGWQMREALKTHgisttQAQAEALRlfkRVALpdAERAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTT 184
Cdd:TIGR03771 74 SgrtghIGWLRRPCVADF-----AAVRDALR---RVGL--TELA-DRPVGELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 185 ALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMeKGQLVESGTVRDVyRNPQ 248
Cdd:TIGR03771 143 GLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL-QDPA 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
67-238 |
8.85e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAeARREVngrriAMIFQDP--LSHLNPVYTVGWQMREALKThgistTQAQAEALR-LFKRVALP 143
Cdd:PRK10771 52 ASGSLTLNGQDHTTTPP-SRRPV-----SMLFQENnlFSHLTVAQNIGLGLNPGLKL-----NAAQREKLHaIARQMGIE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 DAeraLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVA 223
Cdd:PRK10771 121 DL---LARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIA 197
|
170
....*....|....*
gi 2087084196 224 DRVVVMEKGQLVESG 238
Cdd:PRK10771 198 PRSLVVADGRIAWDG 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
140-243 |
9.28e-18 |
|
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: 82.51 E-value: 9.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 140 VALPDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVV 219
Cdd:TIGR01184 99 IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
90 100
....*....|....*....|....
gi 2087084196 220 SEVADRVVVMEKGQLVESGTVRDV 243
Cdd:TIGR01184 179 LLLSDRVVMLTNGPAANIGQILEV 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
291-502 |
1.29e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPD---GGTAHWKGKdlftmsPGDLFKLRRDLQMVFQDptQSLNP 367
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM------PIDAKEMRAISAYVQQD--DLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 368 RMTVY-QLISEAWIIHPEILPKAKWRERVGELLGQVGLS------LEHMGRYpHQFSGGQRQRIAIARALALEPQLIVCD 440
Cdd:TIGR00955 113 TLTVReHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcantrIGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 441 EAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
157-447 |
1.43e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.33 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRET-GMGVLIITHDLgvvsEVADR---VVVMEKG 232
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYM----EEAERfdwLVAMDAG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 233 QLVESGTVRDVYrnpQHAYTKKLIAA-----APGKGEMHEP--------EAQGEPILSVKDARKSYGDFEALKGVSFDLK 299
Cdd:NF033858 214 RVLATGTPAELL---ARTGADTLEAAfiallPEEKRRGHQPvvipprpaDDDDEPAIEARGLTMRFGDFTAVDHVSFRIR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 300 QGETVAVVGESGSGKSTLARILLRLEEPDGGTAhWkgkdLF--TMSPGDLFKLRRDLQMvfqdpTQ--SLNPRMTVYQ-L 374
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-W----LFgqPVDAGDIATRRRVGYM-----SQafSLYGELTVRQnL 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 375 ISEAWIIHpeiLPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALD 447
Cdd:NF033858 361 ELHARLFH---LPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
67-247 |
2.02e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARrevnGRRIAMIFQD-PLSHlnpvytvGWQMRE-----------ALKTHGISTTQAQAEAL 134
Cdd:PRK10575 64 SEGEILLDAQPLESWSSKAF----ARKVAYLPQQlPAAE-------GMTVRElvaigrypwhgALGRFGAADREKVEEAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 135 RLfkrVAL-PDAERALDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIIT 213
Cdd:PRK10575 133 SL---VGLkPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVL 205
|
170 180 190
....*....|....*....|....*....|....
gi 2087084196 214 HDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNP 247
Cdd:PRK10575 206 HDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
265-503 |
2.50e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 265 MHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSp 344
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 GDLFKlrRDLQMVFQDPTQSLNprMTVYQLISeawiihpeiLPKAKW-----------RERVGELLGQVGLS-LEHmgRY 412
Cdd:PRK10575 80 SKAFA--RKVAYLPQQLPAAEG--MTVRELVA---------IGRYPWhgalgrfgaadREKVEEAISLVGLKpLAH--RL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 413 PHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKG 492
Cdd:PRK10575 145 VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
250
....*....|.
gi 2087084196 493 EVVELGTVAQV 503
Cdd:PRK10575 225 EMIAQGTPAEL 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
294-503 |
2.51e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 294 VSFDLKQGETVAVVGESGSGKST-LARI--LLrleePDGGTAHWKGKDLFTMSPGDLFKLRRDLqmvfqdpTQSLNP--R 368
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTlLARMagLL----PGSGSIQFAGQPLEAWSAAELARHRAYL-------SQQQTPpfA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 369 MTVYQLiseaWIIH-PEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGG--QRQRIA-----IARALALEPQLIVCD 440
Cdd:PRK03695 84 MPVFQY----LTLHqPDKTRTEAVASALNEVAEALGLD-DKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 441 EAVSALDVSVQAqvitLLDKLRKEM---GIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:PRK03695 159 EPMNSLDVAQQA----ALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
67-236 |
2.59e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARREVNGRRIAMIFQDPL--SHLNPVYTVgwQMREALKthGISTTQAQAEALRLFKRVALpd 144
Cdd:PRK10584 63 SSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliPTLNALENV--ELPALLR--GESSRQSRNGAKALLEQLGL-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERaLDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvAD 224
Cdd:PRK10584 137 GKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CD 214
|
170
....*....|..
gi 2087084196 225 RVVVMEKGQLVE 236
Cdd:PRK10584 215 RRLRLVNGQLQE 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
67-239 |
2.76e-17 |
|
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: 81.43 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPlsHLnpvytvgwqmrealkthgISTTQAQAEALRLFKRVALPDAE 146
Cdd:cd03249 56 TSGEILLDGVDIRDLNLRWLR----SQIGLVSQEP--VL------------------FDGTIAENIRYGKPDATDEEVEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RALDKYPHEF-------------------SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGM 207
Cdd:cd03249 112 AAKKANIHDFimslpdgydtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GR 189
|
170 180 190
....*....|....*....|....*....|..
gi 2087084196 208 GVLIITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:cd03249 190 TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
273-496 |
2.80e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlftmspgdlfklrr 352
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 dlQMVFQDPTQSLN-------------PRMTVY------QLISEAWIIHPEILpkakwRERVGELLGQVGLSLEhmgryP 413
Cdd:PRK11288 67 --EMRFASTTAALAagvaiiyqelhlvPEMTVAenlylgQLPHKGGIVNRRLL-----NYEAREQLEHLGVDID-----P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 414 HQ----FSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVM 489
Cdd:PRK11288 135 DTplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVF 213
|
....*..
gi 2087084196 490 QKGEVVE 496
Cdd:PRK11288 214 KDGRYVA 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-239 |
3.22e-17 |
|
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: 80.73 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 20 GTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLIdMPPGKITSGEILLDGKDLLKMSAEARREvngrRIAMIFQ 99
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKT----TLINLL-MRFYDPQKGQILIDGIDIRDISRKSLRS----MIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 100 DP------------LSHLNPVYTVgwqMREALKthgisttqaQAEALRLFKRvaLPDAeraLDKYPHE----FSGGQRQR 163
Cdd:cd03254 85 DTflfsgtimenirLGRPNATDEE---VIEAAK---------EAGAHDFIMK--LPNG---YDTVLGEnggnLSQGERQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDV----TVQAEVLALLKelqretGMGVLIITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTetekLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-242 |
3.41e-17 |
|
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: 84.77 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSvdfHTVTGT-VHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSA 83
Cdd:TIGR02203 330 DVEFRNVT---FRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE-----PDSGQILLDGHDLADYTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EARRevngRRIAMIFQDplSHL-------NPVYTVGWQMREAlkthGISTTQAQAEALRLFKRvaLPDAeraLDKYPHE- 155
Cdd:TIGR02203 402 ASLR----RQVALVSQD--VVLfndtianNIAYGRTEQADRA----EIERALAAAYAQDFVDK--LPLG---LDTPIGEn 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 ---FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVsEVADRVVVMEKG 232
Cdd:TIGR02203 467 gvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDG 543
|
250
....*....|
gi 2087084196 233 QLVESGTVRD 242
Cdd:TIGR02203 544 RIVERGTHNE 553
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
68-494 |
3.49e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.40 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDL-LKMSAEARRevNGrrIAMIFQDplshLNPVYTVG-----WQMREALKTHGISTTQAQAEALRLFKrva 141
Cdd:PRK10982 52 SGSILFQGKEIdFKSSKEALE--NG--ISMVHQE----LNLVLQRSvmdnmWLGRYPTKGMFVDQDKMYRDTKAIFD--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 142 lpdaERALDKYPHE----FSGGQRQRVMIAMALALKPDLLIADEPTTALdvtVQAEVLALLKELQ--RETGMGVLIITHD 215
Cdd:PRK10982 121 ----ELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 216 LGVVSEVADRVVVMEKGQLVESGTVRDVYrnpqhayTKKLIAAAPGKGEMHE-PEAQGEP---ILSVKDArkSYGDFEAL 291
Cdd:PRK10982 194 MEEIFQLCDEITILRDGQWIATQPLAGLT-------MDKIIAMMVGRSLTQRfPDKENKPgevILEVRNL--TSLRQPSI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 292 KGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDL----FKL----RR------DLQMV 357
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgFALvteeRRstgiyaYLDIG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPTQSLNPRMTVYQLISEA-------WIIHPEILPKAKWRERVGELlgqvglslehmgryphqfSGGQRQRIAIARAL 430
Cdd:PRK10982 345 FNSLISNIRNYKNKVGLLDNSrmksdtqWVIDSMRVKTPGHRTQIGSL------------------SGGNQQKVIIGRWL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKL-RKEMGIafIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
284-481 |
4.28e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 284 SYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSP-----GDLFKLR-RDLQMV 357
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPqrsevPDSLPLTvRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPTQSLNPRMTvyqliseawiihpeilpkAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLI 437
Cdd:NF040873 81 GRWARRGLWRRLT------------------RDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2087084196 438 VCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRD 481
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
291-502 |
5.75e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.09 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARIL--L------RLEEPDGGTAhwkgkdLFT-----MSPGDLfklrRDlQMV 357
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIagLwpygsgRIARPAGARV------LFLpqrpyLPLGTL----RE-ALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPTQSLNprmtvyqliseawiihpeilpkakwRERVGELLGQVGLS-----LEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:COG4178 448 YPATAEAFS-------------------------DAELREALEAVGLGhlaerLDEEADWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQvitLLDKLRKEM-GIAFIFIAHDLPLvRDFADYVMVMQKGEVVELGTVAQ 502
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAA---LYQLLREELpGTTVISVGHRSTL-AAFHDRVLELTGDGSWQLLPAEA 569
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
68-239 |
6.17e-17 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 84.22 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLlkmsAEARREVNGRRIAMIFQDplshlnpVYTVGWQMREALKTHgiSTTQAQAEALRLFKRVALPDAER 147
Cdd:TIGR03796 533 SGEILFDGIPR----EEIPREVLANSVAMVDQD-------IFLFEGTVRDNLTLW--DPTIPDADLVRACKDAAIHDVIT 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 AL-DKYPHE-------FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLkelqRETGMGVLIITHDLGVV 219
Cdd:TIGR03796 600 SRpGGYDAElaegganLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLSTI 675
|
170 180
....*....|....*....|
gi 2087084196 220 SEvADRVVVMEKGQLVESGT 239
Cdd:TIGR03796 676 RD-CDEIIVLERGKVVQRGT 694
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
291-498 |
6.24e-17 |
|
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: 80.01 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAhwkGKDLFTMSPGDLFKLRRDLQMVFQDPTqsLNPRMT 370
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS---GQILFNGQPRKPDQFQKCVAYVRQDDI--LLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLISEAWIIH-PEILPKAKWRERVG-ELLGQVGLSleHMG-RYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALD 447
Cdd:cd03234 98 VRETLTYTAILRlPRKSSDAIRKKRVEdVLLRDLALT--RIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 448 VSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELG 498
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
157-447 |
6.36e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 83.53 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVE 236
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 237 SGTVRDVYRN---PQHAYTKKLIAAA-PGKGE--MHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGES 310
Cdd:PRK10938 216 TGEREEILQQalvAQLAHSEQLEGVQlPEPDEpsARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 311 GSGKSTlariLLRLEEPDggtaHWKG--KDLFtmspgdLFKLRR------------------DLQMVFQDPTQSLNPRMT 370
Cdd:PRK10938 296 GAGKST----LLSLITGD----HPQGysNDLT------LFGRRRgsgetiwdikkhigyvssSLHLDYRVSTSVRNVILS 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 -------VYQLISEAwiihpeilpkakWRERVGELLGQVGLSlEHMGRYP-HQFSGGQrQRIA-IARALALEPQLIVCDE 441
Cdd:PRK10938 362 gffdsigIYQAVSDR------------QQKLAQQWLDILGID-KRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDE 427
|
....*.
gi 2087084196 442 AVSALD 447
Cdd:PRK10938 428 PLQGLD 433
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
282-506 |
7.02e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 7.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 282 RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGkdlftMSPgdlFKLRRDLQ----MV 357
Cdd:COG4586 29 RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVP---FKRRKEFArrigVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPTQsLNPRMTVYqlisEAWIIHPEI--LPKAKWRERVGELLGQvgLSLEHMGRYP-HQFSGGQRQRIAIARALALEP 434
Cdd:COG4586 101 FGQRSQ-LWWDLPAI----DSFRLLKAIyrIPDAEYKKRLDELVEL--LDLGELLDTPvRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDN 506
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
123-246 |
7.71e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 123 GISTTQAQAEALRLFKRVALPdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQ 202
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLN 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2087084196 203 RETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRN 246
Cdd:PRK13645 198 KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-247 |
7.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 7.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 24 AVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSaearrEVNGRR--IAMIFQDP 101
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL-----RPQKGKVLVSGIDTGDFS-----KLQGIRklVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 102 LSHLnpvytVGWQMREALkthGISTTQAQAEALRLFKRVALPDAERALDKY----PHEFSGGQRQRVMIAMALALKPDLL 177
Cdd:PRK13644 87 ETQF-----VGRTVEEDL---AFGPENLCLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 178 IADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVsEVADRVVVMEKGQLVESGTVRDVYRNP 247
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-244 |
9.11e-17 |
|
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: 79.58 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 12 SVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSAEARRevng 91
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD-----VDSGRILIDGHDVRDYTLASLR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 92 RRIAMIFQDplshlnpVYTVGWQMRE--ALKTHGISTTQA-----QAEALRLFKRvaLPDA------ERALdkyphEFSG 158
Cdd:cd03251 76 RQIGLVSQD-------VFLFNDTVAEniAYGRPGATREEVeeaarAANAHEFIME--LPEGydtvigERGV-----KLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 159 GQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVsEVADRVVVMEKGQLVESG 238
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTI-ENADRIVVLEDGKIVERG 218
|
....*.
gi 2087084196 239 TVRDVY 244
Cdd:cd03251 219 THEELL 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-244 |
1.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSVDFHTVTgTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMppgkiTSGEILLDGKDLLKMS 82
Cdd:PRK13642 2 NKILEVENLVFKYEKES-DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-----FEGKVKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARRevngRRIAMIFQDPLSHLNPVyTVGWQMREALKTHGISTTQAQAEALRLFKRVALPDAEralDKYPHEFSGGQRQ 162
Cdd:PRK13642 76 VWNLR----RKIGMVFQNPDNQFVGA-TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK---TREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvADRVVVMEKGQLVESGTVRD 242
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
..
