|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-527 |
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: 747.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLEVARTG--QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKGRDVLK 78
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 MKENELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYPHEFSGG 158
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGR 238
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 239 TEDLLKAPQHPYTKKLLSSLPfRGRPRQIDLTSVPMISARDIIVDYAGRKSLFRK-NKPKRALHGVSIDIHEGEVVALVG 317
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEP-RGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRtVGHVKAVDGVSLTLRRGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 318 GSGSGKTTLGRTIAGLVtESEGRIQFQGRP----RTENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRpV--PGLD 391
Cdd:COG4172 320 ESGSGKSTLGLALLRLI-PSEGEIRFDGQDldglSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLR-VhgPGLS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 392 GKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGF 471
Cdd:COG4172 398 AAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGL 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 472 SCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPALD 527
Cdd:COG4172 478 AYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-527 |
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: 625.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVAdGSVSYKGRDVLKMKEn 82
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 elrHLRGAEIGVVFQEPMTSLNPSmTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQR 162
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENL-GLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 243 LKAPQhpytkkLLSSLP----FRGRPRQIDLTSVPMISARDIIVDYAGRKSlfrknKPKRALHGVSIDIHEGEVVALVGG 318
Cdd:COG1123 231 LAAPQ------ALAAVPrlgaARGRAAPAAAAAEPLLEVRNLSKRYPVRGK-----GGVRAVDDVSLTLRRGETLGLVGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 319 SGSGKTTLGRTIAGLVTESEGRIQFQGRP----RTENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKA 394
Cdd:COG1123 300 SGSGKSTLARLLLGLLRPTSGSILFDGKDltklSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 395 KRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCL 474
Cdd:COG1123 380 RRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYL 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 475 FISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPALD 527
Cdd:COG1123 460 FISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLD 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-521 |
1.13e-158 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 462.64 E-value: 1.13e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMdKLLTVCGLSLEVARTGQ--QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLP-PTIKVADGSVSYKGRDVL 77
Cdd:PRK15134 1 MTQ-PLLAIENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsPPVVYPSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 78 KMKENELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYPHEFSG 157
Cdd:PRK15134 80 HASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 238 RTEDLLKAPQHPYTKKLLSSLPfRGRPRQIDLTSVPMISARDIIVDYAGRKSLFRKN-KPKRALHGVSIDIHEGEVVALV 316
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNSEP-SGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTvDHNVVVKNISFTLRPGETLGLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 317 GGSGSGKTTLGRTIAGLVtESEGRIQFQGRPrTENWT-----DYRLNCQMVFQDPYSSLDPRMTIEALVEEALR-PVPGL 390
Cdd:PRK15134 319 GESGSGKSTTGLALLRLI-NSQGEIWFDGQP-LHNLNrrqllPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 391 DGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYG 470
Cdd:PRK15134 397 SAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQ 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 471 FSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLS 521
Cdd:PRK15134 477 LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-527 |
5.39e-148 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 438.91 E-value: 5.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVARTGQQV--VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlpptIKVADGSVS-------YKGRDV 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRL----LEQAGGLVQcdkmllrRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 77 LKMKEN---ELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYPH 153
Cdd:PRK10261 88 IELSEQsaaQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 234 VEKGRTEDLLKAPQHPYTKKLLSSLPFRGR------PRQIDLTSV-------------------PMISARDIIVDYAGRK 288
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVPQLGAmkgldyPRRFPLISLehpakqeppieqdtvvdgePILQVRNLVTRFPLRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 289 SLFrkNKPKRALHGV---SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRpRTENWTDYRL-----NCQ 360
Cdd:PRK10261 328 GLL--NRVTREVHAVekvSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ-RIDTLSPGKLqalrrDIQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 361 MVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRF 440
Cdd:PRK10261 405 FIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLL 520
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
....*..
gi 1681691554 521 SAIPALD 527
Cdd:PRK10261 565 AAVPVAD 571
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-273 |
3.36e-122 |
|
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: 361.68 E-value: 3.36e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVARTGQQV--VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVAdGSVSYKGRDVLKMKENE 83
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITS-GEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYPHEFSGGMRQRI 163
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 164 MLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270
....*....|....*....|....*....|
gi 1681691554 244 KAPQHPYTKKLLSSLPfRGRPRQIDLTSVP 273
Cdd:COG0444 240 ENPRHPYTRALLSSIP-RLDPDGRRLIPIP 268
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
270-527 |
6.43e-121 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 358.66 E-value: 6.43e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIIVDYAGRKSLFRKNKPK-RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP- 347
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 348 ---RTENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRpVPGL-DGKAKRKRTLETLEEVGLGVDYAGRYPHELSGG 423
Cdd:COG4608 83 tglSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLR-IHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 424 QRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGD 503
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250 260
....*....|....*....|....
gi 1681691554 504 RDTIFDSPKEAYTRRLLSAIPALD 527
Cdd:COG4608 242 RDELYARPLHPYTQALLSAVPVPD 265
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
274-527 |
1.18e-110 |
|
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: 332.02 E-value: 1.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKSLFRknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLV---TESEGRIQFQGRP--- 347
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDllk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 348 -RTENWTDYRLN-CQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGL--GVDYAGRYPHELSGG 423
Cdd:COG0444 75 lSEKELRKIRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 424 QRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGD 503
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260
....*....|....*....|....
gi 1681691554 504 RDTIFDSPKEAYTRRLLSAIPALD 527
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLD 258
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
274-527 |
9.27e-108 |
|
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: 322.14 E-value: 9.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAgrkslfRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:COG1124 1 MLEVRNLSVSYG------QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 -DYRLNCQMVFQDPYSSLDPRMTIEALVEEALRpVPGLDgkAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIAR 432
Cdd:COG1124 75 kAFRRRVQMVFQDPYASLHPRHTVDRILAEPLR-IHGLP--DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 433 AIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK 512
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
250
....*....|....*
gi 1681691554 513 EAYTRRLLSAIPALD 527
Cdd:COG1124 232 HPYTRELLAASLAFE 246
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
274-502 |
2.07e-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: 302.50 E-value: 2.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKSlfrknkPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGG------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNC----QMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRT-LETLEEVGLGVDYAGRYPHELSGGQRQRV 428
Cdd:cd03257 75 RLRKIRrkeiQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 429 AIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
271-527 |
4.01e-92 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 284.93 E-value: 4.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 271 SVPMISARDIIVDYAGRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG----R 346
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 347 PRTENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQ 426
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 427 RVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDT 506
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250 260
....*....|....*....|.
gi 1681691554 507 IFDSPKEAYTRRLLSAIPALD 527
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLN 262
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-237 |
4.40e-92 |
|
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: 280.93 E-value: 4.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLS--LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEnE 83
Cdd:cd03257 1 LLEVKNLSvsFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT----SGSIIFDGKDLLKLSR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILdMLKRVGIRDPEGALSSYPHEFSGGMRQRI 163
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 164 MLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-259 |
1.40e-84 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 265.44 E-value: 1.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLE-------VARTGQQV--VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSY 71
Cdd:COG4608 2 AMAEPLLEVRDLKKHfpvrgglFGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT----SGEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 72 KGRDVLKMKENELRHLRgAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdPEgALSSY 151
Cdd:COG4608 78 DGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PE-HADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 152 PHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVaRYTS-RIVVMEK 230
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVV-RHISdRVAVMYL 233
|
250 260
....*....|....*....|....*....
gi 1681691554 231 GAIVEKGRTEDLLKAPQHPYTKKLLSSLP 259
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVP 262
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-259 |
8.45e-81 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 255.82 E-value: 8.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVARTGQ--QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKGRDVLKMKENE 83
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYPHEFSGGMRQRI 163
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 164 MLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250
....*....|....*.
gi 1681691554 244 KAPQHPYTKKLLSSLP 259
Cdd:PRK11022 243 RAPRHPYTQALLRALP 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-259 |
2.34e-79 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 251.95 E-value: 2.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 2 TMDKLLTVCGLSLEVARTGQQV--VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVaDGSVSYKGRDVLKM 79
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI-GGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 80 KENELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYPHEFSGGM 159
Cdd:PRK09473 87 PEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 160 RQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRT 239
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250 260
....*....|....*....|
gi 1681691554 240 EDLLKAPQHPYTKKLLSSLP 259
Cdd:PRK09473 247 RDVFYQPSHPYSIGLLNAVP 266
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
283-527 |
3.67e-79 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 251.55 E-value: 3.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 283 DYAGRKSLF-RKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT----ENWTDYRL 357
Cdd:PRK15079 19 DIKDGKQWFwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 358 NCQMVFQDPYSSLDPRMTIEALVEEALRPV-PGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIAR 436
Cdd:PRK15079 99 DIQMIFQDPLASLNPRMTIGEIIAEPLRTYhPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 437 RPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYT 516
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
250
....*....|.
gi 1681691554 517 RRLLSAIPALD 527
Cdd:PRK15079 259 KALMSAVPIPD 269
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
273-522 |
4.40e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 248.98 E-value: 4.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKSLFRKNKpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENw 352
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQQ-FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 tDYRLNCQ---MVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVA 429
Cdd:COG4167 81 -DYKYRCKhirMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|...
gi 1681691554 510 SPKEAYTRRLLSA 522
Cdd:COG4167 240 NPQHEVTKRLIES 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-263 |
7.65e-79 |
|
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: 247.79 E-value: 7.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSL--EVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYKGRDVlkmKEN 82
Cdd:COG1124 1 MLEVRNLSVsyGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKsTLL-RALAGLERPW----SGEVTFDGRPV---TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 ELRHLRGAeIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERrslILDMLKRVGIrdPEGALSSYPHEFSGGMRQR 162
Cdd:COG1124 73 RRKAFRRR-VQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGL--PPSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250 260
....*....|....*....|..
gi 1681691554 243 LKAPQHPYTKKLL-SSLPFRGR 263
Cdd:COG1124 227 LAGPKHPYTRELLaASLAFERA 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-259 |
2.15e-73 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 236.73 E-value: 2.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVaRTGQ---QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKGRDVLKMKEN 82
Cdd:COG4170 3 LLDIRNLTIEI-DTPQgrvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 ELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHT-KAS----AQERRSLILDMLKRVGIRDPEGALSSYPHEFSG 157
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTfKGKwwqrFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260
....*....|....*....|..
gi 1681691554 238 RTEDLLKAPQHPYTKKLLSSLP 259
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMP 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
273-526 |
1.34e-70 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 227.26 E-value: 1.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGrKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----R 348
Cdd:PRK10419 2 TLLNVSGLSHHYAH-GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 349 TENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRV 428
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 429 AIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEE---GDRD 505
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKL 240
|
250 260
....*....|....*....|..
gi 1681691554 506 TiFDSPKeayTRRLLSAI-PAL 526
Cdd:PRK10419 241 T-FSSPA---GRVLQNAVlPAF 258
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-256 |
2.08e-70 |
|
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: 225.33 E-value: 2.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKGRDVLKMKenelrhLRGAEIGVVFQEPMTSL 103
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTIGRQLEEGLILHTKASAQERrSLILDMLKRVGIRDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTT 183
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSKQAR-ALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 184 ALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLLS 256
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-259 |
7.55e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 227.15 E-value: 7.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGL--SLEVAR---TGQQVVKS---VSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYKG 73
Cdd:PRK11308 2 QQPLLQAIDLkkHYPVKRglfKPERLVKAldgVSFTLERGKTLAVVGESGCGKsTLA-RLLTMIETPT----GGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 74 RDVLKMKENELRHLRgAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdPEGAlSSYPH 153
Cdd:PRK11308 77 QDLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLR-PEHY-DRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250 260
....*....|....*....|....*.
gi 1681691554 234 VEKGRTEDLLKAPQHPYTKKLLSSLP 259
Cdd:PRK11308 234 VEKGTKEQIFNNPRHPYTQALLSATP 259
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
274-523 |
1.90e-68 |
|
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: 221.60 E-value: 1.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAgRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT---- 349
Cdd:TIGR02769 2 LLEVRDVTHTYR-TGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVA 429
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|....
gi 1681691554 510 SPKEAyTRRLLSAI 523
Cdd:TIGR02769 241 FKHPA-GRNLQSAV 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-269 |
1.23e-66 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 218.81 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRgAEIGVVFQEPMTSL 103
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT----DGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTIGRQLEEGL-ILHTKASAQERRSLILDMLKRVGIRdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPT 182
Cdd:PRK15079 112 NPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLL--PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 183 TALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLLSSLPF-- 260
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIpd 269
|
250
....*....|.
gi 1681691554 261 --RGRPRQIDL 269
Cdd:PRK15079 270 pdLERNKTIQL 280
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
273-515 |
4.06e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 215.73 E-value: 4.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenW 352
Cdd:COG3842 4 PALELENVSKRYGD----------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD----V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TD---YRLNCQMVFQDpYSsLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVA 429
Cdd:COG3842 70 TGlppEKRNVGMVFQD-YA-LFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDlgvveQ-----VADRVVVMQDGRIIEEGDR 504
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD-----QeealaLADRIAVMNDGRIEQVGTP 220
|
250
....*....|.
gi 1681691554 505 DTIFDSPKEAY 515
Cdd:COG3842 221 EEIYERPATRF 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
270-523 |
7.37e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 209.18 E-value: 7.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIivdyagRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT 349
Cdd:COG1116 3 AAAPALELRGV------SKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTDYRlncqMVFQDPysSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVA 429
Cdd:COG1116 77 GPGPDRG----VVFQEP--ALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDlgVVEQV--ADRVVVMQD--GRIIEE---- 501
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD--VDEAVflADRVVVLSArpGRIVEEidvd 226
|
250 260
....*....|....*....|....*.
gi 1681691554 502 --GDRD-TIFDSPK-EAYTRRLLSAI 523
Cdd:COG1116 227 lpRPRDrELRTSPEfAALRAEILDLL 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
298-520 |
2.11e-63 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 210.77 E-value: 2.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR-------PRtenwtdyRLNCQMVFQDPysSL 370
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlpPR-------ERRVGFVFQHY--AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 DPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:COG1118 87 FPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 451 DVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLL 520
Cdd:COG1118 165 DAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
274-523 |
2.76e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 206.77 E-value: 2.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIivdyagRKSlFRKNKpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:COG1126 1 MIEIENL------HKS-FGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 D---YRLNCQMVFQDPysSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAI 430
Cdd:COG1126 71 DinkLRRKVGMVFQQF--NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 431 ARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
250
....*....|...
gi 1681691554 511 PKEAYTRRLLSAI 523
Cdd:COG1126 227 PQHERTRAFLSKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-501 |
7.02e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 202.97 E-value: 7.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIivdyagRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----R 348
Cdd:COG1136 3 PLLELRNL------TKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 349 TENWTDYRL-NCQMVFQDPYssLDPRMTIEALVEEALRPVpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQR 427
Cdd:COG1136 77 ERELARLRRrHIGFVFQFFN--LLPELTALENVALPLLLA-GVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 428 VAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEE 501
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
275-501 |
4.64e-61 |
|
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: 200.39 E-value: 4.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYAGrkslfrKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTD 354
Cdd:cd03293 1 LEVRNVSKTYGG------GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 355 yrlnCQMVFQDPysSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAI 434
Cdd:cd03293 75 ----RGYVFQQD--ALLPWLTVLDNVALGLE-LQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 435 ARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVM--QDGRIIEE 501
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
275-508 |
2.51e-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: 198.71 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYAGRKslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWT 353
Cdd:COG1122 1 IELENLSFSYPGGT---------PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDiTKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQMVFQDPYSSLdprmtIEALVEE----ALRPVpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVA 429
Cdd:COG1122 72 ELRRKVGLVFQNPDDQL-----FAPTVEEdvafGPENL-GLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-257 |
3.67e-60 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 199.68 E-value: 3.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLE-VARTG------QQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYKGR 74
Cdd:COG4167 1 MSALLEVRNLSKTfKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKsTLA-KMLAGIIEPT----SGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 75 dVLKMKENELR--HLRgaeigVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdPEGALSsYP 152
Cdd:COG4167 76 -KLEYGDYKYRckHIR-----MIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLL-PEHANF-YP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 153 HEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGA 232
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
250 260
....*....|....*....|....*
gi 1681691554 233 IVEKGRTEDLLKAPQHPYTKKLLSS 257
Cdd:COG4167 228 VVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
274-530 |
7.05e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.46 E-value: 7.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIivdyagRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----RT 349
Cdd:COG1135 1 MIELENL------SKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltalSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTDYRLNCQMVFQDpySSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVA 429
Cdd:COG1135 75 RELRAARRKIGMIFQH--FNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250 260
....*....|....*....|.
gi 1681691554 510 SPKEAYTRRLLSAIPALDQNE 530
Cdd:COG1135 231 NPQSELTRRFLPTVLNDELPE 251
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
287-498 |
5.91e-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: 189.62 E-value: 5.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 287 RKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----RTENWTDYRL-NCQM 361
Cdd:cd03255 7 SKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklSEKELAAFRRrHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 362 VFQDPYssLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFL 441
Cdd:cd03255 87 VFQSFN--LLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRI 498
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
296-502 |
6.95e-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: 189.27 E-value: 6.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNWTDYRLNCQMVFQDPysSLDPRMT 375
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNIGMVFQDY--ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR 455
Cdd:cd03259 89 VAENIAFGLK-LRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 456 AQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
273-511 |
2.98e-56 |
|
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: 188.65 E-value: 2.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKslfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT--- 349
Cdd:COG1127 4 PMIEVRNLTKSFGDRV----------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITgls 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 -ENWTDYRLNCQMVFQDP--YSSldprMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQ 426
Cdd:COG1127 74 eKELYELRRRIGMLFQGGalFDS----LTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 427 RVAIARAIARRPRFLIADEPVSALD-VTVRAqVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRD 505
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
....*.
gi 1681691554 506 TIFDSP 511
Cdd:COG1127 228 ELLASD 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
293-524 |
2.68e-55 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 188.80 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVtESEGRI-----QFQGRPRTENWTDYRLN-----CQMV 362
Cdd:PRK11022 16 ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVmaeklEFNGQDLQRISEKERRNlvgaeVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 363 FQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGR---YPHELSGGQRQRVAIARAIARRPR 439
Cdd:PRK11022 95 FQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 440 FLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRL 519
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQAL 253
|
....*
gi 1681691554 520 LSAIP 524
Cdd:PRK11022 254 LRALP 258
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-264 |
3.39e-55 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 188.86 E-value: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVARTGQQV--VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKGRDVLKMKENE 83
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHT-------KASAQERRSLilDMLKRVGIRDPEGALSSYPHEFS 156
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTykgrwwqRFGWRKRRAI--ELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 157 GGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEK 236
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260
....*....|....*....|....*...
gi 1681691554 237 GRTEDLLKAPQHPYTKKLLSSLPFRGRP 264
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSA 268
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
273-530 |
5.08e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 185.65 E-value: 5.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----R 348
Cdd:COG3638 1 PMLELRNLSKRYPGGT---------PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 349 TENWTDYRLNCQMVFQDPYssLDPRMTiealVEEA-----------LRPVPGLDGKAKRKRTLETLEEVGLGvDYAGRYP 417
Cdd:COG3638 72 GRALRRLRRRIGMIFQQFN--LVPRLS----VLTNvlagrlgrtstWRSLLGLFPPEDRERALEALERVGLA-DKAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 418 HELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
250 260 270
....*....|....*....|....*....|...
gi 1681691554 498 IieegdrdtIFDSPKEAYTRRLLSAIPALDQNE 530
Cdd:COG3638 225 V--------VFDGPPAELTDAVLREIYGGEAEE 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
291-525 |
5.83e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 193.38 E-value: 5.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKR-ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL-----VTESEGRIQFQGRP--RTENWTDYRL---NC 359
Cdd:PRK15134 15 FRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESllHASEQTLRGVrgnKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 360 QMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGR---YPHELSGGQRQRVAIARAIAR 436
Cdd:PRK15134 95 AMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIR-QAAKRltdYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 437 RPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYT 516
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYT 253
|
....*....
gi 1681691554 517 RRLLSAIPA 525
Cdd:PRK15134 254 QKLLNSEPS 262
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-522 |
1.64e-54 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 184.99 E-value: 1.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKSLFRKNKPKrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenWT 353
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVE-AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--FG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQ---MVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAI 430
Cdd:PRK15112 81 DYSYRSQrirMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 431 ARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|..
gi 1681691554 511 PKEAYTRRLLSA 522
Cdd:PRK15112 241 PLHELTKRLIAG 252
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
289-497 |
3.23e-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: 182.28 E-value: 3.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 289 SLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPY 367
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDlTKLSLKELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SSLdprmtIEALVEE----ALRPVpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIA 443
Cdd:cd03225 86 DQF-----FGPTVEEevafGLENL-GLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 444 DEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-258 |
3.23e-54 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 183.86 E-value: 3.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTM--DKLLTVCGLSLEVARTGQQVV--KSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGR-- 74
Cdd:COG4107 1 MTNeeQPLLSVRGLSKRYGPGCGTVVacRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPT----SGSVYYRDRdg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 75 ---DVLKMKENELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLIlhtkaSAQER-----RSLILDMLKRVGIrdPEG 146
Cdd:COG4107 77 gprDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLM-----AAGERhygdiRARALEWLERVEI--PLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 147 ALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPmVARY-TSRI 225
Cdd:COG4107 150 RIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLG-VIRLlADRT 228
|
250 260 270
....*....|....*....|....*....|...