gi 2087084196 243 VY 244
Cdd:PRK13642 227 LF 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
68-239 |
1.36e-16 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 83.08 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARRevngRRIAMIFQDplSHLNPvytvGWQMREALKTHGISTTQAQaEALRLfkrVALPDAER 147
Cdd:TIGR03797 507 SGSVFYDGQDLAGLDVQAVR----RQLGVVLQN--GRLMS----GSIFENIAGGAPLTLDEAW-EAARM---AGLAEDIR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 ALDKYPH--------EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQ--RetgmgvLIITHDLG 217
Cdd:TIGR03797 573 AMPMGMHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKvtR------IVIAHRLS 646
|
170 180
....*....|....*....|..
gi 2087084196 218 VVSEvADRVVVMEKGQLVESGT 239
Cdd:TIGR03797 647 TIRN-ADRIYVLDAGRVVQQGT 667
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-257 |
1.81e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.44 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITSGEILLDGKDLLKM 81
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 82 SAEARrEVNgRRIAMIFQDPLSHLNPVY-TVGWQMRealkthgISTTQAQAEAL--RLFKRVALPD-AERALDKYPHEFS 157
Cdd:PRK14243 83 DVDPV-EVR-RRIGMVFQKPNPFPKSIYdNIAYGAR-------INGYKGDMDELveRSLRQAALWDeVKDKLKQSGLSLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 158 GGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtgMGVLIITHDLGVVSEVAD-----RVVVMEK- 231
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDmtaffNVELTEGg 231
|
250 260
....*....|....*....|....*....
gi 2087084196 232 ---GQLVESGTVRDVYRNPQHAYTKKLIA 257
Cdd:PRK14243 232 gryGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
276-479 |
2.18e-16 |
|
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: 77.78 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfklRRDLQ 355
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD------EPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTQSLNPRMTVYQLISEAWIIHpeilpkAKWRERVGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALALEP 434
Cdd:TIGR01189 75 ILYLGHLPGLKPELSALENLHFWAAIH------GGAQRTIEDALAAVGLTgFED--LPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLV 479
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-234 |
2.31e-16 |
|
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: 81.79 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSVdFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmpPGKItSGEILLDGKDL-LKM 81
Cdd:TIGR02633 255 DVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY---PGKF-EGNVFINGKPVdIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 82 SAEARREvngrRIAMIFQDPLSH-LNPVYTVGWQMREAL--KTHGISTTQAQAEA-------LRLFKRVALPDAERAldk 151
Cdd:TIGR02633 330 PAQAIRA----GIAMVPEDRKRHgIVPILGVGKNITLSVlkSFCFKMRIDAAAELqiigsaiQRLKVKTASPFLPIG--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 152 yphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEK 231
Cdd:TIGR02633 403 ---RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGE 478
|
...
gi 2087084196 232 GQL 234
Cdd:TIGR02633 479 GKL 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
291-486 |
2.60e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHwkgkdlftmSPGDlfklrRDLQMVFQDPtqslnprmt 370
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------MPEG-----EDLLFLPQRP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 vYqliseawiihpeiLPkakwrerVGELLGQVglslehmgRYP--HQFSGGQRQRIAIARALALEPQLIVCDEAVSALDV 448
Cdd:cd03223 74 -Y-------------LP-------LGTLREQL--------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 2087084196 449 SVQAQVITLLdklrKEMGIAFIFIAHDlPLVRDFADYV 486
Cdd:cd03223 125 ESEDRLYQLL----KELGITVISVGHR-PSLWKFHDRV 157
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
276-493 |
2.66e-16 |
|
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: 75.95 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlftmspgdlfklrrdlq 355
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 mvfqdptqslnprmtvyqliseawiihpeilpkakwrERVGellgqvglslehmgrYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03221 63 -------------------------------------VKIG---------------YFEQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKemgiAFIFIAHDLPLVRDFADYVMVMQKGE 493
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-243 |
2.74e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMppgkiTSGEILLDGKDLLKMSAea 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP-----TAGTVLVAGDDVEALSA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 rREVnGRRIAMIFQD-PLSHLNPVYTVgWQM-----REALKTHGISTTQAQAEALrlfkrvALPDAERALDKYPHEFSGG 159
Cdd:PRK09536 73 -RAA-SRRVASVPQDtSLSFEFDVRQV-VEMgrtphRSRFDTWTETDRAAVERAM------ERTGVAQFADRPVTSLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 160 QRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGT 239
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
....
gi 2087084196 240 VRDV 243
Cdd:PRK09536 223 PADV 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
291-508 |
3.39e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.13 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDPT-------Q 363
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVlfdgtvrQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 SLNPRMTVYQliSEAWiihpEILPKAKWRERVG-ELLGQVGLSLEHMGRYphqfSGGQRQRIAIARALALEPQ-LIVCDE 441
Cdd:PTZ00243 1403 NVDPFLEASS--AEVW----AALELVGLRERVAsESEGIDSRVLEGGSNY----SVGQRQLMCMARALLKKGSgFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 442 AVS----ALDVSVQAQVITlldklrkemgiAF-----IFIAHDLPLVRDFaDYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PTZ00243 1473 ATAnidpALDRQIQATVMS-----------AFsaytvITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-283 |
3.51e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.62 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 3 DHLLEVRNLSvdFHTVTGTvHAVRNISYYLDRGETLAILGESGSGKSVSSSAiMNLIDMPpgkiTSGEILLDGKDLlkmS 82
Cdd:PRK13647 2 DNIIEVEDLH--FRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLH-LNGIYLP----QRGRVKVMGREV---N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 83 AEARREVNGRrIAMIFQDPLSHLNPVyTVgWqmrEALKTHGISTTQAQAEALRlfkRVAlpDAERAL------DKYPHEF 156
Cdd:PRK13647 71 AENEKWVRSK-VGLVFQDPDDQVFSS-TV-W---DDVAFGPVNMGLDKDEVER---RVE--EALKAVrmwdfrDKPPYHL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVE 236
Cdd:PRK13647 140 SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2087084196 237 SGTVRdVYRNPQHAYTKKLIAAAPGKGEMHEPEAQGEPI-LSVKDARK 283
Cdd:PRK13647 219 EGDKS-LLTDEDIVEQAGLRLPLVAQIFEDLPELGQSKLpLTVKEAVQ 265
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
156-534 |
4.95e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 80.98 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVqaeVLALLKELQRETGMGVLIiTHDLGVVSEVADRVVVMEKGQLV 235
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILI-SHDRDFLDPIVDKIIHIEQQSLF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 236 E-SGTV--------------RDVYRNPQHAYTK----------------------------KLIAAA----PGKGEMHEP 268
Cdd:PRK10636 226 EyTGNYssfevqratrlaqqQAMYESQQERVAHlqsyidrfrakatkakqaqsrikmlermELIAPAhvdnPFHFSFRAP 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 269 EAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT-AHWKGKDLFTMSPGDL 347
Cdd:PRK10636 306 ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiGLAKGIKLGYFAQHQL 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 348 FKLRRDlqmvfQDPTQSLN---PRMTVYQLiseawiihpeilpkakwrervGELLGQVGLSLEHMGRYPHQFSGGQRQRI 424
Cdd:PRK10636 386 EFLRAD-----ESPLQHLArlaPQELEQKL---------------------RDYLGGFGFQGDKVTEETRRFSGGEKARL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 425 AIARALALEPQLIVCDEAVSALDVSV-QAQVITLLDklrkeMGIAFIFIAHDLPLVRDFADYVMVMQKGEVvelgtvaQV 503
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMrQALTEALID-----FEGALVVVSHDRHLLRSTTDDLYLVHDGKV-------EP 507
|
410 420 430
....*....|....*....|....*....|....*..
gi 2087084196 504 FDNPQKPYTQALL------AASLDPDPDVQAANRNAR 534
Cdd:PRK10636 508 FDGDLEDYQQWLSdvqkqeNQTDEAPKENNANSAQAR 544
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-229 |
5.22e-16 |
|
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: 80.79 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSAEA 85
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-----PTEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDP----------LSHLNPVYTVGwQMREALKthgisttqaQAEALRLFKrvALPDA-ERALDKYPH 154
Cdd:TIGR02857 394 WR----DQIAWVPQHPflfagtiaenIRLARPDASDA-EIREALE---------RAGLDEFVA--ALPQGlDTPIGEGGA 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVsEVADRVVVM 229
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-498 |
5.91e-16 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 77.52 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLE--EPDGGTAHWKGKDLFTMSPGDlfKLRR 352
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQDPTQSLNprmtvyqlISEAWIIHPEILPKAKWRER-----------VGELLGQVGLSLEHMGRYPHQ-FSGGQ 420
Cdd:PRK09580 79 GIFMAFQYPVEIPG--------VSNQFFLQTALNAVRSYRGQepldrfdfqdlMEEKIALLKMPEDLLTRSVNVgFSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 421 RQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGiAFIFIAHdLPLVRDF--ADYVMVMQKGEVVELG 498
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
69-244 |
6.00e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGK--DLLKMSAEARREvngrRIAMIFQDPLSHLnpVYT-VGWQMREALKTHGIsttqAQAE-ALRLFKRVALPD 144
Cdd:PRK13638 56 GAVLWQGKplDYSKRGLLALRQ----QVATVFQDPEQQI--FYTdIDSDIAFSLRNLGV----PEAEiTRRVDEALTLVD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVAD 224
Cdd:PRK13638 126 AQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISD 204
|
170 180
....*....|....*....|
gi 2087084196 225 RVVVMEKGQLVESGTVRDVY 244
Cdd:PRK13638 205 AVYVLRQGQILTHGAPGEVF 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-247 |
6.53e-16 |
|
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: 77.20 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDL--LKMSA 83
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV-----KPDSGKILLDGQDItkLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EARR-------EvngrriAMIFQDplshlnpvYTVGWQMREALKTHGISTTQAQAEA---LRLFKrvalpdAERALDKYP 153
Cdd:cd03218 72 RARLgigylpqE------ASIFRK--------LTVEENILAVLEIRGLSKKEREEKLeelLEEFH------ITHLRKSKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQ 233
Cdd:cd03218 132 SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
250
....*....|....
gi 2087084196 234 LVESGTVRDVYRNP 247
Cdd:cd03218 211 VLAEGTPEEIAANE 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
273-506 |
7.74e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 80.32 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDA--RKSYGDFE-ALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK-DLFTMSPGdlf 348
Cdd:PRK13545 19 KPFDKLKDLffRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 klrrdlqmvfqdptqsLNPRMTVYQLIseawiihpEI--LPKAKWRERVGELLGQVgLSLEHMGRYPHQ----FSGGQRQ 422
Cdd:PRK13545 96 ----------------LNGQLTGIENI--------ELkgLMMGLTKEKIKEIIPEI-IEFADIGKFIYQpvktYSSGMKS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 423 RIAIARALALEPQLIVCDEAVSALDvsvQAQVITLLDKLR--KEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTV 500
Cdd:PRK13545 151 RLGFAISVHINPDILVIDEALSVGD---QTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
....*.
gi 2087084196 501 AQVFDN 506
Cdd:PRK13545 228 KEVVDH 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-239 |
1.37e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNlsVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLI----DmppgkITSGEILLDGKDLLKM 81
Cdd:PRK11176 342 IEFRN--VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKS----TIANLLtrfyD-----IDEGEILLDGHDLRDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 82 SAEARREvngrRIAMIFQDplSHL-------NPVYTVGWQM-REAlkthgISTTQAQAEALRLFKRValpdaERALDKYP 153
Cdd:PRK11176 411 TLASLRN----QVALVSQN--VHLfndtianNIAYARTEQYsREQ-----IEEAARMAYAMDFINKM-----DNGLDTVI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HE----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETgmGVLIITHDLGVVsEVADRVVVM 229
Cdd:PRK11176 475 GEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTI-EKADEILVV 551
|
250
....*....|
gi 2087084196 230 EKGQLVESGT 239
Cdd:PRK11176 552 EDGEIVERGT 561
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
157-247 |
1.99e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDvtvqAEVLALLKELQRETGMGVLIITHDLGVVsEVADRVVVMEKGQLVE 236
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVE 693
|
90
....*....|.
gi 2087084196 237 SGTVRDVYRNP 247
Cdd:TIGR00958 694 MGTHKQLMEDQ 704
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
68-243 |
2.01e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARRevngRRIAMIFQ-DPLSHLNPVYtvgwqmrEALKTHGISTTQAQAEALRLfkrVALPDAE 146
Cdd:COG4138 49 QGEILLNGRPLSDWSAAELA----RHRAYLSQqQSPPFAMPVF-------QYLALHQPAGASSEAVEQLL---AQLAEAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 147 RALDKYP---HEFSGGQRQRVMIAMAL-----ALKPD--LLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDL 216
Cdd:COG4138 115 GLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDL 193
|
170 180
....*....|....*....|....*..
gi 2087084196 217 GVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:COG4138 194 NHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-238 |
2.97e-15 |
|
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: 74.93 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNlsVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAEA 85
Cdd:cd03245 3 IEFRN--VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY-----KPTSGSVLLDGTDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDPlsHLnpvytVGWQMREALKT-HGISTTQAQAEALRLFKRVALpdaeraLDKYPHEF-------- 156
Cdd:cd03245 76 LR----RNIGYVPQDV--TL-----FYGTLRDNITLgAPLADDERILRAAELAGVTDF------VNKHPNGLdlqigerg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 ---SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgvLIITHDLGVVSeVADRVVVMEKGQ 233
Cdd:cd03245 139 rglSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLLD-LVDRIIVMDSGR 215
|
....*
gi 2087084196 234 LVESG 238
Cdd:cd03245 216 IVADG 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
276-458 |
3.13e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGdlfklrrdLQ 355
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA--------EA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTQSLNPRMTVyqliseawiihPEILpkAKWRERVGELLGQVGLSLEHMGRYP------HQFSGGQRQRIAIARA 429
Cdd:PRK13539 75 CHYLGHRNAMKPALTV-----------AENL--EFWAAFLGGEELDIAAALEAVGLAPlahlpfGYLSAGQKRRVALARL 141
|
170 180
....*....|....*....|....*....
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLL 458
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
156-243 |
3.16e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
....*...
gi 2087084196 236 ESGTVRDV 243
Cdd:PRK10253 224 AQGAPKEI 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-245 |
3.26e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLlEVRNLSVDFHTV------------------TGTVHAVRNISYYLDRGETLAILGESGSgksvsssaimnlidmp 62
Cdd:COG1134 1 MSSMI-EVENVSKSYRLYhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGA---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 63 pGKITsgeilldgkdLLKMSA------EARREVNGRRIAMI-----FQDPLSHLNPVYTVGwqmreALktHGISttqaQA 131
Cdd:COG1134 64 -GKST----------LLKLIAgileptSGRVEVNGRVSALLelgagFHPELTGRENIYLNG-----RL--LGLS----RK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 132 EALRLFKRVAlpD-AEraLDKYPHE----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETG 206
Cdd:COG1134 122 EIDEKFDEIV--EfAE--LGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESG 196
|
250 260 270
....*....|....*....|....*....|....*....
gi 2087084196 207 MGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYR 245
Cdd:COG1134 197 RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
152-233 |
3.29e-15 |
|
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: 72.87 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 152 YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetgmGVLIITHDLGVVSEVADRVVVMEK 231
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELED 142
|
..
gi 2087084196 232 GQ 233
Cdd:cd03221 143 GK 144
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-247 |
3.50e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGesgsgksvsssaimnlidmPPG--------------KI 66
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIG-------------------PNGagkttvfncltgfyKP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKDLLKMSAE--ARREV-----NGR--RIAMIFQDPL----SHLNPVYTVGwqmreALKTHGI--STTQAQA 131
Cdd:PRK11300 58 TGGTILLRGQHIEGLPGHqiARMGVvrtfqHVRlfREMTVIENLLvaqhQQLKTGLFSG-----LLKTPAFrrAESEALD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 132 EALRLFKRVALPD-AERALDKypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVL 210
Cdd:PRK11300 133 RAATWLERVGLLEhANRQAGN----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVL 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 2087084196 211 IITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRNP 247
Cdd:PRK11300 209 LIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-238 |
5.13e-15 |
|
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: 73.74 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVHA--VRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppGKITSGEILLDGKDLlkmsa 83
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVLINGRPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 eaRREVNGRRIAMIFQDplSHLNPVYTVgwqmREALKThgisttqaqaeALRLfkrvalpdaeRALdkyphefSGGQRQR 163
Cdd:cd03213 76 --DKRSFRKIIGYVPQD--DILHPTLTV----RETLMF-----------AAKL----------RGL-------SGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 164 VMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDL-GVVSEVADRVVVMEKGQLVESG 238
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
126-243 |
6.33e-15 |
|
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: 74.74 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 126 TTQAQAEALRLFKRVALpdAERAlDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRET 205
Cdd:COG1119 116 TDEQRERARELLELLGL--AHLA-DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEG 192
|
90 100 110
....*....|....*....|....*....|....*...
gi 2087084196 206 GMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:COG1119 193 APTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-239 |
7.03e-15 |
|
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: 74.06 E-value: 7.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 24 AVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidMPPgkiTSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPLs 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVP---ENGRVLVDGHDLALADPAWLR----RQVGVVLQENV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 104 hlnpvyTVGWQMREalkthGISTTQAQAEALRLFKRVALPDAERALDKYPHEF-----------SGGQRQRVMIAMALAL 172
Cdd:cd03252 87 ------LFNRSIRD-----NIALADPGMSMERVIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 173 KPDLLIADEPTTALDVTVQAEVLALLKELQreTGMGVLIITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
131-448 |
7.54e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRLfkrvalPDAERALDKypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDvtvqAE-VLALLKELQRETGMgV 209
Cdd:PRK11819 149 MDALRC------PPWDAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPGT-V 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 210 LIITHDLGVVSEVADRVVVMEKGQLV-----------------------ESGTVRDVYR-------NP--QHAYTKKLIA 257
Cdd:PRK11819 214 VAVTHDRYFLDNVAGWILELDRGRGIpwegnysswleqkakrlaqeekqEAARQKALKRelewvrqSPkaRQAKSKARLA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 258 A-----------APGKGEMHEPEAQ--GEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRL 324
Cdd:PRK11819 294 RyeellseeyqkRNETNEIFIPPGPrlGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 325 EEPDGGTahwkgkdlftmspgdlFKLRRDLQMVFQDptQS---LNPRMTVYQLISEawiihpeilpkakwrervgellgq 401
Cdd:PRK11819 374 EQPDSGT----------------IKIGETVKLAYVD--QSrdaLDPNKTVWEEISG------------------------ 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 402 vGLSLEHMGRY---------------PHQ------FSGGQRQRIAIARALALEPQLIVCDEAVSALDV 448
Cdd:PRK11819 412 -GLDIIKVGNReipsrayvgrfnfkgGDQqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-239 |
7.83e-15 |
|
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: 73.22 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVhaVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSAEA 85
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDPLSHLNPVytvgwqmREALKTHGISTTQAQAEALRLfkrvalpdAERALDkypheFSGGQRQRVM 165
Cdd:cd03369 80 LR----SSLTIIPQDPTLFSGTI-------RSNLDPFDEYSDEEIYGALRV--------SEGGLN-----LSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 166 IAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQreTGMGVLIITHDLGVVSEVaDRVVVMEKGQLVESGT 239
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-249 |
1.05e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNLSVDfhtvTGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLI--DMPPgkiTSGEILLDGKDLL 79
Cdd:PRK11831 4 VANLVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIggQIAP---DHGEILFDGENIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 80 KMSAEARREVNgRRIAMIFQDP--LSHLNPVYTVGWQMREalktHgistTQAQAEALRL-----FKRVALPDAERALdky 152
Cdd:PRK11831 73 AMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----H----TQLPAPLLHStvmmkLEAVGLRGAAKLM--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 153 PHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKG 232
Cdd:PRK11831 141 PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK 220
|
250
....*....|....*..
gi 2087084196 233 QLVESGTVRDVYRNPQH 249
Cdd:PRK11831 221 KIVAHGSAQALQANPDP 237
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-502 |
1.15e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 269 EAQGEPILSVKDARksygdfeALKGVSFDLKQGETVAVVGESGSGKSTLARILLrleepdgGTAHWKG---------KDL 339
Cdd:PRK11174 351 EAEDLEILSPDGKT-------LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-------GFLPYQGslkingielREL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 340 ftmspgDLFKLRRDLQMVFQDPT---QSL-------NPRMT---VYQLISEAWIihPEILPKakwrervgelLGQvGLSL 406
Cdd:PRK11174 417 ------DPESWRKHLSWVGQNPQlphGTLrdnvllgNPDASdeqLQQALENAWV--SEFLPL----------LPQ-GLDT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 407 ---EHMGRyphqFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDFa 483
Cdd:PRK11174 478 pigDQAAG----LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW- 550
|
250
....*....|....*....
gi 2087084196 484 DYVMVMQKGEVVELGTVAQ 502
Cdd:PRK11174 551 DQIWVMQDGQIVQQGDYAE 569
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-239 |
1.16e-14 |
|
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: 73.30 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 24 AVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmppgkITSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPL- 102
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE-----LSSGSILIDGVDISKIGLHDLR----SRISIIPQDPVl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 103 ------SHLNP--VYTvGWQMREALK-THGISTTQAQAEALRlfkrvaLPDAERALDkypheFSGGQRQRVMIAMALALK 173
Cdd:cd03244 90 fsgtirSNLDPfgEYS-DEELWQALErVGLKEFVESLPGGLD------TVVEEGGEN-----LSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 174 PDLLIADEPTTALDVTVQAEVLALLKElqRETGMGVLIITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
66-248 |
1.24e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 66 ITSGEILLDGKdllKMSAEARREvngRRIAMIFQdplSH-LNPVYTVGWQMREALKTHGISTTQAQ------AEALRLfk 138
Cdd:PRK11000 55 ITSGDLFIGEK---RMNDVPPAE---RGVGMVFQ---SYaLYPHLSVAENMSFGLKLAGAKKEEINqrvnqvAEVLQL-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 139 rvalpdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALD----VTVQAEVLALLKELQREtgmgVLIITH 214
Cdd:PRK11000 124 -------AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRT----MIYVTH 192
|
170 180 190
....*....|....*....|....*....|....
gi 2087084196 215 DLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:PRK11000 193 DQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
156-234 |
1.51e-14 |
|
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: 71.48 E-value: 1.51e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEvADRVVVMEKGQL 234
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
276-493 |
1.55e-14 |
|
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: 72.50 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDA-----RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLrleepdggtahwkgkdlftmspGDLFKL 350
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL----------------------GELEKL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 351 RRDLQMvfqdptqslNPRMT-VYQlisEAWI----IHPEIL---P-KAKWRERV---------------GEL--LGQVGL 404
Cdd:cd03250 59 SGSVSV---------PGSIAyVSQ---EPWIqngtIRENILfgkPfDEERYEKVikacalepdleilpdGDLteIGEKGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 405 SLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVIT--LLDKLRKemGIAFIFIAHDLPLVRDf 482
Cdd:cd03250 127 NL----------SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH- 193
|
250
....*....|.
gi 2087084196 483 ADYVMVMQKGE 493
Cdd:cd03250 194 ADQIVVLDNGR 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
155-266 |
1.60e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADrVVVMEKGQL 234
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
90 100 110
....*....|....*....|....*....|....
gi 2087084196 235 VESGTVRDVY--RNPQHAYTKKLIAAAPGKGEMH 266
Cdd:PRK15056 220 LASGPTETTFtaENLELAFSGVLRHVALNGSEES 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
273-447 |
1.60e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmsPGDLFKLRR 352
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQMVFQdpTQSLNPRMTVyqliSEAWIIHPEI--LPKAKWRERVGELLGQVGLSLEHMGRYpHQFSGGQRQRIAIARAL 430
Cdd:PRK13537 81 RVGVVPQ--FDNLDPDFTV----RENLLVFGRYfgLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARAL 153
|
170
....*....|....*..
gi 2087084196 431 ALEPQLIVCDEAVSALD 447
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLD 170
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
274-495 |
1.67e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 274 PILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfkLRRD 353
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDptQSLNPRMTVyqliSEAWIIHPEILPKAKWRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALE 433
Cdd:PRK11614 82 VAIVPEG--RRVFSRMTV----EENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
280-509 |
2.06e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 280 DARKsygDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT-----AH---------WKGKD------- 338
Cdd:PTZ00265 393 DTRK---DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDiiindSHnlkdinlkwWRSKIgvvsqdp 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 339 -LFT-----------MSPGDLFKLRRDLQMVFQDPTQSLNPRMTV--------------------------YQLISEAWI 380
Cdd:PTZ00265 470 lLFSnsiknnikyslYSLKDLEALSNYYNEDGNDSQENKNKRNSCrakcagdlndmsnttdsneliemrknYQTIKDSEV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 381 IhpEILPKAKWRERVGELLGQVGLSLehmGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDK 460
Cdd:PTZ00265 550 V--DVSKKVLIHDFVSALPDKYETLV---GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2087084196 461 LRKEMGIAFIFIAHDLPLVRdFADYVMVMQKGEVVELGTVAQVFDNPQK 509
Cdd:PTZ00265 625 LKGNENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDPTK 672
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
288-478 |
2.38e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 288 FEALkgvSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSP---GDLFKL------RRDLQmvf 358
Cdd:PRK13538 17 FSGL---SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhQDLLYLghqpgiKTELT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 359 qdPTQSLNPRMTVYQLISEawiihpeilpkakwrERVGELLGQVGLS-LEHMgryP-HQFSGGQRQRIAIARaLALEPQ- 435
Cdd:PRK13538 91 --ALENLRFYQRLHGPGDD---------------EALWEALAQVGLAgFEDV---PvRQLSAGQQRRVALAR-LWLTRAp 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2087084196 436 LIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPL 478
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
68-248 |
2.66e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAearREVNGRRIAMIFQDPLSHLNPVytvgWQMreaLKTHGISTTQAQAEalrlfkRVALPDAER 147
Cdd:PRK03695 49 SGSIQFAGQPLEAWSA---AELARHRAYLSQQQTPPFAMPV----FQY---LTLHQPDKTRTEAV------ASALNEVAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 AL---DKYP---HEFSGGQRQRVMIAMAL-----ALKPD--LLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITH 214
Cdd:PRK03695 113 ALgldDKLGrsvNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSH 191
|
170 180 190
....*....|....*....|....*....|....
gi 2087084196 215 DLGVVSEVADRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:PRK03695 192 DLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
291-483 |
3.30e-14 |
|
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: 71.37 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPgdlfKLRRDLQMVFQDPtqSLNPRMT 370
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD----SIARGLLYLGHAP--GIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYQLISEAWIIHPeilpkakwRERVGELLGQVGLS-LEHmgRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVS 449
Cdd:cd03231 90 VLENLRFWHADHS--------DEQVEEALARVGLNgFED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|....
gi 2087084196 450 VQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFA 483
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGA 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-262 |
4.92e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSvdfhtvtGTvhAVRNISYYLDRGETLAIlgesGSGKSVSSSAIMNLI--DMPpgkITSGEILLDGKDLLKMSA 83
Cdd:PRK10762 258 LKVDNLS-------GP--GVNDVSFTLRKGEILGV----SGLMGAGRTELMKVLygALP---RTSGYVTLDGHEVVTRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 84 EARREvNGrrIAMIFQD----------------PLSHLNPVYTVGWQMREAlkthgiSTTQAQAEALRLFKrVALPDAER 147
Cdd:PRK10762 322 QDGLA-NG--IVYISEDrkrdglvlgmsvkenmSLTALRYFSRAGGSLKHA------DEQQAVSDFIRLFN-IKTPSMEQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 ALDKypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVV 227
Cdd:PRK10762 392 AIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRIL 466
|
250 260 270
....*....|....*....|....*....|....*
gi 2087084196 228 VMEKGQLveSGTVrdvyrNPQHAYTKKLIAAAPGK 262
Cdd:PRK10762 467 VMHEGRI--SGEF-----TREQATQEKLMAAAVGK 494
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
291-506 |
6.03e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDPTQ------- 363
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLfsgtvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 SLNPrmtvYQLISEA--WiihpEILPKAKWRERVGEllGQVGLSLEhMGRYPHQFSGGQRQRIAIARALALEPQLIVCDE 441
Cdd:PLN03130 1332 NLDP----FNEHNDAdlW----ESLERAHLKDVIRR--NSLGLDAE-VSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 442 AVSALDVSVQAqvitLLDK-LRKEM-GIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDN 506
Cdd:PLN03130 1401 ATAAVDVRTDA----LIQKtIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-238 |
6.49e-14 |
|
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: 71.15 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 27 NISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPGKITSGEILLDGKdllkmsaEARREVNGRRIAMIFQDP--LSH 104
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGQ-------PRKPDQFQKCVAYVRQDDilLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 105 LnpvyTVgwqmREAL------KTHGISTT---QAQAEALRLfKRVALpdaERALDKYPHEFSGGQRQRVMIAMALALKPD 175
Cdd:cd03234 96 L----TV----RETLtytailRLPRKSSDairKKRVEDVLL-RDLAL---TRIGGNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 176 LLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGV-VSEVADRVVVMEKGQLVESG 238
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-238 |
6.67e-14 |
|
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: 74.52 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNlsVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidMPPgkiTSGEILLDGKDLLKMSAEA 85
Cdd:TIGR03375 464 IEFRN--VSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGL--YQP---TEGSVLLDGVDIRQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDP-LSH--------LNPVYTVGWQMREALKTHGIST-TQAQAEALrlfkrvALPDAERALdkyphE 155
Cdd:TIGR03375 537 LR----RNIGYVPQDPrLFYgtlrdniaLGAPYADDEEILRAAELAGVTEfVRRHPDGL------DMQIGERGR-----S 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVsEVADRVVVMEKGQLV 235
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
...