gi 1681691554 226 VVMEKGAIVEKGRTEDLLKAPQHPYTKKLLSSL 258
Cdd:COG4107 229 MVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
297-515 |
6.73e-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: 182.05 E-value: 6.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNWTDYRLNCQMVFQDpYSsLDPRMTI 376
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPVNTVFQN-YA-LFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:cd03300 90 FENIAFGLR-LKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 457 QVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAY 515
Cdd:cd03300 168 DMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
296-498 |
1.02e-52 |
|
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: 178.11 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP---RTENWTDYRLNCQMVFQDpySSLDP 372
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltdDKKNINELRQKVGMVFQQ--FNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 RMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:cd03262 90 HLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1681691554 453 TVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:cd03262 169 ELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
298-512 |
1.05e-52 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 182.58 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQDPysSLDPRMTie 377
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-NIAMVFQSY--ALYPHMT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 alVEE----ALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:COG3839 92 --VYEniafPLK-LRKVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 454 VRAQVLDLFSDLQKRYGFSCLFISHDlgvveQV-----ADRVVVMQDGRIIEEGDRDTIFDSPK 512
Cdd:COG3839 168 LRVEMRAEIKRLHRRLGTTTIYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPEELYDRPA 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
299-536 |
1.25e-52 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 181.85 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTeSEGRI----QFQGRpRTENWTDYRLN------CQMVFQDPYS 368
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGR-EILNLPEKELNklraeqISMIFQDPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 SLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGL--GVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 447 VSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPAL 526
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRL 268
|
250
....*....|
gi 1681691554 527 DQNEKGGVTL 536
Cdd:PRK09473 269 DAEGESLLTI 278
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
274-512 |
2.18e-52 |
|
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: 178.16 E-value: 2.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKSLFRknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE--- 350
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVT------ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 351 -NWTDYRLNCQMVFQDpYSSLDPRmTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVA 429
Cdd:cd03258 75 kELRKARRRIGMIFQH-FNLLSSR-TVFENVALPLE-IAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 1681691554 510 SPK 512
Cdd:cd03258 231 NPQ 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
295-507 |
2.73e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.95 E-value: 2.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 295 KPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPysSLDPRM 374
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEP--ALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TiealVEEALR---PVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:COG1131 89 T----VRENLRffaRLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 452 VTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:COG1131 164 PEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
297-511 |
1.25e-51 |
|
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: 176.15 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEN----WTDYRLNCQMVFQDP--YSSl 370
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaeLYRLRRRMGMLFQSGalFDS- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 dprMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:cd03261 92 ---LTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 451 DVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:cd03261 168 DPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
274-523 |
1.62e-51 |
|
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: 176.39 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEnWT 353
Cdd:COG1120 1 MLEAENLSVGYGGR----------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS-LS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQM--VFQDPysSLDPRMTIEALVEEALRPVPGL---DGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRV 428
Cdd:COG1120 70 RRELARRIayVPQEP--PAPFGLTVRELVALGRYPHLGLfgrPSAEDREAVEEALERTGLE-HLADRPVDELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 429 AIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGdrdtif 508
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG------ 220
|
250
....*....|....*
gi 1681691554 509 dSPKEAYTRRLLSAI 523
Cdd:COG1120 221 -PPEEVLTPELLEEV 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-507 |
1.95e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 183.30 E-value: 1.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGK-TLaTRALISLLPPTikvaDGSVSYKGRDVlkmkenELRHLRGAE---IGVV 95
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKsTL-MKILSGVYQPD----SGEILLDGEPV------RFRSPRDAQaagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 96 FQEPmtSLNPSMTI------GRQLEEGLILHTKASAQERRSLildmLKRVGIR-DPEGALSSYphefSGGMRQRIMLASV 168
Cdd:COG1129 85 HQEL--NLVPNLSVaeniflGREPRRGGLIDWRAMRRRAREL----LARLGLDiDPDTPVGDL----SVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 169 MLLKPALLIADEPTTALDAviqRDV---MELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLlka 245
Cdd:COG1129 155 LSRDARVLILDEPTASLTE---REVerlFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 246 pqhpyTKKLLSSL--------PFRGRPRQIDltsVPMISARDIIVdyagrkslfrknkpKRALHGVSIDIHEGEVVALVG 317
Cdd:COG1129 228 -----TEDELVRLmvgreledLFPKRAAAPG---EVVLEVEGLSV--------------GGVVRDVSFSVRAGEILGIAG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 318 GSGSGKTTLGRTIAGLVTESEGRIQFQGRPR----------------TENwtdyRLNcQMVFQDpySSLDPRMTIEALve 381
Cdd:COG1129 286 LVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdairagiayvPED----RKG-EGLVLD--LSIRENITLASL-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 382 EALRPVPGLDGKAKRKRTLETLEEVGLgvdyagRYPH------ELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR 455
Cdd:COG1129 357 DRLSRGGLLDRRRERALAEEYIKRLRI------KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAK 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 456 AQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:COG1129 431 AEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-252 |
2.03e-51 |
|
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: 175.94 E-value: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 2 TMDKLLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKE 81
Cdd:COG1127 1 MSEPMIEVRNLT--KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD----SGEILVDGQDITGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 82 NELRHLRgAEIGVVFQEPmtSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdpeGALSSYPHEFSGGMRQ 161
Cdd:COG1127 75 KELYELR-RRIGMLFQGG--ALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLP---GAADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 162 RIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTED 241
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
250
....*....|.
gi 1681691554 242 LLKAPqHPYTK 252
Cdd:COG1127 229 LLASD-DPWVR 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-235 |
8.05e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 173.69 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLS--LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLATraLISLL-PPTikvaDGSVSYKGRDVLK 78
Cdd:COG1136 1 MSPLLELRNLTksYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKsTLLN--ILGGLdRPT----SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 MKENELRHLRGAEIGVVFQEPmtSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGG 158
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLLA-GVSRKERRERARELLERVGL---GDRLDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDlPMVARYTSRIVVMEKGAIVE 235
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
270-515 |
2.46e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.97 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT 349
Cdd:COG1121 2 MMMPAIELENLTVSYGGR----------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTD--YrlncqmVFQdpYSSLDPR--MTIEALVEEAL---RPVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSG 422
Cdd:COG1121 72 RARRRigY------VPQ--RAEVDWDfpITVRDVVLMGRygrRGLFRRPSRADREAVDEALERVGLE-DLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 423 GQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMqDGRIIEEG 502
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHG 220
|
250
....*....|....*
gi 1681691554 503 DRDTIFDSP--KEAY 515
Cdd:COG1121 221 PPEEVLTPEnlSRAY 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-507 |
3.11e-50 |
|
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: 180.38 E-value: 3.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLatraLISLL------PPT--------------------------IKVADG 67
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVLrgmdqyEPTsgriiyhvalcekcgyverpskvgepCPVCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 68 SVSYKGRDVLKMKENELRHLRgAEIGVVFQ------EPMTSLNPSMtigRQLEEglilhTKASAQERRSLILDMLKRVGI 141
Cdd:TIGR03269 88 TLEPEEVDFWNLSDKLRRRIR-KRIAIMLQrtfalyGDDTVLDNVL---EALEE-----IGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 142 rdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARY 221
Cdd:TIGR03269 159 ---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 222 TSRIVVMEKGAIVEKGRTEDLLKapqhpytkKLLSSLPFRGRPRQIDLTSvPMISARDIIVDYAgrkSLFRKnkPKRALH 301
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVA--------VFMEGVSEVEKECEVEVGE-PIIKVRNVSKRYI---SVDRG--VVKAVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 302 GVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQ--------GRPRTENWTDYRLNCQMVFQDpYSSLDPR 373
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmTKPGPDGRGRAKRYIGILHQE-YDLYPHR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEALVEEALRPVPglDGKAKRKrTLETLEEVGLGVDYA----GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:TIGR03269 381 TVLDNLTEAIGLELP--DELARMK-AVITLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 450 LDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
291-511 |
3.27e-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: 172.49 E-value: 3.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDpySS 369
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYVIQQ--IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 LDPRMTIEalveEALRPVPGLDG---KAKRKRTLETLEEVGLG-VDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:cd03295 86 LFPHMTVE----ENIALVPKLLKwpkEKIRERADELLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
274-530 |
3.73e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 175.76 E-value: 3.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKslfrknKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT---- 349
Cdd:PRK11153 1 MIELKNISKVFPQGG------RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTDYRLNCQMVFQDpYSSLDPRmTIEALVEEALRpvpgLDGKAK---RKRTLETLEEVGLGvDYAGRYPHELSGGQRQ 426
Cdd:PRK11153 75 KELRKARRQIGMIFQH-FNLLSSR-TVFDNVALPLE----LAGTPKaeiKARVTELLELVGLS-DKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 427 RVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDT 506
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
250 260
....*....|....*....|....
gi 1681691554 507 IFDSPKEAYTRRLLSAIPALDQNE 530
Cdd:PRK11153 228 VFSHPKHPLTREFIQSTLHLDLPE 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-257 |
4.36e-50 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 172.58 E-value: 4.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVARTgqqVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKGRDVLKMKen 82
Cdd:PRK10418 1 MPQQIELRNIALQAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 elrhLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASaqeRRSLILDMLKRVGIRDPEGALSSYPHEFSGGMRQR 162
Cdd:PRK10418 76 ----LRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPA---DDATLTAALEAVGLENAARVLKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|....*
gi 1681691554 243 LKAPQHPYTKKLLSS 257
Cdd:PRK10418 229 FNAPKHAVTRSLVSA 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-233 |
6.30e-50 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 171.13 E-value: 6.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRGAEIGVVFQEPm 100
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT----SGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 tSLNPSMTIGRQLEEGLILHTKASAqERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:cd03255 92 -NLLPDLTALENVELPLLLAGVPKK-ERRERAEELLERVGLGD---RLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 181 PTTALDAVIQRDVMELMVELTRAEGTAILLISHDlPMVARYTSRIVVMEKGAI 233
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
298-529 |
6.82e-50 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 174.71 E-value: 6.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES----EGRIQFQGR------PRtENWTDYRLNCQMVFQDPY 367
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIdllklsPR-ERRKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SSLDPRMTIEALVEEALrPVPGLDG------KAKRKRTLETLEEVGLG--VDYAGRYPHELSGGQRQRVAIARAIARRPR 439
Cdd:COG4170 100 SCLDPSAKIGDQLIEAI-PSWTFKGkwwqrfKWRKKRAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 440 FLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRL 519
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKAL 258
|
250
....*....|
gi 1681691554 520 LSAIPALDQN 529
Cdd:COG4170 259 LRSMPDFRQP 268
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
288-498 |
9.63e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 9.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDP 366
Cdd:COG4619 4 EGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 YssldprmTIEALVEEALRPVPGLDGKA-KRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:COG4619 84 A-------LWGGTVRDNLPFPFQLRERKfDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
298-515 |
3.05e-49 |
|
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: 169.83 E-value: 3.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQdpYSSLDPRMTIE 377
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVFQ--HYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 ALVEEALR--PVPGLDGKAK-RKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:cd03296 93 DNVAFGLRvkPRSERPPEAEiRAKVHELLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 455 RAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAY 515
Cdd:cd03296 172 RKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-507 |
3.36e-49 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 177.14 E-value: 3.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 25 KSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkenelrHLRG------AEIGVVFQE 98
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD----SGEILIDGKPV---------RIRSprdaiaLGIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PMtsLNPSMT------IGRQLEEGLILHTKASAQErrslILDMLKRVGIR-DPEgalsSYPHEFSGGMRQRIMLASVMLL 171
Cdd:COG3845 89 FM--LVPNLTvaenivLGLEPTKGGRLDRKAARAR----IRELSERYGLDvDPD----AKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLlkapqhpyT 251
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET--------S 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 252 KKLLSSLPFrGR--PRQIDLTSV----PMISARDIIVdyagrkslfRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTT 325
Cdd:COG3845 230 EEELAELMV-GRevLLRVEKAPAepgeVVLEVENLSV---------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 326 LGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVF--QDPYSS-LDPRMTI-EALV-----EEALRPVPGLDGKAKR 396
Cdd:COG3845 300 LAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYipEDRLGRgLVPDMSVaENLIlgryrRPPFSRGGFLDRKAIR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 397 KRTLETLEEvglgvdYAGRYPHE------LSGGQRQRVAIARAIARRPRFLIADEPVSALDV----TVRAQVLDLfsdlq 466
Cdd:COG3845 380 AFAEELIEE------FDVRTPGPdtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLEL----- 448
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1681691554 467 KRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:COG3845 449 RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
297-497 |
4.01e-49 |
|
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: 167.36 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGrprtENWTDYRLNCQ-------MVFQDPysS 369
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG----EDLTDLEDELPplrrrigMVFQDF--A 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 LDPRMTIealveealrpvpgldgkakrkrtletLEEVGLGvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:cd03229 87 LFPHLTV--------------------------LENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 450 LDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:cd03229 131 LDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
297-523 |
1.06e-48 |
|
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: 168.52 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNWTDYRLNCQ-----MVFQDPysSLD 371
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN-KLKGKALRQLrrqigMIFQQF--NLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMT-IEALVEEAL------RPVPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIAD 444
Cdd:cd03256 91 ERLSvLENVLSGRLgrrstwRSLFGLFPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 445 EPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIieegdrdtIFDSPKEAYTRRLLSAI 523
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGPPAELTDEVLDEI 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-252 |
2.41e-48 |
|
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: 167.29 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRgAEIG 93
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD----SGEVLIDGEDISGLSEAELYRLR-RRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQEPmtSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdpeGALSSYPHEFSGGMRQRIMLASVMLLKP 173
Cdd:cd03261 81 MLFQSG--ALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR---GAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDlLKAPQHPYTK 252
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LRASDDPLVR 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
299-504 |
2.58e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.77 E-value: 2.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----RTENWTDYRLNCQMVFQDpySSLDPRM 374
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlKRREIPYLRRRIGVVFQD--FRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:COG2884 95 TVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 455 RAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDR 504
Cdd:COG2884 173 SWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
276-518 |
3.07e-48 |
|
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: 168.21 E-value: 3.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 276 SARDIIVDYAGRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-----RTE 350
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 351 NWTDYRLNCQMVFQDpySSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAI 430
Cdd:cd03294 96 LRELRRKKISMVFQS--FALLPHRTVLENVAFGLE-VQGVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 431 ARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
....*...