gi 2087084196 236 ESG 238
Cdd:TIGR03375 679 ADG 681
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
267-499 |
7.79e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 267 EPEAQGEPILSVKDARKSYGD--FEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSP 344
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 GDLfklRRDLQMVFQDP---TQSL--NPRMTvyqliseawiihpeiLPKAKwRERVGELLGQVGLS--LEHM-------- 409
Cdd:PRK11160 410 AAL---RQAISVVSQRVhlfSATLrdNLLLA---------------APNAS-DEALIEVLQQVGLEklLEDDkglnawlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 410 --GRyphQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLPLVRDFaDYVM 487
Cdd:PRK11160 471 egGR---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRIC 544
|
250
....*....|..
gi 2087084196 488 VMQKGEVVELGT 499
Cdd:PRK11160 545 VMDNGQIIEQGT 556
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
157-239 |
1.07e-13 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 74.01 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVSEvADRVVVMEKGQLVE 236
Cdd:TIGR01846 595 SGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
...
gi 2087084196 237 SGT 239
Cdd:TIGR01846 672 SGR 674
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
66-239 |
1.15e-13 |
|
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: 73.70 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 66 ITSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPlshlnpV-------YTVGW--------QMREAlkthgisttqAQ 130
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLR----AAIGIVPQDT------VlfndtiaYNIAYgrpdaseeEVEAA----------AR 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRLFKRvALPDA------ERALdkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRe 204
Cdd:COG5265 470 AAQIHDFIE-SLPDGydtrvgERGL-----KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR- 542
|
170 180 190
....*....|....*....|....*....|....*
gi 2087084196 205 tGMGVLIITHDLGVVSEvADRVVVMEKGQLVESGT 239
Cdd:COG5265 543 -GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
156-238 |
1.67e-13 |
|
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: 68.88 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETgmGVLIITHDLGVVsEVADRVVVMEKGQLV 235
Cdd:cd03247 99 FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGI-EHMDKILFLENGKII 175
|
...
gi 2087084196 236 ESG 238
Cdd:cd03247 176 MQG 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
155-238 |
2.50e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
....
gi 2087084196 235 VESG 238
Cdd:cd03220 221 RFDG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
146-230 |
2.92e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.12 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADR 225
Cdd:COG1245 446 EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDR 525
|
....*
gi 2087084196 226 VVVME 230
Cdd:COG1245 526 LMVFE 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
286-505 |
3.05e-13 |
|
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: 72.67 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 286 GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmsPGDLFKLRRDLQ--MVFQDPtq 363
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQAWIQNDSLRenILFGKA-- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 sLNPRMtvYQLISEAWIIHP--EILPKAKWRErvgelLGQVGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDE 441
Cdd:TIGR00957 725 -LNEKY--YQQVLEACALLPdlEILPSGDRTE-----IGEKGVNL----------SGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 442 AVSALDVSVQAQVitlLDKLRKEMGI----AFIFIAHD---LPLVrdfaDYVMVMQKGEVVELGTVAQVFD 505
Cdd:TIGR00957 787 PLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGisyLPQV----DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-229 |
3.24e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 2 ADHLLEVRNlsVDFHTvtGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmpPgkiTSGEILLDGKDLLKM 81
Cdd:PRK10247 4 NSPLLQLQN--VGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--P---TSGTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 82 SAEARREvngrRIAMIFQDPLSHLNPVY---TVGWQMREalkthgistTQAQAEALRLF-KRVALPdaERALDKYPHEFS 157
Cdd:PRK10247 75 KPEIYRQ----QVSYCAQTPTLFGDTVYdnlIFPWQIRN---------QQPDPAIFLDDlERFALP--DTILTKNIAELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 158 GGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEvADRVVVM 229
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-488 |
5.09e-13 |
|
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: 68.97 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 283 KSYGDF--EALKGvsfDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAhwkGKDLFTMSpgdlFKlrrdlqmvfqd 360
Cdd:cd03237 8 KTLGEFtlEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVS----YK----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 361 pTQSLNPR--MTVYQLISEawiIHPEILPKAKWRERVGELLGQVGLslehMGRYPHQFSGGQRQRIAIARALALEPQLIV 438
Cdd:cd03237 67 -PQYIKADyeGTVRDLLSS---ITKDFYTHPYFKTEIAKPLQIEQI----LDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 439 CDEAVSALDV---SVQAQVIT-LLDKLRKemgIAFIfIAHDLPLVRDFADYVMV 488
Cdd:cd03237 139 LDEPSAYLDVeqrLMASKVIRrFAENNEK---TAFV-VEHDIIMIDYLADRLIV 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
273-493 |
5.61e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 273 EPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmspgdLFKLRR 352
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-------TFNGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 353 DLQ-----MVFQDptqsLN--PRMTvyqlISEAWIIHPEI---LPKAKWRERVGE---LLGQVGLSlehmgRYPHQFSG- 418
Cdd:PRK10762 75 SSQeagigIIHQE----LNliPQLT----IAENIFLGREFvnrFGRIDWKKMYAEadkLLARLNLR-----FSSDKLVGe 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 419 ---GQRQRIAIARALALEPQLIVCDEAVSAL-DVSVQA--QVITLLdklrKEMGIAFIFIAHDLPLVRDFADYVMVMQKG 492
Cdd:PRK10762 142 lsiGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESlfRVIREL----KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
.
gi 2087084196 493 E 493
Cdd:PRK10762 218 Q 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
140-249 |
6.64e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 140 VALPDAERALDKYPHEFSGGQRQRVMIAMALA-LKPD--------LLIADEPTTALDVTVQAEVLALLKELQRETGMGVL 210
Cdd:PRK13547 130 LALAGATALVGRDVTTLSGGELARVQFARVLAqLWPPhdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVL 209
|
90 100 110
....*....|....*....|....*....|....*....
gi 2087084196 211 IITHDLGVVSEVADRVVVMEKGQLVESGTVRDVYRnPQH 249
Cdd:PRK13547 210 AIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
291-509 |
7.64e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLfklRRDLQMVFQDP-----TQSL 365
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPvlfsgTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTVYQLISEAWiihpEILPKAKWRERVGEllGQVGLSLEhMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSA 445
Cdd:PLN03232 1329 NIDPFSEHNDADLW----EALERAHIKDVIDR--NPFGLDAE-VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 446 LDVSVQAqvitLLDK-LRKEM-GIAFIFIAHDLPLVRDfADYVMVMQKGEVVElgtvaqvFDNPQK 509
Cdd:PLN03232 1402 VDVRTDS----LIQRtIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQE 1455
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
157-234 |
1.54e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.54e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
157-234 |
2.61e-12 |
|
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: 66.34 E-value: 2.61e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKE-LQRETgmgVLIITHDLGVVsEVADRVVVMEKGQL 234
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwPERRT---VLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
65-248 |
2.87e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDL--LKMSAEARR-------EvngrriAMIFQDplshLnpvyTVGWQMREALKTHGISTTQAQAEAlr 135
Cdd:COG1137 54 KPDSGRIFLDGEDIthLPMHKRARLgigylpqE------ASIFRK----L----TVEDNILAVLELRKLSKKEREERL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 136 lfkrvalpdaERALDkyphEF-------------SGGQRQRVMIAMALALKPDLLIADEPTTALD-VTVqAEVLALLKEL 201
Cdd:COG1137 118 ----------EELLE----EFgithlrkskayslSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 202 qRETGMGVLIITHD----LGVVsevaDRVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:COG1137 183 -KERGIGVLITDHNvretLGIC----DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
130-248 |
3.23e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 130 QAEALRLFKRValpDAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGV 209
Cdd:PRK09544 98 KEDILPALKRV---QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAV 174
|
90 100 110
....*....|....*....|....*....|....*....
gi 2087084196 210 LIITHDLGVVSEVADRVVVMeKGQLVESGTVRDVYRNPQ 248
Cdd:PRK09544 175 LMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
275-508 |
3.41e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDlfKLRRDL 354
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPtqSLNPRMTVYQLISEAWIIHPEiLPKAKWRERVGELLGQvgLSLEHMGRYPHQ-FSGGQRQRIAIARALALE 433
Cdd:PRK10895 81 GYLPQEA--SIFRRLSVYDNLMAVLQIRDD-LSAEQREDRANELMEE--FHIEHLRDSMGQsLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRkEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQVFDNPQ 508
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
291-512 |
3.94e-12 |
|
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: 66.47 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDPTQ------- 363
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 SLNPRMTVYQliSEAWiihpEILPKAKWRERVGELLGQVGLSLEHMGRyphQFSGGQRQRIAIARALALEPQLIVCDEAV 443
Cdd:cd03288 114 NLDPECKCTD--DRLW----EALEIAQLKNMVKSLPGGLDAVVTEGGE---NFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 444 SALDVSVQaqvitllDKLRKEMGIAF-----IFIAHDLPLVRDfADYVMVMQKGEVVELGTVAQVFDNPQKPYT 512
Cdd:cd03288 185 ASIDMATE-------NILQKVVMTAFadrtvVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
146-230 |
4.26e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADR 225
Cdd:PRK13409 444 ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDR 523
|
....*
gi 2087084196 226 VVVME 230
Cdd:PRK13409 524 LMVFE 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
291-503 |
4.51e-12 |
|
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: 69.20 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSpgdLFKLRRDLQMVFQDP---TQSLNP 367
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPvlfSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 368 RMTVYQLIS--EAWIIhpeiLPKAKWRERVGELLGQVGLSLEHMGRyphQFSGGQRQRIAIARALALEPQLIVCDEAVSA 445
Cdd:TIGR00957 1379 NLDPFSQYSdeEVWWA----LELAHLKTFVSALPDKLDHECAEGGE---NLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 446 LDVS----VQAQVITLLDKlrkemgIAFIFIAHDLPLVRDFADyVMVMQKGEVVELGTVAQV 503
Cdd:TIGR00957 1452 VDLEtdnlIQSTIRTQFED------CTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNL 1506
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
157-243 |
4.61e-12 |
|
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: 68.24 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSeVADRVVVMEKGQLVE 236
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLA-AVDKLLVLRDGRVQA 546
|
....*..
gi 2087084196 237 SGTVRDV 243
Cdd:COG4618 547 FGPRDEV 553
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-447 |
4.75e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 280 DARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmsPGDLFKLRRDLQMVFQ 359
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 360 dpTQSLNPRMTVYQLI-------------SEAWIihPEILPKA----KWRERVGELlgqvglslehmgryphqfSGGQRQ 422
Cdd:PRK13536 122 --FDNLDLEFTVRENLlvfgryfgmstreIEAVI--PSLLEFArlesKADARVSDL------------------SGGMKR 179
|
170 180
....*....|....*....|....*
gi 2087084196 423 RIAIARALALEPQLIVCDEAVSALD 447
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLD 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-216 |
4.88e-12 |
|
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: 68.16 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFhtvTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDmPPGkitsGEILLDGKDLLKMSAEA 85
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-PLQ----GEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RRevngRRIAMIFQDPlsHLNPVyTVGWQMREALKThgisttQAQAEALRLFKRVALPDAERAL----DKYPHE----FS 157
Cdd:TIGR02868 407 VR----RRVSVCAQDA--HLFDT-TVRENLRLARPD------ATDEELWAALERVGLADWLRALpdglDTVLGEggarLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 158 GGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLkeLQRETGMGVLIITHDL 216
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
68-248 |
6.05e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKD--LLKMSAEARREVNG-RRIAMIFQDpLSHLNPVYTVgWQMREALkthgiSTTQAQAEALRLFKRVALpd 144
Cdd:PRK10895 57 AGNIIIDDEDisLLPLHARARRGIGYlPQEASIFRR-LSVYDNLMAV-LQIRDDL-----SAEQREDRANELMEEFHI-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 aERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVAD 224
Cdd:PRK10895 128 -EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCE 205
|
170 180
....*....|....*....|....
gi 2087084196 225 RVVVMEKGQLVESGTVRDVYRNPQ 248
Cdd:PRK10895 206 RAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
275-496 |
7.55e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.51 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILlrleepDG----GTahWKGKDLFTmspGDL--F 348
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SGvyphGS--YEGEILFD---GEVcrF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 KLRRDlqmvfqdptqslnprmtvyqliSEAW---IIHPEIL---------------PKAK-----WRE---RVGELLGQV 402
Cdd:NF040905 70 KDIRD----------------------SEALgivIIHQELAlipylsiaeniflgnERAKrgvidWNEtnrRARELLAKV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 403 GLSlEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDF 482
Cdd:NF040905 128 GLD-ESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRV 205
|
250
....*....|....
gi 2087084196 483 ADYVMVMQKGEVVE 496
Cdd:NF040905 206 ADSITVLRDGRTIE 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
276-497 |
8.99e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGD--FeALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmSPGDLFKLRRD 353
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 354 LQMVFQDP---TQSLNPrmtvyqlisEAWIIHPEILpkAKWRERVGEllgQVGLSLEHmGRYPH-QFSGGQRQRIAIARA 429
Cdd:PRK10522 399 FSAVFTDFhlfDQLLGP---------EGKPANPALV--EKWLERLKM---AHKLELED-GRISNlKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 430 LALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDlPLVRDFADYVMVMQKGEVVEL 497
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
281-495 |
1.43e-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: 63.82 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 281 ARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDG---GTAHWKGKdlftmsPGDLFKLRRDLQMV 357
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGI------PYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPTQSLNPRMTVYQLIseawiihpeilpkakwrERVGELLGqvglslehmGRYPHQFSGGQRQRIAIARALALEPQLI 437
Cdd:cd03233 87 YVSEEDVHFPTLTVRETL-----------------DFALRCKG---------NEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 438 VCDEAVSALDVSVQAQVITLLDKLRKEMG-IAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
131-236 |
1.89e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRLFKRVALPDAERALDKYpHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVL 210
Cdd:COG2401 113 KDAVELLNAVGLSDAVLWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLV 191
|
90 100
....*....|....*....|....*..
gi 2087084196 211 IITHDLGVVSEVA-DRVVVMEKGQLVE 236
Cdd:COG2401 192 VATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
69-333 |
2.01e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 69 GEILLDGKDLLKMSAEARREVNGRRIAMIfQDPLSHLNpvytvGWQMRealkthgiSTTQAQAEALRLfkrvalpDAERA 148
Cdd:PRK11147 95 AEYLKRYHDISHLVETDPSEKNLNELAKL-QEQLDHHN-----LWQLE--------NRINEVLAQLGL-------DPDAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 149 LDkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQretgmGVLI-ITHDLGVVSEVADRVV 227
Cdd:PRK11147 154 LS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ-----GSIIfISHDRSFIRNMATRIV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 228 VMEKGQLVESGTVRDVY----------RNPQHA-YTKKL----------IAAAPGKGE-------------MHEPEAQGE 273
Cdd:PRK11147 225 DLDRGKLVSYPGNYDQYllekeealrvEELQNAeFDRKLaqeevwirqgIKARRTRNEgrvralkalrrerSERREVMGT 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 274 PILSVKDARKS-------------YGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAH 333
Cdd:PRK11147 305 AKMQVEEASRSgkivfemenvnyqIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-239 |
2.24e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNlsVDFHTVTGTVHAVRNISYYLDRGETLAILGESGSgksvsssaimnlidmppGKIT------------SGEIL 72
Cdd:PRK11160 338 SLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGC-----------------GKSTllqlltrawdpqQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 73 LDGKDLLKMSAEARRE---VNGRRIaMIFQDPLshlnpvytvgwqmREALKthgISTTQAQAEALR-LFKRV---ALPDA 145
Cdd:PRK11160 399 LNGQPIADYSEAALRQaisVVSQRV-HLFSATL-------------RDNLL---LAAPNASDEALIeVLQQVgleKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKYPHE----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLgVVSE 221
Cdd:PRK11160 462 DKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL-TGLE 538
|
250
....*....|....*...