gi 1681691554 511 PKEAYTRR 518
Cdd:cd03294 252 PANDYVRE 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-257 |
2.60e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 165.48 E-value: 2.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGR-----D 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYG--PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD----AGEVHYRMRdgqlrD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 76 VLKMKENELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIrdPEGALSSYPHEF 155
Cdd:PRK11701 75 LYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEI--DAARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPmVARYTS-RIVVMEKGAIV 234
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLA-VARLLAhRLLVMKQGRVV 231
|
250 260
....*....|....*....|...
gi 1681691554 235 EKGRTEDLLKAPQHPYTKKLLSS 257
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
303-511 |
4.81e-47 |
|
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: 167.59 E-value: 4.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenWTD---------YRLNCQMVFQDPysSLDPR 373
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV----LQDsargiflppHRRRIGYVFQEA--RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEALVEEALRPVPGLDGKAKRKRTLETLeevGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEVVELL---GIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 454 VRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
297-508 |
1.16e-46 |
|
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: 164.14 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG-RPRTE-NWTDYRLNCQMVFQDPYSSLdprm 374
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEeNLWEIRKKVGMVFQNPDNQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 tIEALVE-------EALrpvpGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:TIGR04520 91 -VGATVEddvafglENL----GVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 448 SALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIF 508
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-267 |
1.26e-46 |
|
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: 163.82 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 17 ARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVLKMKENELRHLRgAEIGVVF 96
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP----AQGTVSFRGQDLYQLDRKQRRAFR-RDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEgaLSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:TIGR02769 95 QDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSED--ADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKApQHPYTKKLLS 256
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQS 251
|
250
....*....|..
gi 1681691554 257 S-LPFRGRPRQI 267
Cdd:TIGR02769 252 AvLPEHPVRRSI 263
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-245 |
1.32e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.93 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaeIGVVFQEP 99
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT----SGEVRVLGEDVARDPAEVRRR-----IGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:COG1131 83 --ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 180 EPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:COG1131 157 EPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-247 |
2.10e-46 |
|
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: 162.12 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaEIGVVFQe 98
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKsTLL-RLLNGLLKPT----SGEVLVDGKDITKKNLRELRR----KVGLVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 pmtslNP-----SMTIgrqLEE---GLiLHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVML 170
Cdd:COG1122 83 -----NPddqlfAPTV---EEDvafGP-ENLGLPREEIRERVEEALELVGL---EHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 171 LKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
301-526 |
2.58e-46 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 162.56 E-value: 2.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 301 HGVSIDIHEGEVVALVGGSGSGKT-----TLGRTIAGlVTESEGRIQFQGRPRTENWTDYRLnCQMVFQDPYSSLDPRMT 375
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAG-VRQTAGRVLLDGKPVAPCALRGRK-IATIMQNPRSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALVEEALRPVpgldGKAKRKRTL-ETLEEVGLGVD--YAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:PRK10418 98 MHTHARETCLAL----GKPADDATLtAALEAVGLENAarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 453 TVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPAL 526
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLAL 247
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
297-536 |
5.53e-46 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 163.34 E-value: 5.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDpySSLDPRMT 375
Cdd:COG1125 15 TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDiRDLDPVELRRRIGYVIQQ--IGLFPHMT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IE---ALVEEALrpvpGLDGKAKRKRTLETLEEVGLGVD-YAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:COG1125 93 VAeniATVPRLL----GWDKERIRARVDELLELVGLDPEeYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 452 VTVRAQVLDLFSDLQKRYGFSCLFISHDLGvvEQV--ADRVVVMQDGRIIEEGDRDTIFDSPKEAYTR---------RLL 520
Cdd:COG1125 169 PITREQLQDELLRLQRELGKTIVFVTHDID--EALklGDRIAVMREGRIVQYDTPEEILANPANDFVAdfvgadrglRRL 246
|
250
....*....|....*.
gi 1681691554 521 SAIPALDQNEKGGVTL 536
Cdd:COG1125 247 SLLRVEDLMLPEPPTV 262
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-250 |
1.88e-45 |
|
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: 160.89 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQV-VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRGAEIGVVF 96
Cdd:cd03294 33 KTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT----SGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEpmTSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:cd03294 109 QS--FALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPY 250
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
297-513 |
2.39e-45 |
|
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: 160.69 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR---PRT-ENWTDYRLNCQMVFQDPYSSLdp 372
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKkKKLKDLRKKVGLVFQFPEHQL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 rmtIEALVEE--ALRPVP-GLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:TIGR04521 96 ---FEETVYKdiAFGPKNlGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 450 LDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKE 513
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-257 |
4.75e-45 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 159.57 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVA-RTG----QQV--VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPT---IKVADGSVSYK 72
Cdd:PRK15112 1 VETLLEVRNLSKTFRyRTGwfrrQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTsgeLLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 73 GRdvlkmkenelrHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdPEGAlSSYP 152
Cdd:PRK15112 81 DY-----------SYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLL-PDHA-SYYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 153 HEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGA 232
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
250 260
....*....|....*....|....*
gi 1681691554 233 IVEKGRTEDLLKAPQHPYTKKLLSS 257
Cdd:PRK15112 228 VVERGSTADVLASPLHELTKRLIAG 252
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
300-520 |
6.45e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 158.33 E-value: 6.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQ---MVFQDPYssLDPRMTi 376
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQeagMVFQQFY--LFPHLT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 eALVEEALRP--VPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:PRK09493 94 -ALENVMFGPlrVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 455 RAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLL 520
Cdd:PRK09493 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
315-523 |
8.15e-45 |
|
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: 160.74 E-value: 8.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 315 LVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENwTDYRLNCQMVFQDpySSLDPRMTIEALVEEALRpVPGLDGKA 394
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV-PPHLRHINMVFQS--YALFPHMTVEENVAFGLK-MRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 395 KRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCL 474
Cdd:TIGR01187 77 IKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1681691554 475 FISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAI 523
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
297-502 |
1.26e-44 |
|
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: 155.67 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrTENWTDYRLNCQMvfqdpyssldprmti 376
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-LASLSPKELARKI--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 eALVEEALrpvpgldgkakrkrtletlEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:cd03214 76 -AYVPQAL-------------------ELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1681691554 457 QVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-258 |
1.33e-44 |
|
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: 158.07 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRD-----VLKMK 80
Cdd:TIGR02323 3 LLQVSGLSKSYG--GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPD----HGTATYIMRSgaeleLYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 81 ENELRHLRGAEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMR 160
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEI--DPTRIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 161 QRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTE 240
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
250
....*....|....*...
gi 1681691554 241 DLLKAPQHPYTKKLLSSL 258
Cdd:TIGR02323 235 QVLDDPQHPYTQLLVSSI 252
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
296-507 |
1.88e-44 |
|
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: 156.96 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTE-----SEGRIQFQGRPRTENWTD---YRLNCQMVFQDPY 367
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvleLRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 ssldP-RMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGR--YPHELSGGQRQRVAIARAIARRPRFLIAD 444
Cdd:cd03260 92 ----PfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALW-DEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 445 EPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
307-522 |
2.62e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.45 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 307 IHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLnCQMVFQDpySSLDPRMTIEALVEEALRP 386
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-VSMLFQE--NNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 387 vpGLD-GKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDL 465
Cdd:COG3840 99 --GLKlTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 466 QKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSA 522
Cdd:COG3840 176 CRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
270-523 |
6.71e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 156.24 E-value: 6.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIIVDYAGRKslfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFqgRPRT 349
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRK----------GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY--RMRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTD------------YRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYP 417
Cdd:PRK11701 70 GQLRDlyalseaerrrlLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 418 HELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|....*.
gi 1681691554 498 IIEEGDRDTIFDSPKEAYTRRLLSAI 523
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
299-512 |
7.43e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 155.56 E-value: 7.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQ-------FQGRPRTENWTDYRLNCQMVFQDpYSsLD 371
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIRELRRNVGMVFQQ-YN-LW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMT-IEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:PRK11124 95 PHLTvQQNLIEAPCR-VLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 451 DVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTiFDSPK 512
Cdd:PRK11124 173 DPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
298-515 |
1.10e-43 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 155.58 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNWTDYRLnCQM----VFQDPysSLDPR 373
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-GLPPHRI-ARLgiarTFQNP--RLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTI-------------EALVEEALR-PVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPR 439
Cdd:COG0411 94 LTVlenvlvaaharlgRGLLAALLRlPRARREEREARERAEELLERVGLA-DRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 440 FLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK--EAY 515
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRviEAY 250
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
299-505 |
2.34e-43 |
|
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: 164.24 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDPY---SSL---- 370
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFlfsGTIreni 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 ---DPRMTIEAlVEEALRPVpGLDGK-AKRKRTLET-LEEVGLGvdyagrypheLSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:COG2274 570 tlgDPDATDEE-IIEAARLA-GLHDFiEALPMGYDTvVGEGGSN----------LSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRD 505
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHE 694
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
297-502 |
3.46e-43 |
|
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: 153.99 E-value: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG----RPRTENWTDYRLNCQMVFQDpySSLDP 372
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditKLRGKKLRKLRRRIGMIFQH--YNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 RMT-IEALVEEALRPVPGLDG------KAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:TIGR02315 93 RLTvLENVLHGRLGYKPTWRSllgrfsEEDKERALSALERVGL-ADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-247 |
3.90e-43 |
|
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: 153.51 E-value: 3.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRaLISLLP-PTikvaDGSVSYKGRDVLKMKENELRHLRgAEIGVVFQE--P 99
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLErPT----SGSVLVDGTDLTLLSGKELRKAR-RRIGMIFQHfnL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSLNPSMTIGRQLEeglILHTKASAQERRslILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03258 94 LSSRTVFENVALPLE---IAGVPKAEIEER--VLELLELVGLEDKADA---YPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-231 |
3.99e-43 |
|
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: 152.62 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgA 90
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT----SGEVLVDGKDLTKLSLKELR----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 EIGVVFQEPMTSL-NPsmTIGRQLEEGLiLHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVM 169
Cdd:cd03225 76 KVGLVFQNPDDQFfGP--TVEEEVAFGL-ENLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 170 LLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
295-498 |
5.67e-43 |
|
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: 152.41 E-value: 5.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 295 KPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRpRTENWTDYRLNCQMVFQDpYSsLDPRM 374
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-DVTDLPPKDRDIAMVFQN-YA-LYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:cd03301 88 TVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1681691554 455 RAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:cd03301 166 RVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
299-526 |
8.70e-43 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 152.65 E-value: 8.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQdpYSSLDPRMTIEA 378
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDR-KIGFVFQ--HYALFKHLTVRD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:TIGR00968 92 NIAFGLE-IRKHPKAKIKARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 459 LDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPAL 526
Cdd:TIGR00968 170 RSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
309-502 |
9.21e-43 |
|
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: 151.68 E-value: 9.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 309 EGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenWTDYRLNCQM---------VFQDpySSLDPRMTIEAL 379
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV----LFDSRKKINLppqqrkiglVFQQ--YALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 VEEALRpvpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVL 459
Cdd:cd03297 96 LAFGLK---RKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1681691554 460 DLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
273-508 |
1.97e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.86 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYagrkslfrKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEN- 351
Cdd:PRK13635 4 EIIRVEHISFRY--------PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 352 -WtDYRLNCQMVFQDPysslDPRM---TIEALVEEAL--RPVPGLDgkaKRKRTLETLEEVGLgVDYAGRYPHELSGGQR 425
Cdd:PRK13635 76 vW-DVRRQVGMVFQNP----DNQFvgaTVQDDVAFGLenIGVPREE---MVERVDQALRQVGM-EDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 426 QRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRD 505
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
...
gi 1681691554 506 TIF 508
Cdd:PRK13635 226 EIF 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
288-498 |
2.67e-42 |
|
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: 149.08 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPy 367
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 sSLDPRMTiealVEEALRpvpgldgkakrkrtletleevglgvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:cd03230 83 -SLYENLT----VRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 448 SALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-333 |
4.19e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 153.69 E-value: 4.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRaLISLL-PPTikvaDGSVSYKGRDVLKMKENELRHLRgAEIGVVFQEP 99
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKsTLI-R-CINLLeRPT----SGSVLVDGVDLTALSERELRAAR-RKIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMT----IGRQLEeglilHTKASAQERRSLILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPAL 175
Cdd:COG1135 92 --NLLSSRTvaenVALPLE-----IAGVPKAEIRKRVAELLELVGLSDKADA---YPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 176 LIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLL 255
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 256 SSLPFRGRPRQIDLTSVPMISARDII-VDYAGRKS-------LFRKnkpkralHGVSIDIHEGEVVALvggsgsGKTTLG 327
Cdd:COG1135 242 PTVLNDELPEELLARLREAAGGGRLVrLTFVGESAdepllseLARR-------FGVDVNILSGGIEEI------QGTPVG 308
|
....*.
gi 1681691554 328 RTIAGL 333
Cdd:COG1135 309 RLIVEL 314
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
274-507 |
4.57e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 150.78 E-value: 4.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYagrkslfrknKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:COG4555 1 MIEVENLSKKY----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQMVFQDPYssLDPRMTiealVEEALR---PVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAI 430
Cdd:COG4555 71 EARRQIGVLPDERG--LYDRLT----VRENIRyfaELYGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 431 ARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
273-500 |
1.23e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 150.40 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKSlfrknkPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENW 352
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ------PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDyRlncQMVFQDpySSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIAR 432
Cdd:COG4525 76 AD-R---GVVFQK--DALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 433 AIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDlgvVEQ---VADRVVVMQD--GRIIE 500
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVMSPgpGRIVE 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-238 |
1.71e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.66 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRgAEIGVVFQ 97
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT----SGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EpmTSLNPSMTIGRQLEegLILH-TKASAQERRSLILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:COG2884 87 D--FRLLPDRTVYENVA--LPLRvTGKSRKEIRRRVREVLDLVGLSDKAKA---LPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGR 238
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
300-533 |
2.61e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 152.16 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGrprtenwTDY-RLNCQ-----MVFQdpYSSLDPR 373
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG-------TDVsRLHARdrkvgFVFQ--HYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEALVEEALRPVPG---LDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:PRK10851 89 MTVFDNIAFGLTVLPRrerPNAAAIKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 451 DVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPALDQNE 530
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRLQGTI 247
|
...
gi 1681691554 531 KGG 533
Cdd:PRK10851 248 RGG 250
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
299-512 |
4.45e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 148.24 E-value: 4.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQ-------FQGRPRTENWTDYRLNCQMVFQDpYSsLD 371
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdFSQKPSEKAIRLLRQKVGMVFQQ-YN-LW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMT-IEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:COG4161 95 PHLTvMENLIEAPCK-VLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 451 DVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRdTIFDSPK 512
Cdd:COG4161 173 DPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
298-512 |
4.83e-41 |
|
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: 147.97 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNWTDYRLnCQM----VFQDPysSLDPR 373
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-GLPPHEI-ARLgigrTFQIP--RLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIE---ALVEEALRPVPGLDGKAK------RKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIAD 444
Cdd:cd03219 90 LTVLenvMVAAQARTGSGLLLARARreereaRERAEELLERVGLA-DLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 445 EPVSALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK 512
Cdd:cd03219 169 EPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-522 |
5.61e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 148.34 E-value: 5.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEnWT 353
Cdd:COG4559 1 MLEAENLSVRLGGR----------TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA-WS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRL---------NCQMVFqdPYssldprmTIEALVEEALRPVpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQ 424
Cdd:COG4559 70 PWELarrravlpqHSSLAF--PF-------TVEEVVALGRAPH-GSSAAQDRQIVREALALVGLA-HLAGRSYQTLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 425 RQRVAIARAIA-------RRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:COG4559 139 QQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
250 260
....*....|....*....|....*
gi 1681691554 498 IIEEGdrdtifdSPKEAYTRRLLSA 522
Cdd:COG4559 218 LVAQG-------TPEEVLTDELLER 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
270-501 |
8.85e-41 |
|
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: 147.20 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIivdyagRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT 349
Cdd:COG4181 4 SSAPIIELRGL------TKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTDYRL-----NCQMVFQDpySSLDPRMTieALvEEALRPVPgLDGKAK-RKRTLETLEEVGLGvDYAGRYPHELSGG 423
Cdd:COG4181 78 ALDEDARArlrarHVGFVFQS--FQLLPTLT--AL-ENVMLPLE-LAGRRDaRARARALLERVGLG-HRLDHYPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 424 QRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEE 501
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
271-507 |
1.05e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 153.64 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 271 SVPMISARDIIVDYAGRKslfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTe 350
Cdd:COG1129 1 AEPLLEMRGISKSFGGVK----------ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 351 nWTDYR----LNCQMVFQDPysSLDPRMTIE---ALVEEALRPvPGLDGKAKRKRTLETLEEVGLGVDyagryPH----E 419
Cdd:COG1129 70 -FRSPRdaqaAGIAIIHQEL--NLVPNLSVAeniFLGREPRRG-GLIDWRAMRRRARELLARLGLDID-----PDtpvgD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 420 LSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
....*...
gi 1681691554 500 EEGDRDTI 507
Cdd:COG1129 220 GTGPVAEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
298-499 |
1.35e-40 |
|
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: 144.11 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenwtdyrlncqmvfqdpYSSLDPRmtie 377
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-------------------VSFASPR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 alveEALRpvpgldgkakrkrtletleevgLGVdyagRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQ 457
Cdd:cd03216 71 ----DARR----------------------AGI----AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1681691554 458 VLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:cd03216 121 LFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-266 |
2.51e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 147.14 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLS-------LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLK 78
Cdd:PRK10419 3 LLNVSGLShhyahggLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS----QGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 MKENELRHLRGaEIGVVFQEPMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDpeGALSSYPHEFSGG 158
Cdd:PRK10419 79 LNRAQRKAFRR-DIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGR 238
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
250 260
....*....|....*....|....*....
gi 1681691554 239 TEDLLkAPQHPYTKKLLSS-LPFRGRPRQ 266
Cdd:PRK10419 236 VGDKL-TFSSPAGRVLQNAvLPAFPVRRR 263
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-243 |
3.48e-40 |
|
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: 145.96 E-value: 3.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYKGRDVLKMKENEL 84
Cdd:COG1120 1 MLEAENLS--VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKsTLL-RALAGLLKPS----SGEVLLDGRDLASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 85 -RHlrgaeIGVVFQEPmtSLNPSMTIGRQLEEGLILHTKASAQER---RSLILDMLKRVGIRDpegaLSSYP-HEFSGGM 159
Cdd:COG1120 74 aRR-----IAYVPQEP--PAPFGLTVRELVALGRYPHLGLFGRPSaedREAVEEALERTGLEH----LADRPvDELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 160 RQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRT 239
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 1681691554 240 EDLL 243
Cdd:COG1120 223 EEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
300-446 |
4.38e-40 |
|
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: 142.40 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPysSLDPRMTIEA 378
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 379 LVEEALRpVPGLDGKAKRKRTLETLEEVGLGV---DYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
300-522 |
5.71e-40 |
|
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: 145.17 E-value: 5.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQDPYssLDPRMTIEAL 379
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR-DISYVPQNYA--LFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 VEEALRPVpgLDGKAKRKRTLETLEEVgLGVDYA-GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:cd03299 92 IAYGLKKR--KVDKKEIERKVLEIAEM-LGIDHLlNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 459 LDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSA 522
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGF 232
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
287-500 |
5.93e-40 |
|
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: 144.42 E-value: 5.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 287 RKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP---RTENWTDYRLNCQMVF 363
Cdd:TIGR02211 8 GKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlskLSSNERAKLRNKKLGF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 364 QDPYSSLDPRMTiealveeALRPV--PGLDGKAKRK----RTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARR 437
Cdd:TIGR02211 88 IYQFHHLLPDFT-------ALENVamPLLIGKKSVKeakeRAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 438 PRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIE 500
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
300-532 |
8.67e-40 |
|
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: 148.22 E-value: 8.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES--EGRIQFQGRPRTeNWTDYRLNCQMVFQDpySSLDPRMTIE 377
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLT-HAPPHKRGLALLFQN--YALFPHLKVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 ALVEEALRPVPGLDGKAKRkRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQ 457
Cdd:TIGR03258 98 DNVAFGLRAQKMPKADIAE-RVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 458 VLDLFSDLQKRY-GFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPALDQNEKG 532
Cdd:TIGR03258 176 MREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPAIALG 251
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
270-522 |
8.75e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 145.33 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIivdyagRKSlFRKNKpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF------ 343
Cdd:COG4598 4 TAPPALEVRDL------HKS-FGDLE---VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeir 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 344 -----QGRPRTENW---TDYRLNCQMVFQDpySSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGvDYAGR 415
Cdd:COG4598 74 lkpdrDGELVPADRrqlQRIRTRLGMVFQS--FNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLA-DKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 416 YPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQD 495
Cdd:COG4598 151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQ 229
|
250 260
....*....|....*....|....*..