gi 2087084196 222 VADRVVVMEKGQLVESGT 239
Cdd:PRK11160 539 QFDRICVMDNGQIIEQGT 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
66-239 |
2.55e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 66 ITSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPLSHLNPVY---TVGWQMREALKTHGISTTQAqAEALRlfkrvAL 142
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLR----QGVAMVQQDPVVLADTFLanvTLGRDISEEQVWQALETVQL-AELAR-----SL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PDA-ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgvLIITHDLGVVSE 221
Cdd:PRK10790 463 PDGlYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE 540
|
170
....*....|....*...
gi 2087084196 222 vADRVVVMEKGQLVESGT 239
Cdd:PRK10790 541 -ADTILVLHRGQAVEQGT 557
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
287-492 |
4.87e-11 |
|
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: 62.73 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 287 DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTMSPGDLFKLRR-DLQMVFQDP---T 362
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQKPwllN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 QSLNPRMTV--------YQLISEAWIIHPEI--LPKAKWRErvgelLGQVGLSLehmgryphqfSGGQRQRIAIARALAL 432
Cdd:cd03290 93 ATVEENITFgspfnkqrYKAVTDACSLQPDIdlLPFGDQTE-----IGERGINL----------SGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 433 EPQLIVCDEAVSALDVSV-----QAQVITLLDKLRKEMgiafIFIAHDLPLVrDFADYVMVMQKG 492
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKLQYL-PHADWIIAMKDG 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-243 |
8.50e-11 |
|
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: 64.29 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 25 VRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPgkiTSGEILLDGKDLLKMSaearREVNGRRIAMIFQDplSH 104
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIW--PP---TSGSVRLDGADLKQWD----RETFGKHIGYLPQD--VE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 105 LNPvYTVGW---QMREALKTHGISTTQAQAEALRLFKRvaLPDA-ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIAD 180
Cdd:TIGR01842 403 LFP-GTVAEniaRFGENADPEKIIEAAKLAGVHELILR--LPDGyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 181 EPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVsEVADRVVVMEKGQLVESGTVRDV 243
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEV 540
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-317 |
9.84e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 64.65 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMAL--ALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEvADRVVVM----- 229
Cdd:TIGR00630 490 SGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADYVIDIgpgag 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 230 -EKGQLVESGTVRDVYRNPQHaytkklIAAAPGKGEMHEP----EAQGEP-ILSVKDARKSygdfeALKGVSFDLKQGET 303
Cdd:TIGR00630 568 eHGGEVVASGTPEEILANPDS------LTGQYLSGRKKIEvpaeRRPGNGkFLTLKGAREN-----NLKNITVSIPLGLF 636
|
170
....*....|....
gi 2087084196 304 VAVVGESGSGKSTL 317
Cdd:TIGR00630 637 TCITGVSGSGKSTL 650
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-240 |
1.82e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.53 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 20 GTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmPPGKITSGEILLDGKdllKMSAEARRevngRRIAMIFQ 99
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLNGM---PIDAKEMR----AISAYVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 100 DPLshLNPVYTVgwqmREALKTHG-------ISTTQAQA------EALRLFK----RVALPDAERALdkyphefSGGQRQ 162
Cdd:TIGR00955 107 DDL--FIPTLTV----REHLMFQAhlrmprrVTKKEKRErvdevlQALGLRKcantRIGVPGRVKGL-------SGGERK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKEL-QRetGMGVLIITHDLGV-VSEVADRVVVMEKGQLVESGTV 240
Cdd:TIGR00955 174 RLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSP 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
152-214 |
2.02e-10 |
|
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: 59.47 E-value: 2.02e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 152 YP--HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqretGMGVLIITH 214
Cdd:cd03223 86 YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-240 |
3.03e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLsvdfHTVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNlidMPPGKITSGEILLDGKDLLK 80
Cdd:CHL00131 3 KNKPILEIKNL----HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYKILEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 MSAEARREvngRRIAMIFQDPLShLNPVYTVGWqMREALKTHGISTTQAQAEALRLF-------KRVALpdAERALDKYP 153
Cdd:CHL00131 76 LEPEERAH---LGIFLAFQYPIE-IPGVSNADF-LRLAYNSKRKFQGLPELDPLEFLeiineklKLVGM--DPSFLSRNV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 154 HE-FSGGQRQRVMI-AMALaLKPDLLIADEPTTALDV---TVQAEVLALLKELQRetgmGVLIITHDLGVVSEVA-DRVV 227
Cdd:CHL00131 149 NEgFSGGEKKRNEIlQMAL-LDSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVH 223
|
250
....*....|...
gi 2087084196 228 VMEKGQLVESGTV 240
Cdd:CHL00131 224 VMQNGKIIKTGDA 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
295-474 |
3.11e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.84 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 295 SFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTahwkgkdLFTMSPGDLFKLrrdlqmvfqdPTQslnPRMTVYQL 374
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR-------LTKPAKGKLFYV----------PQR---PYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 375 ISEawIIHPEILPKAKWR----ERVGELLGQVGL--------SLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:TIGR00954 532 RDQ--IIYPDSSEDMKRRglsdKDLEQILDNVQLthileregGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 2087084196 443 VSALDVSVQAQVITLLdklrKEMGIAFIFIAH 474
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
124-243 |
3.47e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.67 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 124 ISTTQAQAEALRLFKRVALPDAE-RALDKYphefSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQ 202
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAgRAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2087084196 203 REtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRDV 243
Cdd:NF000106 192 RD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
295-529 |
3.67e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 295 SFDLKQGETVAVVGESGSGKSTLARILlrleepdggtahwkgkdlftmsPGDLFKLRRDLQMVFQDPTqslnpRMTVYQL 374
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL----------------------AGELPLLSGERQSQFSHIT-----RLSFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 375 ---ISEAW------IIHPE-----------ILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALALEP 434
Cdd:PRK10938 76 qklVSDEWqrnntdMLSPGeddtgrttaeiIQDEVKDPARCEQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 435 QLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIA---HDLPlvrDFADYVMVMQKGEVVELGTVAQVFDN---PQ 508
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLnrfDEIP---DFVQFAGVLADCTLAETGEREEILQQalvAQ 230
|
250 260
....*....|....*....|.
gi 2087084196 509 KPYTQALLAASLdPDPDVQAA 529
Cdd:PRK10938 231 LAHSEQLEGVQL-PEPDEPSA 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
131-214 |
4.08e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.13 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRlfkRVALPDAERALDK---YPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKElqRETGM 207
Cdd:COG4178 461 REALE---AVGLGHLAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGT 535
|
....*..
gi 2087084196 208 GVLIITH 214
Cdd:COG4178 536 TVISVGH 542
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
146-230 |
5.59e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADR 225
Cdd:cd03237 106 EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADR 185
|
....*
gi 2087084196 226 VVVME 230
Cdd:cd03237 186 LIVFE 190
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
300-493 |
6.69e-10 |
|
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: 57.77 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 300 QGETVAVVGESGSGKSTLARILLRLEEPDGGtahwkgkDLFTMSPGDLFKLRRDLqmvfqdptqslnprmtvyqliseaw 379
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------GVIYIDGEDILEEVLDQ------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 380 iihpeilpkakwrervgellgqvgLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVI---- 455
Cdd:smart00382 49 ------------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLllee 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2087084196 456 -TLLDKLRKEMGIAFIFIAHDLP-----LVRDFADYVMVMQKGE 493
Cdd:smart00382 105 lRLLLLLKSEKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
275-495 |
7.82e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDggtahwKGKDLFTmspGDLFKLRrdL 354
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLD------DGRIIYE---QDLIVAR--L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QmvfQDPtqslnPRM---TVYQLISEAWIIHPEIL-------------PKAK-----------------WR--ERVGELL 399
Cdd:PRK11147 72 Q---QDP-----PRNvegTVYDFVAEGIEEQAEYLkryhdishlvetdPSEKnlnelaklqeqldhhnlWQleNRINEVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 400 GQVGLSlehmgryPHQ----FSGGQRQRIAIARALALEPQLIVCDEAVSALDVsvqaQVITLLDKLRKEMGIAFIFIAHD 475
Cdd:PRK11147 144 AQLGLD-------PDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
250 260
....*....|....*....|
gi 2087084196 476 LPLVRDFADYVMVMQKGEVV 495
Cdd:PRK11147 213 RSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-238 |
8.19e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.61 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 10 NLSVDFHTVT---GTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKITsgeilldgkdLLKMSAEAR 86
Cdd:PRK13536 39 TVAIDLAGVSksyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT----------VLGVPVPAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 87 REVNGRRIAMIFQdpLSHLNPVYTVgwqmREALKTHG----ISTTQAQA--EALRLFKRValpdaERALDKYPHEFSGGQ 160
Cdd:PRK13536 109 ARLARARIGVVPQ--FDNLDLEFTV----RENLLVFGryfgMSTREIEAviPSLLEFARL-----ESKADARVSDLSGGM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVMEKGQLVESG 238
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
68-243 |
1.05e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARRevngrRIAMIFQdpLSHLNPVYTVGWQMREALKTHGISTTQAQAEALRLFKRVALpdaER 147
Cdd:PRK13537 61 AGSISLCGEPVPSRARHARQ-----RVGVVPQ--FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKL---EN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 ALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHDLGVVSEVADRVV 227
Cdd:PRK13537 131 KADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLC 209
|
170
....*....|....*.
gi 2087084196 228 VMEKGQLVESGTVRDV 243
Cdd:PRK13537 210 VIEEGRKIAEGAPHAL 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
276-503 |
1.31e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLArILLRLEEPDGGTAHWKgkdlFTMSPGDLFKLRRDL- 354
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWR----F*TWCANRRALRRTIg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 --QMVFQDPTQSLNPRMTVYQliseawIIHPEILPKAKWRERVGELLGQVGLSlEHMGRYPHQFSGGQRQRIAIARALAL 432
Cdd:NF000106 89 *hRPVR*GRRESFSGRENLYM------IGR*LDLSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 433 EPQLIVCDEAVSALDVSVQAQVitlLDKLRKEM--GIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEV---WDEVRSMVrdGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
275-485 |
1.33e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 275 ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLftmsPGDLFKLRRdl 354
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPTQSLNPRMTVYQliSEAWIIHpeilpKAKWRERVGELLGQvgLSLEHMGRYP-HQFSGGQRQRIAIARALALE 433
Cdd:PRK13540 75 QLCFVGHRSGINPYLTLRE--NCLYDIH-----FSPGAVGITELCRL--FSLEHLIDYPcGLLSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 434 PQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVR-DFADY 485
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKaDYEEY 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
65-264 |
1.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKMSAEARRevngRRIAMIFQDPLSHLNpvyTVGWQMrEALKTHGisttqaQAEALRLFKRVALPD 144
Cdd:PLN03232 1287 ELEKGRIMIDDCDVAKFGLTDLR----RVLSIIPQSPVLFSG---TVRFNI-DPFSEHN------DADLWEALERAHIKD 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 145 AER----ALDKYPHE----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgvLIITHDL 216
Cdd:PLN03232 1353 VIDrnpfGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRL 1430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2087084196 217 GVVSEvADRVVVMEKGQLVESGTVRDVYRNPQHAYTKKLIAAAPGKGE 264
Cdd:PLN03232 1431 NTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQ 1477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
163-334 |
2.17e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDV-TVQ--AEVLAllkelQRETGMgvLIITHDL----GVVSEVADrvvvMEKGQL- 234
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDInTIRwlEDVLN-----ERNSTM--IIISHDRhflnSVCTHMAD----LDYGELr 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 235 VESGTVRDVYRNPQHAYTKKLIAAAPGKGEMHE----------------------------------PEAQGEP------ 274
Cdd:PRK15064 232 VYPGNYDEYMTAATQARERLLADNAKKKAQIAElqsfvsrfsanaskakqatsrakqidkikleevkPSSRQNPfirfeq 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2087084196 275 -------ILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHW 334
Cdd:PRK15064 312 dkklhrnALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW 378
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
292-480 |
2.66e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 292 KGVSFDLKQGETVAVVGESGSGKSTLARILLRL----------------------------EEPDGG------------T 331
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdEEQNVGmknvnefsltkeG 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 332 AHWKGKDLFTMSPG-----------DLFKLRRDLQMVFQDPtqsLNPRMTVYQLI----SEAWIihpEILPKAKWRERVG 396
Cdd:PTZ00265 1265 GSGEDSTVFKNSGKilldgvdicdyNLKDLRNLFSIVSQEP---MLFNMSIYENIkfgkEDATR---EDVKRACKFAAID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 397 ELLGQVGLSLE-HMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVS----VQAQVITLLDKLRKEMgiafIF 471
Cdd:PTZ00265 1339 EFIESLPNKYDtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTI----IT 1414
|
....*....
gi 2087084196 472 IAHDLPLVR 480
Cdd:PTZ00265 1415 IAHRIASIK 1423
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
156-494 |
3.62e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVqaeVLALLKELQRETGMgVLIITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKT-FIVVSHAREFLNTVVTDILHLHGQKLV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 236 ESGTVRDVY--------RNPQHA---------------------------------------YTKKLIAAAPGKGEMHEP 268
Cdd:PLN03073 421 TYKGDYDTFertreeqlKNQQKAfesnersrshmqafidkfrynakraslvqsrikaldrlgHVDAVVNDPDYKFEFPTP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 269 EAQ-GEPILSVKDARKSY-GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGK---DLFTMS 343
Cdd:PLN03073 501 DDRpGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmAVFSQH 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 344 PGDLFKLrrdlqmvfqdptqSLNPRMTVYQLISEAwiihpeilPKAKWRERVGELLGQVGLSLEHMgrypHQFSGGQRQR 423
Cdd:PLN03073 581 HVDGLDL-------------SSNPLLYMMRCFPGV--------PEQKLRAHLGSFGVTGNLALQPM----YTLSGGQKSR 635
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2087084196 424 IAIARALALEPQLIVCDEAVSALDV-SVQAqvitLLDKLRKEMGiAFIFIAHDLPLVRDFADYVMVMQKGEV 494
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLdAVEA----LIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
134-239 |
4.06e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.72 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 134 LRLFKRVALPDAERALDK-----YPHE----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRE 204
Cdd:PRK09984 122 FSWFTREQKQRALQALTRvgmvhFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQN 201
|
90 100 110
....*....|....*....|....*....|....*
gi 2087084196 205 TGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGT 239
Cdd:PRK09984 202 DGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
157-335 |
5.75e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVL--ALLKELQRETGmgvLIITHDLGVVSEVaDRVVVMEKGQL 234
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkCIKDELRGKTR---VLVTNQLHFLSQV-DRIILVHEGMI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 235 VESGTVRDVYRNPQhaYTKKLIAAApGKGEMHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKqgetvavvgESGSGK 314
Cdd:PLN03130 818 KEEGTYEELSNNGP--LFQKLMENA-GKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKK---------KSKEGK 885
|
170 180
....*....|....*....|.