gi 1681691554 496 GRIIEEGDRDTIFDSPKEAYTRRLLSA 522
Cdd:COG4598 230 GRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
291-499 |
9.31e-40 |
|
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: 143.55 E-value: 9.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENwtDYRLNCQMVFQDPYSSL 370
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 dprmtIEALVEEALRPvpGLDGKAKRKRTLET-LEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:cd03226 85 -----FTDSVREELLL--GLKELDAGNEQAETvLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 450 LDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:cd03226 157 LDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
294-497 |
9.83e-40 |
|
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: 142.14 E-value: 9.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 294 NKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPYssldp 372
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlRDLDLESLRKNIAYVPQDPF----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 rmtieaLVEEALRpvpgldgkakrkrtletlEEVglgvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:cd03228 87 ------LFSGTIR------------------ENI-------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1681691554 453 TVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGR 497
Cdd:cd03228 130 ETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
297-499 |
1.12e-39 |
|
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: 143.44 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTD--YrlncqmVFQDPYSSLDPRM 374
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigY------VPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEEALRPVPGLDG---KAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:cd03235 86 SVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 452 VTVRAQVLDLFSDLQkRYGFSCLFISHDLGVVEQVADRVVVMqDGRII 499
Cdd:cd03235 165 PKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
274-508 |
1.24e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 145.62 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKslfrKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG--RPRTEN 351
Cdd:PRK13633 4 MIKCKNVSYKYESNE----ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 352 WTDYRLNCQMVFQDPYSSLdprmtIEALVEEALRPVP---GLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRV 428
Cdd:PRK13633 80 LWDIRNKAGMVFQNPDNQI-----VATIVEEDVAFGPenlGIPPEEIRERVDESLKKVGM-YEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 429 AIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-258 |
1.96e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.08 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDK-LLTVCGLSL--EVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVL 77
Cdd:COG1116 1 MSAAApALELRGVSKrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT----SGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 78 KmkenelrhlRGAEIGVVFQEPmtSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSG 157
Cdd:COG1116 77 G---------PGPDRGVVFQEP--ALLPWLTVLDNVALGLELR-GVPKAERRERARELLELVGL---AGFEDAYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEK--GAIVE 235
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
250 260 270
....*....|....*....|....*....|.
gi 1681691554 236 -------KGRTEDLLKAPQ-HPYTKKLLSSL 258
Cdd:COG1116 222 eidvdlpRPRDRELRTSPEfAALRAEILDLL 252
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
297-497 |
2.53e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 140.46 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEN-WTDYRLNCQMVFQdpyssldprmt 375
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 iealveealrpvpgldgkakrkrtletleevglgvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR 455
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1681691554 456 AQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
296-524 |
4.68e-39 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 145.33 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGlVTESEGRIQfQGRPRTENWTDYRL-----------NCQMVFQ 364
Cdd:PRK15093 19 WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVT-ADRMRFDDIDLLRLsprerrklvghNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 365 DPYSSLDPRMTIEalvEEALRPVPGLDGKA--------KRKRTLETLEEVGLG--VDYAGRYPHELSGGQRQRVAIARAI 434
Cdd:PRK15093 97 EPQSCLDPSERVG---RQLMQNIPGWTYKGrwwqrfgwRKRRAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 435 ARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEA 514
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHP 253
|
250
....*....|
gi 1681691554 515 YTRRLLSAIP 524
Cdd:PRK15093 254 YTQALIRAIP 263
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
288-521 |
4.89e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF------QGRPRTENWTDYRLNCQ- 360
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQLRQh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 361 --MVFQDpySSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLgvdyAGR---YPHELSGGQRQRVAIARAIA 435
Cdd:PRK11264 87 vgFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKetsYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 436 RRPRFLIADEPVSALDVTVRAQVLDLFSDL--QKRygfSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKE 513
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*...
gi 1681691554 514 AYTRRLLS 521
Cdd:PRK11264 238 PRTRQFLE 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
273-497 |
5.69e-39 |
|
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: 141.46 E-value: 5.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKsLFRknkpkralhGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENW 352
Cdd:COG4133 1 MMLEAENLSCRRGERL-LFS---------GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLncQMVFQDPYSSLDPRMTiealVEEALRPVPGLDG-KAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIA 431
Cdd:COG4133 71 EDYRR--RLAYLGHADGLKPELT----VRENLRFWAALYGlRADREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 432 RAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLgvVEQVADRVVVMQDGR 497
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQP--LELAAARVLDLGDFK 206
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
273-523 |
7.61e-39 |
|
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: 142.66 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKSLFrknkpkralhGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR------ 346
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCR----------DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaele 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 347 ----PRTENWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSG 422
Cdd:TIGR02323 72 lyqlSEAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 423 GQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 1681691554 503 DRDTIFDSPKEAYTRRLLSAI 523
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
273-522 |
7.78e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.60 E-value: 7.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEnW 352
Cdd:PRK13548 1 AMLEARNLSVRLGGR----------TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD-W 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLN------CQmvfqdpYSSLDPRMTIEALVEEALrpVPGLDGKAKRKRTLET-LEEVGLgVDYAGRYPHELSGGQR 425
Cdd:PRK13548 70 SPAELArrravlPQ------HSSLSFPFTVEEVVAMGR--APHGLSRAEDDALVAAaLAQVDL-AHLAGRDYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 426 QRVAIARAIAR------RPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:PRK13548 141 QRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
250 260
....*....|....*....|...
gi 1681691554 500 EEGdrdtifdSPKEAYTRRLLSA 522
Cdd:PRK13548 221 ADG-------TPAEVLTPETLRR 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
265-506 |
1.02e-38 |
|
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: 149.14 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 265 RQIDLTSVPMISARDIIVDYAGRKslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQ 344
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGR---------PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 345 GRPRTE-NWTDYRLNCQMVFQDPY---SSL-------DPRMTIEALvEEALRPVpGLDGKAKR-KRTLET-LEEVGLGvd 411
Cdd:COG4988 398 GVDLSDlDPASWRRQIAWVPQNPYlfaGTIrenlrlgRPDASDEEL-EAALEAA-GLDEFVAAlPDGLDTpLGEGGRG-- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 412 yagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVV 491
Cdd:COG4988 474 --------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRIL 542
|
250
....*....|....*
gi 1681691554 492 VMQDGRIIEEGDRDT 506
Cdd:COG4988 543 VLDDGRIVEQGTHEE 557
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-240 |
1.53e-38 |
|
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: 141.03 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSLEVARTGQQVV--KSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKE 81
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELTilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT----SGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 82 NELRHLRGAEIGVVFQEPMtsLNPSMT----IGRQLEEglilhtkASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSG 157
Cdd:COG4181 82 DARARLRARHVGFVFQSFQ--LLPTLTalenVMLPLEL-------AGRRDARARARALLERVGL---GHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKG 237
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
...
gi 1681691554 238 RTE 240
Cdd:COG4181 229 AAT 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
297-527 |
2.18e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 144.70 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQDpYSsLDPRMTI 376
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR-HVNTVFQS-YA-LFPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALR--PVPgldgKAK-RKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:PRK09452 104 FENVAFGLRmqKTP----AAEiTPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 454 VRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPALD 527
Cdd:PRK09452 179 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFD 252
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-507 |
5.39e-38 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 146.35 E-value: 5.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIkvadGSVSYKGRDVLKMK 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYS--GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS----GTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 81 ENELRHLrgaEIGVVFQEPMtsLNPSMTIGRQLEEGLILHTKAS-------AQERRSLILDMlkrvgirdPEGALSSYPH 153
Cdd:PRK15439 80 PAKAHQL---GIYLVPQEPL--LFPNLSVKENILFGLPKRQASMqkmkqllAALGCQLDLDS--------SAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLASVmllkpalLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PRK15439 147 QIVEILRGLMRDSRI-------LILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 234 VEKGRTEDL------------LKAPQHPYTKKLLSSLPFRGRPRQIDLtsvPMISARDIivdyAGRKslFRKnkpkralh 301
Cdd:PRK15439 219 ALSGKTADLstddiiqaitpaAREKSLSASQKLWLELPGNRRQQAAGA---PVLTVEDL----TGEG--FRN-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 302 gVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVF--QDPYSS---LDPRMT- 375
Cdd:PRK15439 282 -ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYlpEDRQSSglyLDAPLAw 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 -IEALVEEalRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:PRK15439 361 nVCALTHN--RRGFWIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 455 RAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
6.32e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 6.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlaT--RALISLLPPTikvaDGSVSYKGRDVlk 78
Cdd:COG1121 1 MMMMPAIELENLT--VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKS--TllKAILGLLPPT----SGTVRLFGKPP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 mkenelrHLRGAEIGVVFQepMTSLNPSMTI--------GRQLEEGLILHTKAsaqERRSLILDMLKRVGIRD----PEG 146
Cdd:COG1121 71 -------RRARRRIGYVPQ--RAEVDWDFPItvrdvvlmGRYGRRGLFRRPSR---ADREAVDEALERVGLEDladrPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 147 ALSsyphefsGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIV 226
Cdd:COG1121 139 ELS-------GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVL 210
|
250
....*....|....*..
gi 1681691554 227 VMEKGAIVEkGRTEDLL 243
Cdd:COG1121 211 LLNRGLVAH-GPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-235 |
9.32e-38 |
|
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: 138.37 E-value: 9.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 17 ARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkenelrHLRGAEIGVVF 96
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT----SGEVLVDGEPV---------TGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEPmtSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:cd03293 80 QQD--ALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGL---SGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEK--GAIVE 235
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
297-502 |
9.73e-38 |
|
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: 138.12 E-value: 9.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVfqdPYSSLDPRMTi 376
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI---EAPGFYPNLT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 ealVEEALRPVPGLDGKaKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:cd03268 89 ---ARENLRLLARLLGI-RKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1681691554 457 QVLDLFSDLQKrYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03268 164 ELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
297-508 |
1.50e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 140.18 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE---NWTDYRLNCQMVFQDPYSSLDPR 373
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 mTIEALVEEALRPVpGLDGKAKRKRTLETLEEVGLGVD-YAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:PRK13637 100 -TIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 453 TVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
293-517 |
1.58e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.78 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSID-----IHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCqMVFQDpY 367
Cdd:PRK11432 10 KNITKRFGSNTVIDnlnltIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC-MVFQS-Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SsLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:PRK11432 88 A-LFPHMSLGENVGYGLK-MLGVPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 448 SALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGdrdtifdSPKEAYTR 517
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIG-------SPQELYRQ 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-242 |
1.83e-37 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 137.70 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 13 SLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRAL--ISLLPPTIKVaDGSVSYKGRDVLKMKENELRHLRga 90
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGAPD-EGEVLLDGKDIYDLDVDVLELRR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 EIGVVFQEPmtslNP-SMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIrDPEGALSSYPHEFSGGMRQRIMLASVM 169
Cdd:cd03260 82 RVGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL-WDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 170 LLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-235 |
3.28e-37 |
|
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: 137.10 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRGAEIGVVFQepMT 101
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT----SGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQ--FH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIgrqLEEGLI--LHTKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:TIGR02211 93 HLLPDFTA---LENVAMplLIGKKSVKEAKERAYEMLEKVGLEH---RINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVE 235
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
298-497 |
3.45e-37 |
|
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: 136.61 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrTENWTDYRL-----NCQMVFQDpySSLDP 372
Cdd:TIGR02673 16 AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGED-VNRLRGRQLpllrrRIGVVFQD--FRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 RMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:TIGR02673 93 DRTVYENVALPLE-VRGKKEREIQRRVGAALRQVGLE-HKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1681691554 453 TVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:TIGR02673 171 DLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-237 |
6.04e-37 |
|
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: 136.11 E-value: 6.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEnelrHLRGaeIGVVFQEP 99
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD----SGEILIDGRDVTGVPP----ERRN--IGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMTIGRQLEEGLILHTKASAQERRSlILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03259 82 --ALFPHLTVAENIAFGLKLRGVPKAEIRAR-VRELLELVGLEGLLNR---YPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-233 |
7.53e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 7.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaEIG 93
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT----SGEIYLDGKPLSAMPPPEWRR----QVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQEPmtSLnPSMTIGRQLEEGLILHTKASAQERrslILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKP 173
Cdd:COG4619 78 YVPQEP--AL-WGGTVRDNLPFPFQLRERKFDRER---ALELLERLGL--PPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
291-502 |
1.60e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.00 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPY-- 367
Cdd:COG1132 347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDiRDLTLESLRRQIGVVPQDTFlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 -SSL-------DPRMTiEALVEEALRpvpgldgKAKRKRTLETLEEvglGVD-YAGRYPHELSGGQRQRVAIARAIARRP 438
Cdd:COG1132 427 sGTIrenirygRPDAT-DEEVEEAAK-------AAQAHEFIEALPD---GYDtVVGERGVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 439 RFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEG 502
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-231 |
5.90e-36 |
|
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: 131.75 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaeIGVVFQEP 99
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD----SGEIKVLGKDIKKEPEEVKRR-----IGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMTigrqleeglilhtkasaqerrslILDMLKrvgirdpegalssypheFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03230 83 --SLYENLT-----------------------VRENLK-----------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 180 EPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:cd03230 121 EPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-250 |
9.98e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.77 E-value: 9.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMdKLLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMK 80
Cdd:COG3842 1 MAM-PALELENVS--KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD----SGRILLDGRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 81 ENElrhlRGaeIGVVFQEPmtSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMR 160
Cdd:COG3842 74 PEK----RN--VGMVFQDY--ALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGL---EGLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 161 QRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHD----LPMvarytS-RIVVMEKGAIVE 235
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLAL-----AdRIAVMNDGRIEQ 216
|
250
....*....|....*
gi 1681691554 236 KGRTEDLLKAPQHPY 250
Cdd:COG3842 217 VGTPEEIYERPATRF 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
299-507 |
1.05e-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: 132.94 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNWTDY---RLNCQMVFQDPysSLDPRMT 375
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPHeraRAGIGYVPEGR--RIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 iealVEEALRPVPGLDGKAKRKRTLE-------TLEEVglgvdyAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:cd03224 92 ----VEENLLLGAYARRRAKRKARLErvyelfpRLKER------RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 449 ALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
297-520 |
1.32e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenwtdyrlncqmvfQDPYS-------- 368
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--------------PEDRRrigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 -SLDPRMTI-EALVEEA-LRpvpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:COG4152 80 rGLYPKMKVgEQLVYLArLK---GLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 446 PVSALD-VTVraqvlDLFSDL---QKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIfdspKEAYTRRLL 520
Cdd:COG4152 156 PFSGLDpVNV-----ELLKDVireLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI----RRQFGRNTL 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
297-498 |
1.84e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.26 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlncqMVFQDpySSLDPRMTI 376
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR----LMFQD--ARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVeeALrpvpGLDGKAkRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:PRK11247 99 IDNV--GL----GLKGQW-RDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1681691554 457 QVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:PRK11247 171 EMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
299-523 |
2.31e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 136.50 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENwTDYRLNCQMVFQDpySSLDPRMTIEA 378
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRPINMMFQS--YALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRPvpglDGKAK---RKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR 455
Cdd:PRK11607 111 NIAFGLKQ----DKLPKaeiASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 456 AQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAI 523
Cdd:PRK11607 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
303-511 |
3.15e-35 |
|
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: 135.24 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRprteNWTDYRLNCQM---------VFQDpySSLDPR 373
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR----TLFDSRKGIFLppekrrigyVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEALVEEALRPVpglDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:TIGR02142 90 LSVRGNLRYGMKRA---RPSERRISFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 454 VRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
288-491 |
1.04e-34 |
|
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: 129.66 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-----ENWTDYRLNCQMV 362
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPplnskKASKFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 363 FQDpYSSLDpRMTIEALVEEALRPVPgLDGKAKRKRTLETLEEVGLGVDYAgRYPHELSGGQRQRVAIARAIARRPRFLI 442
Cdd:TIGR03608 82 FQN-FALIE-NETVEENLDLGLKYKK-LSKKEKREKKKEALEKVGLNLKLK-QKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1681691554 443 ADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQvADRVV 491
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRVI 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-280 |
1.20e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 134.78 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLE--VARTGQQV-VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHL 87
Cdd:PRK10070 28 GLSKEqiLEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT----RGQVLIDGVDIAKISDAELREV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 88 RGAEIGVVFQEpmTSLNPSMTIGRQLEEGLILhTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLAS 167
Cdd:PRK10070 104 RRKKIAMVFQS--FALMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
250 260 270
....*....|....*....|....*....|...
gi 1681691554 248 HPYTKKLlsslpFRGrprqIDLTSVpmISARDI 280
Cdd:PRK10070 258 NDYVRTF-----FRG----VDISQV--FSAKDI 279
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-521 |
1.55e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.93 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRT-------IAGlvTESEGRIQFQG 345
Cdd:COG1117 10 PKIEVRNLNVYYGD----------KQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPG--ARVEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 346 RP---RTENWTDYRLNCQMVFQDP----------------YSSLDPRMTIEALVEEALRPVpGLDGKAKRKrtletLEEV 406
Cdd:COG1117 78 EDiydPDVDVVELRRRVGMVFQKPnpfpksiydnvayglrLHGIKSKSELDEIVEESLRKA-ALWDEVKDR-----LKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 407 GLGvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLgvvEQ- 485
Cdd:COG1117 152 ALG----------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNM---QQa 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 1681691554 486 --VADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLS 521
Cdd:COG1117 217 arVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-242 |
1.67e-34 |
|
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: 130.38 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLeVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRH 86
Cdd:cd03256 1 IEVENLSK-TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT----SGSVLIDGTDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRgAEIGVVFQEP------------MTSLNPSMTIGRQLeegLILHTKASAQERRSLildmLKRVGIRDPEGALSSyphE 154
Cdd:cd03256 76 LR-RQIGMIFQQFnlierlsvlenvLSGRLGRRSTWRSL---FGLFPKEEKQRALAA----LERVGLLDKAYQRAD---Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 155 FSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV 234
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
....*...
gi 1681691554 235 EKGRTEDL 242
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-267 |
1.89e-34 |
|
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: 130.11 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaEIGVVFQEp 99
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT----SGEIFIDGEDIREQDPVELRR----KIGYVIQQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLeeGLILH-TKASAQERRSLILDMLKRVGIrDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIA 178
Cdd:cd03295 84 -IGLFPHMTVEENI--ALVPKlLKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 179 DEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKllssl 258
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE----- 234
|
....*....
gi 1681691554 259 pFRGRPRQI 267
Cdd:cd03295 235 -FVGADRLL 242
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
264-503 |
2.51e-34 |
|
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: 136.43 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 264 PRQIDLTSVPMISARDIIVDYAGRkslfrknkPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF 343
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGA--------GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 344 QGRP-RTENWTDYRLNCQMVFQDPY---SSL-------DPRMTIEALVEeALRPVpGLDGkakrkrTLETLEEvGLG--V 410
Cdd:COG4987 395 GGVDlRDLDEDDLRRRIAVVPQRPHlfdTTLrenlrlaRPDATDEELWA-ALERV-GLGD------WLAALPD-GLDtwL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 411 DYAGRyphELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVL-DLFSDLQKRygfSCLFISHDLGVVEQvADR 489
Cdd:COG4987 466 GEGGR---RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGR---TVLLITHRLAGLER-MDR 538
|
250
....*....|....
gi 1681691554 490 VVVMQDGRIIEEGD 503
Cdd:COG4987 539 ILVLEDGRIVEQGT 552
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
300-521 |
3.03e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.09 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT--------------ENWTDYRLNCQMVFQd 365
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTRLTMVFQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 pYSSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK10619 100 -HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLS 521
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
297-502 |
4.29e-34 |
|
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: 128.08 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGeVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPysSLDPRMTI 376
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEF--GVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:cd03264 90 REFLDYIAW-LKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1681691554 457 QVLDLFSDLQKryGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03264 168 RFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
299-498 |
5.70e-34 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 131.89 E-value: 5.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQDpYSsLDPRMTIEA 378
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR-DIAMVFQN-YA-LYPHMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:PRK11650 96 NMAYGLK-IRGMPKAEIEERVAEAARILELE-PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1681691554 459 LDLFSDLQKRYGFSCLFISHDlgvveQV-----ADRVVVMQDGRI 498
Cdd:PRK11650 174 RLEIQRLHRRLKTTSLYVTHD-----QVeamtlADRVVVMNGGVA 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-515 |
7.90e-34 |
|
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: 128.18 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNW 352
Cdd:COG0410 2 PMLEVENLHAGYGGI----------HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-GL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLnCQM----------VFqdpyssldPRMTiealVEEALR-PVPGLDGKAKRKRTLET-------LEEvglgvdYAG 414
Cdd:COG0410 71 PPHRI-ARLgigyvpegrrIF--------PSLT----VEENLLlGAYARRDRAEVRADLERvyelfprLKE------RRR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 415 RYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQ 494
Cdd:COG0410 132 QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLE 210
|
250 260
....*....|....*....|...
gi 1681691554 495 DGRIIEEGDRDTIFDSP--KEAY 515
Cdd:COG0410 211 RGRIVLEGTAAELLADPevREAY 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-244 |
7.97e-34 |
|
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: 128.44 E-value: 7.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmKENELRhlrgAEIGVVFQEPMt 101
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD----SGSILIDGEDVRK-EPREAR----RQIGVLPDERG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 sLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIRDPegaLSSYPHEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:COG4555 85 -LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEF---LDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 182 TTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:COG4555 160 TNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
299-498 |
1.45e-33 |
|
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: 126.75 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----RTENWTDYRLNCQMVFQDpySSLDPRM 374
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlRGRAIPYLRRKIGVVFQD--FRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:cd03292 94 NVYENVAFALE-VTGVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1681691554 455 RAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:cd03292 172 TWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
298-502 |
1.86e-33 |
|
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: 126.72 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPysSLDPRMT-I 376
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL--SVDDELTgW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEAlrPVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:cd03265 92 ENLYIHA--RLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1681691554 457 QVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-233 |
1.89e-33 |
|
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: 126.49 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMkenelrhlrGAEIG 93
Cdd:cd03235 5 LTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT----SGSIRVFGKPLEKE---------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQEpmTSLNPSMTI--------GRQLEEGLILHTKasaQERRSLILDMLKRVGIRDpegaLSSYP-HEFSGGMRQRIM 164
Cdd:cd03235 72 YVPQR--RSIDRDFPIsvrdvvlmGLYGHKGLFRRLS---KADKAKVDEALERVGLSE----LADRQiGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-237 |
2.32e-33 |
|
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: 125.24 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVLKMKENELRHLrgaeIG 93
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP----SSGEILLDGKDLASLSPKELARK----IA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQepmtslnpsmtigrqleeglilhtkasaqerrslildMLKRVGIRDpegaLSSYP-HEFSGGMRQRIMLASVMLLK 172
Cdd:cd03214 77 YVPQ-------------------------------------ALELLGLAH----LADRPfNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-233 |
4.83e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 125.33 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENeLRHLRgAEIGVVFQEp 99
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD----SGTIIIDGLKLTDDKKN-INELR-QKVGMVFQQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEgalSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03262 85 -FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKA---DAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-183 |
5.78e-33 |
|
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: 123.14 E-value: 5.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKenelRHLRGAEIGVVFQEPmtSL 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT----EGTILLDGQDLTDDE----RKSLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTIGRQLEEGLILH--TKASAQERRSLILDMLKRVGIRDPegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKglSKREKDARAEEALEKLGLGDLADR--PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 1681691554 182 TT 183
Cdd:pfam00005 149 TA 150
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
274-499 |
6.02e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 126.74 E-value: 6.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIivdyagRKSlFRKNKP--KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeN 351
Cdd:COG1101 1 MLELKNL------SKT-FNPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 352 WTDYRLNCQM--VFQDPYSSLDPRMTIE---ALveeALR------PVPGLDgKAKRKRTLETLEEVGLGV-----DYAGr 415
Cdd:COG1101 73 LPEYKRAKYIgrVFQDPMMGTAPSMTIEenlAL---AYRrgkrrgLRRGLT-KKRRELFRELLATLGLGLenrldTKVG- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 416 yphELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLgvvEQ---VADRVVV 492
Cdd:COG1101 148 ---LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM---EQaldYGNRLIM 221
|
....*..