gi 2087084196 315 StlarILLRLEEPDGGTAHWK 335
Cdd:PLN03130 886 S----VLIKQEERETGVVSWK 902
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
278-503 |
9.71e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 278 VKDA---RKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILlrleepdGGTahwkgkdlftMSPGDlFKLRRDL 354
Cdd:PRK13546 24 MKDAlipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNII-------GGS----------LSPTV-GKVDRNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 355 QMVFQDPTQSLNPRMTVYQLISEawiihpEILPKAKWRERVGELLGQVgLSLEHMGRYPHQ----FSGGQRQRIAIARAL 430
Cdd:PRK13546 86 EVSVIAISAGLSGQLTGIENIEF------KMLCMGFKRKEIKAMTPKI-IEFSELGEFIYQpvkkYSSGMRAKLGFSINI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 431 ALEPQLIVCDEAVSALDvsvQAQVITLLDKLR--KEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:PRK13546 159 TVNPDILVIDEALSVGD---QTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
157-233 |
1.10e-08 |
|
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: 55.17 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVL--ALLKELQRE-TgmgVLIITHDLGVVSEvADRVVVMEKGQ 233
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLLNNkT---RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
144-229 |
1.38e-08 |
|
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: 55.84 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 DAERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVA 223
Cdd:cd03236 128 ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLS 206
|
....*.
gi 2087084196 224 DRVVVM 229
Cdd:cd03236 207 DYIHCL 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
64-235 |
2.06e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.17 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 64 GKITsGEILLDGKdllkmsaeARREVNGRRIAMIFQDPLshLNPVYTVgwqmREALKTHGisttqaqaeALRlfkrvalp 143
Cdd:cd03232 60 GVIT-GEILINGR--------PLDKNFQRSTGYVEQQDV--HSPNLTV----REALRFSA---------LLR-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 daeraldkyphEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQrETGMGVLIITHD-LGVVSEV 222
Cdd:cd03232 108 -----------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHQpSASIFEK 175
|
170
....*....|....
gi 2087084196 223 ADRVVVMEK-GQLV 235
Cdd:cd03232 176 FDRLLLLKRgGKTV 189
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-230 |
2.14e-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: 2.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVME 230
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
272-499 |
2.23e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 272 GEPILSVKD---ARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTL-ARILLRLEEPDGGTAHWKGKDLFTMSPGDL 347
Cdd:PLN03130 611 GLPAISIKNgyfSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVVIRGTVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 348 FKLR-RDlQMVFQDPTQSlnPRMtvYQLISEAWIIHP-EILPKAKWRErvgelLGQVGLSLehmgryphqfSGGQRQRIA 425
Cdd:PLN03130 691 FNATvRD-NILFGSPFDP--ERY--ERAIDVTALQHDlDLLPGGDLTE-----IGERGVNI----------SGGQKQRVS 750
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2087084196 426 IARALALEPQLIVCDEAVSALDVSVQAQVIT--LLDKLRKEMGIAFIFIAHDLPLVrdfaDYVMVMQKGEVVELGT 499
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTRVLVTNQLHFLSQV----DRIILVHEGMIKEEGT 822
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
268-506 |
2.41e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 268 PEAQGEPILSVKDARKSYG---DFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLrleepdGGTAHWKgkdlftmsp 344
Cdd:PLN03232 607 PLQPGAPAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML------GELSHAE--------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 gdlfklrrdlqmvfqdpTQSLNPRMTVYQLISEAWI----IHPEILPKAKWR-ERVGELLGQVGLS----------LEHM 409
Cdd:PLN03232 672 -----------------TSSVVIRGSVAYVPQVSWIfnatVRENILFGSDFEsERYWRAIDVTALQhdldllpgrdLTEI 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 410 GRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVIT--LLDKLRKEMGIAFIFIAHDLPLVrdfaDYVM 487
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTRVLVTNQLHFLPLM----DRII 810
|
250
....*....|....*....
gi 2087084196 488 VMQKGEVVELGTVAQVFDN 506
Cdd:PLN03232 811 LVSEGMIKEEGTFAELSKS 829
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-235 |
2.43e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 1 MADHLLEVRNLSVDFhtvtGTVHAVRNISYYLDRGETLAILGESGSGKSvsssAIMNLIDMPPgKITSGEILLDGKDLLK 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDP-RATSGRIVFDGKDITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 81 -MSAEARREV-----NGRRI--AMIFQDPLshlnpvytvgwqmreALKTHGISTTQAQAEALR---LFKRVALPDAERAl 149
Cdd:PRK11614 72 wQTAKIMREAvaivpEGRRVfsRMTVEENL---------------AMGGFFAERDQFQERIKWvyeLFPRLHERRIQRA- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 dkypHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:PRK11614 136 ----GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVL 210
|
....*.
gi 2087084196 230 EKGQLV 235
Cdd:PRK11614 211 ENGHVV 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
68-253 |
3.57e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARREVNGrriaMIFQdplshlNPVYTVGwQMREALKTHGISTTQAQAEALrlfKRVALPDAER 147
Cdd:PLN03130 1293 RGRILIDGCDISKFGLMDLRKVLG----IIPQ------APVLFSG-TVRFNLDPFNEHNDADLWESL---ERAHLKDVIR 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 148 ----ALDKYPHE----FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgvLIITHDLGVV 219
Cdd:PLN03130 1359 rnslGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTI 1436
|
170 180 190
....*....|....*....|....*....|....
gi 2087084196 220 SEvADRVVVMEKGQLVESGTVRDVYRNPQHAYTK 253
Cdd:PLN03130 1437 ID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
291-454 |
4.41e-08 |
|
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: 56.07 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFT-----MSPGDLfklrRDlQMVFqdptqSL 365
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSpqtswIMPGTI----KD-NIIF-----GL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTVYQLISEAWIIHPEIlpkAKWRERVGELLGQVGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSA 445
Cdd:TIGR01271 512 SYDEYRYTSVIKACQLEEDI---ALFPEKDKTVLGEGGITL----------SGGQRARISLARAVYKDADLYLLDSPFTH 578
|
....*....
gi 2087084196 446 LDVSVQAQV 454
Cdd:TIGR01271 579 LDVVTEKEI 587
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
291-454 |
4.56e-08 |
|
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: 54.48 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFT-----MSPGDLfklrRDlQMVFqdptqSL 365
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSsqfswIMPGTI----KE-NIIF-----GV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 366 NPRMTVYQLISEAWIIHPEIlpkAKWRERVGELLGQVGLSLehmgryphqfSGGQRQRIAIARALALEPQLIVCDEAVSA 445
Cdd:cd03291 123 SYDEYRYKSVVKACQLEEDI---TKFPEKDNTVLGEGGITL----------SGGQRARISLARAVYKDADLYLLDSPFGY 189
|
....*....
gi 2087084196 446 LDVSVQAQV 454
Cdd:cd03291 190 LDVFTEKEI 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
156-238 |
5.10e-08 |
|
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: 53.42 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGV-VSEVADRVVVMEKGQL 234
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQ 198
|
....
gi 2087084196 235 VESG 238
Cdd:cd03233 199 IYYG 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
299-489 |
5.95e-08 |
|
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: 53.91 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 299 KQGETVAVVGESGSGKSTLARILLRLEEPDGGTahwkgkdlFTMSPG--DLFKLRR--DLQMVFqdpTQSLNPRMTVyql 374
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDwdEILDEFRgsELQNYF---TKLLEGDVKV--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 375 iseawIIHPE---ILPKAkWRERVGELLGQVG-----------LSLEH-MGRYPHQFSGGQRQRIAIARALALEPQLIVC 439
Cdd:cd03236 90 -----IVKPQyvdLIPKA-VKGKVGELLKKKDergkldelvdqLELRHvLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2087084196 440 DEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVM 489
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
157-335 |
6.51e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVL--ALLKELQRETGmgvLIITHDLGVVSEvADRVVVMEKGQL 234
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeeCFLGALAGKTR---VLATHQVHVVPR-ADYVVALGDGRV 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 235 VESGTVRDVYRNPqhaytkklIAAAPGKGEMHEPEAQGEpilsvkDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGK 314
Cdd:PTZ00243 860 EFSGSSADFMRTS--------LYATLAAELKENKDSKEG------DADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDG 925
|
170 180
....*....|....*....|....
gi 2087084196 315 STL---ARILLRLEEPDGGTAHWK 335
Cdd:PTZ00243 926 AALdaaAGRLMTREEKASGSVPWS 949
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
61-239 |
6.66e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.79 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 61 MPPgkiTSGEILLDGKDLlkmsaEARREVNGRRIAMIFQDPL--SHLnpvyTVGWQMREALKTHGISTTQAQAEALRLFK 138
Cdd:TIGR01257 980 LPP---TSGTVLVGGKDI-----ETNLDAVRQSLGMCPQHNIlfHHL----TVAEHILFYAQLKGRSWEEAQLEMEAMLE 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 139 RVALpdaERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLkeLQRETGMGVLIITHDLGV 218
Cdd:TIGR01257 1048 DTGL---HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDE 1122
|
170 180
....*....|....*....|.
gi 2087084196 219 VSEVADRVVVMEKGQLVESGT 239
Cdd:TIGR01257 1123 ADLLGDRIAIISQGRLYCSGT 1143
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
68-259 |
8.11e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 68 SGEILLDGKDLLKMSAEARREVngrrIAMIFQDPLSHLNPVYtvgwqmrEALKTHGISTTQAQAEALRLFKRV-----AL 142
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNL----FSIVSQEPMLFNMSIY-------ENIKFGKEDATREDVKRACKFAAIdefieSL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PDA-ERALDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSE 221
Cdd:PTZ00265 1345 PNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087084196 222 vADRVVVMEK----GQLVESGTVRDVYRNPQHAYTKKLIAAA 259
Cdd:PTZ00265 1425 -SDKIVVFNNpdrtGSFVQAHGTHEELLSVQDGVYKKYVKLA 1465
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
65-238 |
8.75e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 65 KITSGEILLDGKDLLKMSAEARRevnGRRIAMIFQdplshlNPVYTVGWQMREALKTHGISTTQ-AQAEALRLFKRVALP 143
Cdd:PRK09580 54 EVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQ------YPVEIPGVSNQFFLQTALNAVRSyRGQEPLDRFDFQDLM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 DAERALDKYPHE---------FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITH 214
Cdd:PRK09580 125 EEKIALLKMPEDlltrsvnvgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
170 180
....*....|....*....|....*
gi 2087084196 215 DLGVVSEVA-DRVVVMEKGQLVESG 238
Cdd:PRK09580 204 YQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
283-495 |
1.41e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 283 KSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDL-FTMSPGdlfKLRRDLQMVFQDP 361
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKE---ALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 362 TQSLN------------PRMTVY----QLISEAWIIHPEILPKAKWRERVGELlgqvglslehmgryphqfSGGQRQRIA 425
Cdd:PRK10982 83 NLVLQrsvmdnmwlgryPTKGMFvdqdKMYRDTKAIFDELDIDIDPRAKVATL------------------SVSQMQMIE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 426 IARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLrKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVV 495
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
157-248 |
1.74e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.95 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRetGMGVLIITHDLGVVSEvADRVVVMEKGQLVE 236
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
90 100
....*....|....*....|..
gi 2087084196 237 SGTV----------RDVYRNPQ 248
Cdd:PRK10789 530 RGNHdqlaqqsgwyRDMYRYQQ 551
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-239 |
2.30e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.70 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVrnLSVDFHTVTGtvhavrNISYYLDRGETLAILGESGSgksvsssaimnlidmppGKiTS------------GEILL 73
Cdd:PRK11174 355 LEI--LSPDGKTLAG------PLNFTLPAGQRIALVGPSGA-----------------GK-TSllnallgflpyqGSLKI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 74 DGKDLLKMSAEARRevngRRIAMIFQDPlsHLnPVYTVgwqmRE--ALKTHGISTTQ-----AQAEAL----RLFKRVAL 142
Cdd:PRK11174 409 NGIELRELDPESWR----KHLSWVGQNP--QL-PHGTL----RDnvLLGNPDASDEQlqqalENAWVSeflpLLPQGLDT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PDAERALDkypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVL-ALLKELQRETgmgVLIITHDLGVVSE 221
Cdd:PRK11174 478 PIGDQAAG-----LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMqALNAASRRQT---TLMVTHQLEDLAQ 549
|
250
....*....|....*...
gi 2087084196 222 VaDRVVVMEKGQLVESGT 239
Cdd:PRK11174 550 W-DQIWVMQDGQIVQQGD 566
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
260-538 |
3.07e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 260 PGKGEMHEpeAQGEPILSVKDARKSYGDF------EALKGVSFDLKQGETVAVVGESGSGKSTLARILLrleepdggtah 333
Cdd:PTZ00243 641 GGTGGGHE--ATPTSERSAKTPKMKTDDFfelepkVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL----------- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 334 wkgkDLFTMSPGDLFKlRRDLQMVFQdptqslnprmtvyqlisEAWIIH--------------PEILPKAKwreRVGEL- 398
Cdd:PTZ00243 708 ----SQFEISEGRVWA-ERSIAYVPQ-----------------QAWIMNatvrgnilffdeedAARLADAV---RVSQLe 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 399 --LGQVGLSLE-HMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVI--TLLDKLRKEMGIAFIFIA 473
Cdd:PTZ00243 763 adLAQLGGGLEtEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeeCFLGALAGKTRVLATHQV 842
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 474 HDLPLvrdfADYVMVMQKGEVVELGTVAQVFDNPqkpyTQALLAASLDPDPDVQAANRNARLASV 538
Cdd:PTZ00243 843 HVVPR----ADYVVALGDGRVEFSGSSADFMRTS----LYATLAAELKENKDSKEGDADAEVAEV 899
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-240 |
3.28e-07 |
|
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: 51.83 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVhaVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKItsgeiLLDGKDLLKMSAEA 85
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-----VIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREvngrRIAMIFQDPLshlnpvyTVGWQMREALKTHGISTTQAQAEALRL--FKRV--ALPDAERALDKYPHE-FSGGQ 160
Cdd:cd03288 93 LRS----RLSIILQDPI-------LFSGSIRFNLDPECKCTDDRLWEALEIaqLKNMvkSLPGGLDAVVTEGGEnFSVGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 161 RQRVMIAMALALKPDLLIADEPTTALDVT----VQAEVLALLKELQretgmgVLIITHDLGVVSEvADRVVVMEKGQLVE 236
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMAteniLQKVVMTAFADRT------VVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
....
gi 2087084196 237 SGTV 240
Cdd:cd03288 235 CDTP 238
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
157-334 |
3.53e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVL--ALLKELQRETGmgvLIITHDLGVVSEVaDRVVVMEKGQL 234
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdsCMKDELKGKTR---VLVTNQLHFLPLM-DRIILVSEGMI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 235 VESGTVRDVYRNPQhaYTKKLIAAAPGKGEMHEPEAQGEPILsvKDARKSYGDFEALKGVSfdLKQGEtvavvgesgSGK 314
Cdd:PLN03232 818 KEEGTFAELSKSGS--LFKKLMENAGKMDATQEVNTNDENIL--KLGPTVTIDVSERNLGS--TKQGK---------RGR 882
|
170 180
....*....|....*....|
gi 2087084196 315 StlarILLRLEEPDGGTAHW 334
Cdd:PLN03232 883 S----VLVKQEERETGIISW 898
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
298-489 |
3.71e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 298 LKQGETVAVVGESGSGKSTLARIL---LR--LEEPDGGTA------HWKGKDLFT----MSPGDLfKLRRDLQMVFQDPT 362
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILsgeLKpnLGDYDEEPSwdevlkRFRGTELQDyfkkLANGEI-KVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 Q-SLNPRmtvyqliseawiihpEILPKAKWRERVGELLGQvgLSLEH-MGRYPHQFSGGQRQRIAIARALALEPQLIVCD 440
Cdd:COG1245 175 VfKGTVR---------------ELLEKVDERGKLDELAEK--LGLENiLDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2087084196 441 EAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVM 489
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-317 |
5.96e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMAL---ALKPDLLIADEPTTALDVtvqAEVLALLKELQRETGMG--VLIITHDLGVVsEVADRVVVM-- 229
Cdd:PRK00635 811 SGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHT---HDIKALIYVLQSLTHQGhtVVIIEHNMHVV-KVADYVLELgp 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 230 ----EKGQLVESGTVRDVYrnpqHAYTKKLIAAAPG-KGEMHEP----EAQGEPIL---SVKDARKsygdfEALKGVSFD 297
Cdd:PRK00635 887 eggnLGGYLLASCSPEELI----HLHTPTAKALRPYlSSPQELPylpdPSPKPPVPadiTIKNAYQ-----HNLKHIDLS 957
|
170 180
....*....|....*....|
gi 2087084196 298 LKQGETVAVVGESGSGKSTL 317
Cdd:PRK00635 958 LPRNALTAVTGPSASGKHSL 977
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
291-461 |
7.90e-07 |
|
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: 49.55 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEpdGGTAhwKGKDLFTMSPGDLfKLRRDLQMVFQDPTqsLNPRMT 370
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVI--TGEILINGRPLDK-NFQRSTGYVEQQDV--HSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 371 VYqlisEAWIIHpeilpkAKWRervgellgqvGLSLEhmgryphqfsggQRQRIAIARALALEPQLIVCDEAVSALDVSV 450
Cdd:cd03232 96 VR----EALRFS------ALLR----------GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170
....*....|.
gi 2087084196 451 QAQVITLLDKL 461
Cdd:cd03232 144 AYNIVRFLKKL 154
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
276-498 |
8.62e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSygdfeALKGVSFDLKQGETVAVVGESGSGKSTLARillrleepdggtahwkgkdlftmspgDLFKLRRDLQ 355
Cdd:cd03238 1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------------------------EGLYASGKAR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 356 MVFQDPTQSLNPRMTVYQLiseawiihpeilpkakwrervgELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQ 435
Cdd:cd03238 50 LISFLPKFSRNKLIFIDQL----------------------QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPP 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2087084196 436 --LIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVrDFADYVMVM------QKGEVVELG 498
Cdd:cd03238 108 gtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVL-SSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
157-239 |
9.17e-07 |
|
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: 50.31 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALAlKPD----LLIADEPTTALDVtvqAEVLALLKELQR--ETGMGVLIITHDLGVVsEVADRVVVM- 229
Cdd:cd03271 171 SGGEAQRIKLAKELS-KRStgktLYILDEPTTGLHF---HDVKKLLEVLQRlvDKGNTVVVIEHNLDVI-KCADWIIDLg 245
|
90
....*....|....*
gi 2087084196 230 -----EKGQLVESGT 239
Cdd:cd03271 246 peggdGGGQVVASGT 260
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
156-232 |
9.57e-07 |
|
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: 50.02 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDV-----TVQAEVLALLKELQREtgmgVLIITHDLGVVSEvADRVVVME 230
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKRT----LVLVTHKLQYLPH-ADWIIAMK 215
|
..
gi 2087084196 231 KG 232
Cdd:cd03290 216 DG 217
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-274 |
1.16e-06 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 46.59 E-value: 1.16e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2087084196 233 QLVESGTVRDVYRNPQHAYTKKLIAAAPGKGEMHEP--EAQGEP 274
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKliSIPGEV 44
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
67-242 |
1.28e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 67 TSGEILLDGKdllKMSAEARREVngrriamifqdpLSHLNPVYTVGWQMREALKTHGISTTQAQAEA----LRLFKRVAL 142
Cdd:PRK10522 376 QSGEILLDGK---PVTAEQPEDY------------RKLFSAVFTDFHLFDQLLGPEGKPANPALVEKwlerLKMAHKLEL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 143 PDAERALDKypheFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLIITHDlGVVSEV 222
Cdd:PRK10522 441 EDGRISNLK----LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIH 515
|
170 180
....*....|....*....|.
gi 2087084196 223 ADRVVVMEKGQLVE-SGTVRD 242
Cdd:PRK10522 516 ADRLLEMRNGQLSElTGEERD 536
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
157-215 |
1.40e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAmALALKP-DLLIADEPTTALDVtvqaEVLALLKELQRETGMGVLIITHD 215
Cdd:PRK11147 442 SGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-317 |
1.53e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 146 ERALDKypheFSGGQRQRVMIAMALA--LKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSeVA 223
Cdd:PRK00635 471 ERALAT----LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMIS-LA 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 224 DRVVVMEK------GQLVESGTVRDvYRNPQHAYTKKLIaaapgKGEMH--EPEAQGEPI--LSVKDARKSygdfeALKG 293
Cdd:PRK00635 545 DRIIDIGPgagifgGEVLFNGSPRE-FLAKSDSLTAKYL-----RQELTipIPEKRTNSLgtLTLSKATKH-----NLKD 613
|
170 180
....*....|....*....|....
gi 2087084196 294 VSFDLKQGETVAVVGESGSGKSTL 317
Cdd:PRK00635 614 LTISLPLGRLTVVTGVSGSGKSSL 637
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
280-498 |
1.72e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 280 DARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTahwkGKDLftMSPGDLFK--LRRdLQMV 357
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFT----GTIL--ANNRKPTKqiLKR-TGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 358 FQDPTqsLNPRMTVYQ-LISEAWIIHPEILPKAKwRERVGE-LLGQVGLSLEHMGRYPHQF----SGGQRQRIAIARALA 431
Cdd:PLN03211 146 TQDDI--LYPHLTVREtLVFCSLLRLPKSLTKQE-KILVAEsVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEML 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 432 LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDlPLVRDFA--DYVMVMQKGEVVELG 498
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQ-PSSRVYQmfDSVLVLSEGRCLFFG 289
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-240 |
2.08e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIA--MALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEvADRVVVMEKGQL 234
Cdd:cd03238 89 SGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDFGPGSG 166
|
....*.
gi 2087084196 235 VESGTV 240
Cdd:cd03238 167 KSGGKV 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-243 |
2.15e-06 |
|
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: 50.71 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVDFHTVTGTVhaVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMppgkiTSGEILLDGKDLLKMSAEA 85
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGLNIAKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 RREvngrRIAMIFQDPL-------SHLNPVYTVG----WQMREALKTHGISTtqaqaealrlfkrvALPDaeraldKYPH 154
Cdd:TIGR00957 1358 LRF----KITIIPQDPVlfsgslrMNLDPFSQYSdeevWWALELAHLKTFVS--------------ALPD------KLDH 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 E-------FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKElQRETgMGVLIITHDLGVVSEVAdRVV 227
Cdd:TIGR00957 1414 EcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFED-CTVLTIAHRLNTIMDYT-RVI 1490
|
250
....*....|....*.
gi 2087084196 228 VMEKGQLVESGTVRDV 243
Cdd:TIGR00957 1491 VLDKGEVAEFGAPSNL 1506
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
294-331 |
2.73e-06 |
|
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: 50.18 E-value: 2.73e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2087084196 294 VSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT 331
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE 388
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
157-231 |
2.80e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.37 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQ------RVMIAMALALKPDLLIADEPTTALDVTVQAEVLA-LLKELQRETGMGVLIITHDLGVVsEVADRVVVM 229
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAeIIEERKSQKNFQLIVITHDEELV-DAADHIYRV 195
|
..
gi 2087084196 230 EK 231
Cdd:cd03240 196 EK 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-243 |
3.04e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALK---PDLLIADEPTTALDVtvqAEVLALLKELQR--ETGMGVLIITHDLGVVsEVADRVVVM-- 229
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRlvDKGNTVVVIEHNLDVI-KTADYIIDLgp 906
|
90
....*....|....*...
gi 2087084196 230 ----EKGQLVESGTVRDV 243
Cdd:TIGR00630 907 eggdGGGTVVASGTPEEV 924
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
298-489 |
3.32e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 298 LKQGETVAVVGESGSGKSTLARILL--------RLEEPDGGTA---HWKGKDLFT----MSPGDLfKLRRDLQMVfqdpt 362
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEvlkRFRGTELQNyfkkLYNGEI-KVVHKPQYV----- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 qslnprmtvyqliseawiihpEILPKAkWRERVGELLGQVG-----------LSLEH-MGRYPHQFSGGQRQRIAIARAL 430
Cdd:PRK13409 170 ---------------------DLIPKV-FKGKVRELLKKVDergkldevverLGLENiLDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 431 ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemGIAFIFIAHDLpLVRDF-ADYVMVM 489
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL-AVLDYlADNVHIA 284
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
394-487 |
3.95e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 394 RVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKemgiAFIFIA 473
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVS 398
|
90
....*....|....
gi 2087084196 474 HdlplVRDFADYVM 487
Cdd:PLN03073 399 H----AREFLNTVV 408
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
291-503 |
4.46e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRlEEPDGGTAH---------WKGKDLFTMSPGDLFKLRRDLQMVFQdP 361
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAPRgarvtgdvtLNGEPLAAIDAPRLARLRAVLPQAAQ-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 362 TQSLNPRMTVyqLISEawiiHPEILPKAKWRERVGELLGQvGLSLEH----MGRYPHQFSGGQRQRIAIARALA------ 431
Cdd:PRK13547 95 AFAFSAREIV--LLGR----YPHARRAGALTHRDGEIAWQ-ALALAGatalVGRDVTTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 432 ---LEPQLIVCDEAVSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-219 |
4.81e-06 |
|
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: 47.35 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 6 LEVRNLSVdfhtVTGTVHAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLidMPPgkiTSGEILLDGKDLLKMsaea 85
Cdd:TIGR01189 1 LAARNLAC----SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRP---DSGEVRWNGTPLAEQ---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 86 rREVNGRRIAMifqdpLSHLN---PVYTVgwqmREALK-THGISTTqAQAEALRLFKRVALPDAEralDKYPHEFSGGQR 161
Cdd:TIGR01189 68 -RDEPHENILY-----LGHLPglkPELSA----LENLHfWAAIHGG-AQRTIEDALAAVGLTGFE---DLPAAQLSAGQQ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 162 QRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKE-LQRetGMGVLIITH-DLGVV 219
Cdd:TIGR01189 134 RRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLAR--GGIVLLTTHqDLGLV 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-236 |
5.88e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 131 AEALRLFKRVALPDAERAL-DKY-------PHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQ 202
Cdd:PTZ00265 547 SEVVDVSKKVLIHDFVSALpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
90 100 110
....*....|....*....|....*....|....*..
gi 2087084196 203 RETGMGVLIITHDLGVVsEVADRVVVM---EKGQLVE 236
Cdd:PTZ00265 627 GNENRITIIIAHRLSTI-RYANTIFVLsnrERGSTVD 662
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
123-226 |
7.12e-06 |
|
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: 47.10 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 123 GISTTQAQAEALRLFKRVALPDA-ERALDKYP---------HEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQA 192
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHSDEQvEEALARVGlngfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
90 100 110
....*....|....*....|....*....|....
gi 2087084196 193 EVLALLKELQRETGMGVLIITHDLGVVSEVADRV 226
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
495-524 |
1.03e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 43.16 E-value: 1.03e-05
10 20 30
....*....|....*....|....*....|
gi 2087084196 495 VELGTVAQVFDNPQKPYTQALLAASLDPDP 524
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-242 |
1.09e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 35 GETLAILGESGSGKSVSSSAIMNLIDmppGKITSGEILLDGKDLLKMSAearrevngRRIAMIFQDPLshLNPVYTVgwq 114
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQ---GNNFTGTILANNRKPTKQIL--------KRTGFVTQDDI--LYPHLTV--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 115 mREAL---KTHGISTTQAQAEALRLFKRVAlpdAERALDK---------YPHEFSGGQRQRVMIAMALALKPDLLIADEP 182
Cdd:PLN03211 158 -RETLvfcSLLRLPKSLTKQEKILVAESVI---SELGLTKcentiignsFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 183 TTALDVTVQAEVLALLKELQRETGMGVLIITHDLGVVSEVADRVVVMEKGQLVESGTVRD 242
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
61-221 |
1.17e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.34 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 61 MPPgkiTSGEILLDGKDLLKMSAEARREvngrriaMIFqdpLSHLNPVYTV--GWQ-MREALKTHGISTTQAQAEALRlf 137
Cdd:PRK13538 51 ARP---DAGEVLWQGEPIRRQRDEYHQD-------LLY---LGHQPGIKTEltALEnLRFYQRLHGPGDDEALWEALA-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 138 kRVALPDAERALdkyPHEFSGGQRQRVmiAMA-LAL-KPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgVLIITH- 214
Cdd:PRK13538 116 -QVGLAGFEDVP---VRQLSAGQQRRV--ALArLWLtRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGM-VILTTHq 188
|
....*..
gi 2087084196 215 DLGVVSE 221
Cdd:PRK13538 189 DLPVASD 195
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
235-260 |
1.20e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 43.16 E-value: 1.20e-05
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
300-499 |
1.25e-05 |
|
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: 48.47 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 300 QGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKLRRDLQMVFQDptqslnpRMTVYQLISEAW 379
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQH-------NILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 380 IIHPEILPKAKWRERVGELLGQVGLSLEHMGR--YPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVITL 457
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2087084196 458 LDKLRKemGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGT 499
Cdd:TIGR01257 1104 LLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-231 |
1.25e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 1.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 157 SGGQRQRVMIAMALAL---KPD-LLIADEPTTALDVTVQAEVLALLKELQRETGMgVLIITHDLGVVsEVADRVVVMEK 231
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELA-ELADKLIHIKK 155
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
265-461 |
1.27e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 265 MHEPEAQGEPILSVKDARKSYGDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKdlfTMSP 344
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 345 GDlfklrRDLQMVFQDPTQSLNPRMTVYQLISEAWIIH---PEILPkakwrervGELLGQVGLSlEHMGRYPHQFSGGQR 421
Cdd:PRK13543 78 GD-----RSRFMAYLGHLPGLKADLSTLENLHFLCGLHgrrAKQMP--------GSALAIVGLA-GYEDTLVRQLSAGQK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2087084196 422 QRIAIARaLALEPQ-LIVCDEAVSALDVsvqaQVITLLDKL 461
Cdd:PRK13543 144 KRLALAR-LWLSPApLWLLDEPYANLDL----EGITLVNRM 179
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
150-241 |
1.44e-05 |
|
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: 48.09 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 150 DKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQREtGMGVLIITHDLGVVSEVADRVVVM 229
Cdd:TIGR01257 2065 DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
90
....*....|..
gi 2087084196 230 EKGQLVESGTVR 241
Cdd:TIGR01257 2144 VKGAFQCLGTIQ 2155
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
301-484 |
1.90e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 301 GETVAVVGESGSGKSTLARILLRLEEPDGGT----AHWKGKDLFTMSP------------GDlfKLRRDLQMVFQDPTQ- 363
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpGNWQLAWVNQETPalpqpaleyvidGD--REYRQLEAQLHDANEr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 364 -SLNPRMTVYQLIS--EAWIIhpeilpkakwRERVGELLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALEPQLIVCD 440
Cdd:PRK10636 105 nDGHAIATIHGKLDaiDAWTI----------RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2087084196 441 EAVSALDVSvqaqVITLLDKLRKEMGIAFIFIAHDlplvRDFAD 484
Cdd:PRK10636 175 EPTNHLDLD----AVIWLEKWLKSYQGTLILISHD----RDFLD 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
157-218 |
2.42e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.64 E-value: 2.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMgVLIITH-DLGV 218
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATHiPLGL 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
156-269 |
2.68e-05 |
|
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: 47.25 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVL-------ALLKELQRetgmgvLIITHDLGVVSEVaDRVVV 228
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFehvigpeGVLKNKTR------ILVTHGISYLPQV-DVIIV 833
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2087084196 229 MEKGQLVESGTVRDVY-RNpqHAYTKKLIAAAPGKGEMHEPE 269
Cdd:TIGR00957 834 MSGGKISEMGSYQELLqRD--GAFAEFLRTYAPDEQQGHLED 873
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
291-500 |
2.83e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLA---------------------RILLRLEEPDggtahwkgKDLFT-MSPGdlf 348
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPD--------VDSIEgLSPA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 349 klrrdlqMVFQDPTQSLNPRMTVyQLISEAWIIHPEILPKAKWRERVGELLgQVGLSLEHMGRYPHQFSGGQRQRIAIAR 428
Cdd:cd03270 80 -------IAIDQKTTSRNPRSTV-GTVTEIYDYLRLLFARVGIRERLGFLV-DVGLGYLTLSRSAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 429 AL--ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRkEMGIAFIFIAHDLPLVRDfADYVMVMQKGEVVELGTV 500
Cdd:cd03270 151 QIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDEDTIRA-ADHVIDIGPGAGVHGGEI 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
283-490 |
2.98e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 283 KSYGDFEALKGVSfDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGkdlftmspgdlfklrrdlqmvfqdPT 362
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------------------IT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 363 QSLNPrmtvyQLISeawiihpeilpkakwrervgellgqvglslehmgryphqFSGGQRQRIAIARALALEPQLIVCDEA 442
Cdd:cd03222 63 PVYKP-----QYID---------------------------------------LSGGELQRVAIAAALLRNATFYLFDEP 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2087084196 443 VSALDVSVQAQVITLLDKLRKEMGIAFIFIAHDLPLVRDFADYVMVMQ 490
Cdd:cd03222 99 SAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
135-239 |
3.21e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 135 RLFKrvaLPDAERA---------------LDKYPHEFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLK 199
Cdd:NF033858 365 RLFH---LPAAEIAarvaemlerfdladvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLI 441
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2087084196 200 ELQRETGMGVLIITHdlgVVSEVA--DRVVVMEKGQLVESGT 239
Cdd:NF033858 442 ELSREDGVTIFISTH---FMNEAErcDRISLMHAGRVLASDT 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
64-232 |
3.25e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 64 GKITSGEILLDGKdllkmsaeARREVNGRRIAMIFQDPLsHLnPVYTVgwqmREALKThgisttqaqAEALRLFKRVALP 143
Cdd:TIGR00956 816 GVITGGDRLVNGR--------PLDSSFQRSIGYVQQQDL-HL-PTSTV----RESLRF---------SAYLRQPKSVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 144 DAERALDK---------YPHEFSG--------GQRQRVMIAMALALKPDLLI-ADEPTTALDVTVQAEVLALLKELQrET 205
Cdd:TIGR00956 873 EKMEYVEEvikllemesYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DH 951
|
170 180
....*....|....*....|....*...
gi 2087084196 206 GMGVLIITHD-LGVVSEVADRVVVMEKG 232
Cdd:TIGR00956 952 GQAILCTIHQpSAILFEEFDRLLLLQKG 979
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-260 |
3.47e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALAlKPD----LLIADEPTTAL---DVTVqaevlaLLKELQR--ETGMGVLIITHDLGVVSeVADRVV 227
Cdd:COG0178 828 SGGEAQRVKLASELS-KRStgktLYILDEPTTGLhfhDIRK------LLEVLHRlvDKGNTVVVIEHNLDVIK-TADWII 899
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2087084196 228 VM-----EK-GQLVESGTVRDVYRNPQhAYT----KKLIAAAP 260
Cdd:COG0178 900 DLgpeggDGgGEIVAEGTPEEVAKVKA-SYTgrylKEYLEAAR 941
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
493-518 |
5.78e-05 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 41.96 E-value: 5.78e-05
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
276-455 |
8.21e-05 |
|
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: 44.46 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 276 LSVKDARKSY--GDFEALKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGT----AHW------KGKDLFTMS 343
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIqidgVSWnsvplqKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 344 PGDLF----KLRRDLqmvfqDPTQSLNPRmtvyqlisEAWIIHPEIlpkaKWRERVGELLGQVGLSLEHMGrypHQFSGG 419
Cdd:cd03289 83 PQKVFifsgTFRKNL-----DPYGKWSDE--------EIWKVAEEV----GLKSVIEQFPGQLDFVLVDGG---CVLSHG 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 2087084196 420 QRQRIAIARALALEPQLIVCDEAVSALDvSVQAQVI 455
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVI 177
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
155-243 |
8.71e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 155 EFSGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELqRETGMGVLIITHDLGVVSEVADRVVVMEKGQL 234
Cdd:PRK13546 143 KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
....*....
gi 2087084196 235 VESGTVRDV 243
Cdd:PRK13546 222 KDYGELDDV 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
291-455 |
9.15e-05 |
|
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: 45.67 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTLARILLRLEEPDGGTA----HWKGKDL------FTMSPGDLFKLRRDLQMvfqd 360
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQidgvSWNSVTLqtwrkaFGVIPQKVFIFSGTFRK---- 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 361 ptqSLNPrmtvYQLIS--EAWIIHPEIlpkaKWRERVGELLGQVGLSLEHMGrypHQFSGGQRQRIAIARALALEPQLIV 438
Cdd:TIGR01271 1311 ---NLDP----YEQWSdeEIWKVAEEV----GLKSVIEQFPDKLDFVLVDGG---YVLSNGHKQLMCLARSILSKAKILL 1376
|
170
....*....|....*..
gi 2087084196 439 CDEAVSALDvSVQAQVI 455
Cdd:TIGR01271 1377 LDEPSAHLD-PVTLQII 1392
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
157-242 |
1.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVqaeVLALLKELQRETGmGVLIITHDLGVVSEVADRVVVMEKGQLVE 236
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKVTP 704
|
....*..
gi 2087084196 237 -SGTVRD 242
Cdd:PLN03073 705 fHGTFHD 711
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
156-248 |
1.37e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 156 FSGGQRQRVMIAMALaLKPD--LLIADEPTT----ALDVTVQAEVLALLkelqreTGMGVLIITHDLGVVSEVaDRVVVM 229
Cdd:PTZ00243 1446 YSVGQRQLMCMARAL-LKKGsgFILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQY-DKIIVM 1517
|
90
....*....|....*....
gi 2087084196 230 EKGQLVESGTVRDVYRNPQ 248
Cdd:PTZ00243 1518 DHGAVAEMGSPRELVMNRQ 1536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
157-238 |
1.69e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKELQRETGMGVLI-ITHDLGVVSEVADRVVVMEKGQLV 235
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQI 290
|
...
gi 2087084196 236 ESG 238
Cdd:TIGR00956 291 YFG 293
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
392-508 |
3.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 392 RERVGELLgQVGLSLEHMGRYPHQFSGGQRQRIAIARAL--ALEPQLIVCDEAVSALDVSVQAQVITLLDKLRKeMGIAF 469
Cdd:TIGR00630 466 RERLGFLI-DVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTL 543
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2087084196 470 IFIAHDLPLVRDfADYVMVM------QKGEVVELGTVAQVFDNPQ 508
Cdd:TIGR00630 544 IVVEHDEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILANPD 587
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
298-503 |
3.85e-04 |
|
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: 43.46 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 298 LKQGETVAVVGESGSGKSTLARILLRLEEPDGGTAHWKGKDLFTmspgDLFKLRRDLQMV--FQDPTQSLNPRMTVYQLI 375
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCpqFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 376 SEAWIIHPEILPKAKWRervgelLGQVGLSLeHMGRYPHQFSGGQRQRIAIARALALEPQLIVCDEAVSALDVSVQAQVI 455
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWS------IQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2087084196 456 TLLDKLRKEmGIAFIFIAHDLPLVRDFADYVMVMQKGEVVELGTVAQV 503
Cdd:TIGR01257 2111 NTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
291-499 |
6.33e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 291 LKGVSFDLKQGETVAVVGESGSGKSTL---------ARILLRLEEPDGGTAHWKGKDLftmspgdLFKLRrdlqMVFQDP 361
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypalARRLHLKKEQPGNHDRIEGLEH-------IDKVI----VIDQSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 362 ---TQSLNP-----------------------------------------RMTVYQlISEAWIIHPEIlpkakwrERVGE 397
Cdd:cd03271 80 igrTPRSNPatytgvfdeirelfcevckgkrynretlevrykgksiadvlDMTVEE-ALEFFENIPKI-------ARKLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 398 LLGQVGLSLEHMGRYPHQFSGGQRQRIAIARALALE---PQLIVCDEAVSALDVSVQAQVITLLDKLRkEMGIAFIFIAH 474
Cdd:cd03271 152 TLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEH 230
|
250 260 270
....*....|....*....|....*....|.
gi 2087084196 475 DLPLVRDfADYVMVM------QKGEVVELGT 499
Cdd:cd03271 231 NLDVIKC-ADWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
270-322 |
7.07e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 7.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2087084196 270 AQGEPILSVkDARKSYGdFEALKGVsfdLKQGETVAVVGESGSGKSTLARILL 322
Cdd:PRK01889 169 APGVPVLAV-SALDGEG-LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALL 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-214 |
8.26e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.70 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 5 LLEVRNLSVDFHTVTgtvhAVRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIdmppgKITSGEILLDGKDLLKMSAE 84
Cdd:PRK13540 1 MLDVIELDFDYHDQP----LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL-----NPEKGEILFERQSIKKDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 85 ARREvngrriaMIFQDPLSHLNPVYTvgwqMREA--LKTHGISTTQAQAEALRLFKRVALPDAERALdkypheFSGGQRQ 162
Cdd:PRK13540 72 YQKQ-------LCFVGHRSGINPYLT----LRENclYDIHFSPGAVGITELCRLFSLEHLIDYPCGL------LSSGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 163 RVMIAMALALKPDLLIADEPTTALDvtvQAEVLALLKELQ--RETGMGVLIITH 214
Cdd:PRK13540 135 QVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
198-317 |
8.67e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 198 LKELqRETGMGVLIITHDLGVVsEVADRVVVM------EKGQLVESGTVRDVYRNPQH---AYT--KKLIAAA----PGK 262
Cdd:PRK00349 534 LKHL-RDLGNTLIVVEHDEDTI-RAADYIVDIgpgagvHGGEVVASGTPEEIMKNPNSltgQYLsgKKKIEVPkerrKGN 611
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 263 GEMhepeaqgepiLSVKDARKSygdfeALKGVSFDLKQGETVAVVGESGSGKSTL 317
Cdd:PRK00349 612 GKF----------LKLKGAREN-----NLKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
157-240 |
1.02e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVTVQAEVLALLKElQRETGMGVLIITHDLGV-VSEVADRVVVMEK-GQL 234
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQV 1099
|
....*.
gi 2087084196 235 VESGTV 240
Cdd:PLN03140 1100 IYSGPL 1105
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-256 |
1.07e-03 |
|
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: 42.20 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 25 VRNISYYLDRGETLAILGESGSGKSVSSSAIMNLIDMPPGKIT-SGEILLDGKDLLKMSAEARREVngrriamIFqdpls 103
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhSGRISFSPQTSWIMPGTIKDNI-------IF----- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 104 hlnpvytvGWQMREALKTHGISTTQAQAEALRLFKRVALPDAERALdkyphEFSGGQRQRVMIAMALALKPDLLIADEPT 183
Cdd:TIGR01271 510 --------GLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGI-----TLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2087084196 184 TALDVTVQAEVL--ALLKELQRETGmgvLIITHDLGVVSEvADRVVVMEKGQLVESGTVRDVyRNPQHAYTKKLI 256
Cdd:TIGR01271 577 THLDVVTEKEIFesCLCKLMSNKTR---ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL-QAKRPDFSSLLL 646
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
414-483 |
2.69e-03 |
|
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: 38.88 E-value: 2.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2087084196 414 HQFSGGQRQRIAIARALAL----EPQLIVCDEAVSALDVSVQAQVITLLDKLRKEmGIAFIFIAHDLPLVRDFA 483
Cdd:cd03227 76 LQLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAELAD 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
157-239 |
5.29e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDV-TVQAEVLALlkelqrETGMGVLI-ITHDLGVVSEVADRVVVMEKGQL 234
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIESLNMAL------EKYEGTLIfVSHDREFVSSLATRIIEITPDGV 513
|
....*.
gi 2087084196 235 VE-SGT 239
Cdd:PRK15064 514 VDfSGT 519
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
157-215 |
6.22e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 6.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2087084196 157 SGGQRQRVMIAMALALKPDLLIADEPTTALDVtvqaEVLALLKELQRETGMGVLIITHD 215
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEEALLEFPGCAVVISHD 501
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
299-329 |
8.18e-03 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 38.88 E-value: 8.18e-03
10 20 30
....*....|....*....|....*....|..
gi 2087084196 299 KQGETVAVVGESGSGKSTLARILL-RLEEPDG 329
Cdd:PRK05537 390 KQGFTVFFTGLSGAGKSTIAKALMvKLMEMRG 421
|
|
| |