gi 1681691554 493 MQDGRII 499
Cdd:COG1101 222 MHEGRII 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-231 |
7.24e-33 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 123.84 E-value: 7.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRgaEIGVVFQEP 99
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD----SGSILIDGEDLTDLEDELPPLRR--RIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMTIGRQLEEGLilhtkasaqerrslildmlkrvgirdpegalssyphefSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03229 86 --ALFPHLTVLENIALGL--------------------------------------SGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
300-496 |
1.10e-32 |
|
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: 124.89 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDyRLncqMVFQDpYSSLdPRMTIEAL 379
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-RM---VVFQN-YSLL-PWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 VEEALRPV-PGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:TIGR01184 75 IALAVDRVlPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1681691554 459 LDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDG 496
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
297-518 |
1.38e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 126.48 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR---PRT--ENWTDYRLNCQMVFQDPYSSLD 371
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitPETgnKNLKKLRKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMTIEAlVEEALRPVPGLDGKAKRKrTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:PRK13641 100 ENTVLKD-VEFGPKNFGFSEDEAKEK-ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 452 VTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEgdrdtifDSPKEAYTRR 518
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKH-------ASPKEIFSDK 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
300-493 |
1.52e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.75 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTE---SEGRIQFQGRPRTENWTDYRlNCQMVFQDPYssLDPRMTI 376
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR-RIGILFQDDL--LFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRPvpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:COG4136 94 GENLAFALPP--TIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1681691554 457 QVLDL-FSDLQKRyGFSCLFISHDLGVVEQvADRVVVM 493
Cdd:COG4136 171 QFREFvFEQIRQR-GIPALLVTHDEEDAPA-AGRVLDL 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
297-513 |
1.55e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.29 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF-----QGRPRTENWTDYRLNCQMVFQDPYSSLd 371
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgerviTAGKKNKKLKPLRKKVGIVFQFPEHQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 prmtIEALVEE--ALRP----VPGLDGKAKRKrtlETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK13634 99 ----FEETVEKdiCFGPmnfgVSEEDAKQKAR---EMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKE 513
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
304-507 |
2.87e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 123.92 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 304 SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQDpySSLDPRMTIEALVeeA 383
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-PVSMLFQE--NNLFSHLTVAQNI--G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 384 LRPVPGLDGKAKRKRTLETL-EEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLF 462
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIaRQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1681691554 463 SDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
304-502 |
3.24e-32 |
|
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: 122.99 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 304 SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlNCQMVFQDpySSLDPRMTIEALVeeA 383
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-PVSMLFQE--NNLFAHLTVEQNV--G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 384 LRPVPGLDGKA-KRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLF 462
Cdd:cd03298 93 LGLSPGLKLTAeDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1681691554 463 SDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
274-512 |
4.51e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.42 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYagrkslfrkNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP---RTE 350
Cdd:PRK13639 1 ILETRDLKYSY---------PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikyDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 351 NWTDYRLNCQMVFQDPYSSL-DPRmtiealVEE--ALRPVP-GLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQ 426
Cdd:PRK13639 72 SLLEVRKTVGIVFQNPDDQLfAPT------VEEdvAFGPLNlGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 427 RVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDT 506
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
....*.
gi 1681691554 507 IFDSPK 512
Cdd:PRK13639 224 VFSDIE 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
270-513 |
5.38e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.33 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 270 TSVPMISARDIIVDYAGRKSLfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT 349
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENN--------ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 -ENWTDYRLNCQMVFQDPYSSLdprmtIEALVEE--ALrpvpGLDGK----AKRKRTLETL-EEVGLGvDYAGRYPHELS 421
Cdd:PRK13632 75 kENLKEIRKKIGIIFQNPDNQF-----IGATVEDdiAF----GLENKkvppKKMKDIIDDLaKKVGME-DYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 422 GGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEE 501
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQ 223
|
250
....*....|..
gi 1681691554 502 GDRDTIFDSPKE 513
Cdd:PRK13632 224 GKPKEILNNKEI 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-250 |
5.92e-32 |
|
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: 130.72 E-value: 5.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDvlkMKENELRHLRGAeIGVVFQEP 99
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT----SGRILIDGID---LRQIDPASLRRQ-IGVVLQDV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSlnpSMTIgrqlEEGLILHTKASAQERrslILDMLKRVGIRD-----PEG---ALSSYPHEFSGGMRQRIMLASVMLL 171
Cdd:COG2274 559 FLF---SGTI----RENITLGDPDATDEE---IIEAARLAGLHDfiealPMGydtVVGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELTRaeGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDLLKAPQHPY 250
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-247 |
8.74e-32 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 122.55 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRgaeIGVVFQepMTS 102
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT----SGSVLFDGEDITGLPPHEIARLG---IGRTFQ--IPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSMT------IGRQLEEGLILHTKASAQERRSL---ILDMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKP 173
Cdd:cd03219 86 LFPELTvlenvmVAAQARTGSGLLLARARREEREArerAEELLERVGLADLADRPAG---ELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
274-526 |
1.07e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 123.37 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-ENW 352
Cdd:PRK13652 3 LIETRDLCYSYSGSK---------EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLNCQMVFQDPYSSL-DPrmTIEALVeeALRPVP-GLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAI 430
Cdd:PRK13652 74 REVRKFVGLVFQNPDDQIfSP--TVEQDI--AFGPINlGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 431 ARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
250
....*....|....*..
gi 1681691554 511 PKEAYTRRL-LSAIPAL 526
Cdd:PRK13652 229 PDLLARVHLdLPSLPKL 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
291-498 |
1.75e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.92 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDPyss 369
Cdd:PRK13650 14 YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEeNVWDIRHKIGMVFQNP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 lDPRM---TIEALVEEALRPvPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:PRK13650 91 -DNQFvgaTVEDDVAFGLEN-KGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 447 VSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLgvvEQVA--DRVVVMQDGRI 498
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL---DEVAlsDRVLVMKNGQV 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
299-521 |
2.01e-31 |
|
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: 121.48 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNC--------QMVFqdpyssl 370
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgiayvpqgREIF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 dPRMTiealVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:TIGR03410 88 -PRLT----VEENLLTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 451 DVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIfdspKEAYTRRLLS 521
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
298-509 |
2.14e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.54 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR---PRTENWTdyRLNCQMVFQDPYSSLDPrM 374
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnAENEKWV--RSKVGLVFQDPDDQVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVeeALRPVP-GLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:PRK13647 96 TVWDDV--AFGPVNmGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 454 VRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-505 |
2.38e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.49 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKgrdvlkmkenelrhlRGAEIG 93
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD----SGEVSIP---------------KGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQEP------------MTSLNPSMTIGRQLEE--------GLILHTKASAQER---------RSLILDMLKRVGI--R 142
Cdd:COG0488 65 YLPQEPpldddltvldtvLDGDAELRALEAELEEleaklaepDEDLERLAELQEEfealggweaEARAEEILSGLGFpeE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 143 DPEGALSsyphEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAViqrdvmelMVE-----LTRAEGTaILLISHDlpm 217
Cdd:COG0488 145 DLDRPVS----ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleefLKNYPGT-VLVVSHD--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 218 vaRY-----TSRIVVMEKGAIV---------EKGRTEDL-----------------------LKAPQHPYTK-----KLL 255
Cdd:COG0488 209 --RYfldrvATRILELDRGKLTlypgnysayLEQRAERLeqeaaayakqqkkiakeeefirrFRAKARKAKQaqsriKAL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 256 SSL-----PFRGRPRQIDLTSVP-----MISARDIIVDYAGRKsLFRknkpkralhGVSIDIHEGEVVALVGGSGSGKTT 325
Cdd:COG0488 287 EKLereepPRRDKTVEIRFPPPErlgkkVLELEGLSKSYGDKT-LLD---------DLSLRIDRGDRIGLIGPNGAGKST 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 326 LGRTIAGLVTESEGRIQFqGRprtenwtdyrlNCQMVF--QDpYSSLDPRMT-IEALVEEAlrpvpglDGKAKRK-RTLe 401
Cdd:COG0488 357 LLKLLAGELEPDSGTVKL-GE-----------TVKIGYfdQH-QEELDPDKTvLDELRDGA-------PGGTEQEvRGY- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 402 tLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDlqkrYGFSCLFISHDLG 481
Cdd:COG0488 416 -LGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD----FPGTVLLVSHDRY 490
|
570 580
....*....|....*....|....*
gi 1681691554 482 VVEQVADRVVVMQDGRIIE-EGDRD 505
Cdd:COG0488 491 FLDRVATRILEFEDGGVREyPGGYD 515
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-255 |
3.81e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDV---LKMKEnelRHlrgaeIGVVFQE 98
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD----SGRIVLNGRDLftnLPPRE---RR-----VGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PMtsLNPSMTIGRQLEEGLiLHTKASAQERRSLILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPALLIA 178
Cdd:COG1118 84 YA--LFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 179 DEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLL 255
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
291-513 |
4.07e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.12 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG-RPRTENWTDYRLNCQMVFQDPYSS 369
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGeLLTAENVWNLRRKIGMVFQNPDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 LdprmtIEALVEEALrpVPGLDGKA-KRKRTLETLEEVGLGV---DYAGRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK13642 94 F-----VGATVEDDV--AFGMENQGiPREEMIKRVDEALLAVnmlDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDSPKE 513
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
298-503 |
4.09e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.50 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF-------QGRPRTENWTDYRLNCQ---------- 360
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEKEKVLEKLVIQktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 361 --------MVFQDPYSSLdprmtIEALVEE--ALRPVP-GLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVA 429
Cdd:PRK13651 101 keirrrvgVVFQFAEYQL-----FEQTIEKdiIFGPVSmGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGD 503
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-245 |
4.14e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.42 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENEL- 84
Cdd:PRK13548 2 MLEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD----SGEVRLNGRPLADWSPAELa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 85 RHLrgaeiGVVFQEpmTSLNPSMTIgrqlEE----GLILHTkASAQERRSLILDMLKRVGIRDPEGalSSYPhEFSGGMR 160
Cdd:PRK13548 76 RRR-----AVLPQH--SSLSFPFTV----EEvvamGRAPHG-LSRAEDDALVAAALAQVDLAHLAG--RDYP-QLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 161 QRIMLASVML------LKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV 234
Cdd:PRK13548 141 QRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
250
....*....|.
gi 1681691554 235 EKGRTEDLLKA 245
Cdd:PRK13548 221 ADGTPAEVLTP 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-244 |
4.20e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.20 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVL-KMKENELRHLRgAEIGVVFQEPM 100
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT----TGTVTVDDITIThKTKDKYIRPVR-KRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 TSLNPSmTIGRQLEEGlILHTKASAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:PRK13646 96 SQLFED-TVEREIIFG-PKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 181 PTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
304-523 |
4.45e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.76 E-value: 4.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 304 SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR-----PRTENWTDYRLNCQMVFQDpySSLDPRMTIEA 378
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakiSDAELREVRRKKIAMVFQS--FALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:PRK10070 126 NTAFGME-LAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 459 LDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAI 523
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-242 |
4.81e-31 |
|
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: 120.17 E-value: 4.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmkenELRHLRgAEIGVVFQEPmtSL 103
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT----SGRATVAGHDVVR----EPREVR-RRIGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTiGRqleEGLILHTK---ASAQERRSLILDMLKRVGIRDPEGALSSYpheFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:cd03265 85 DDELT-GW---ENLYIHARlygVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 181 PTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
298-505 |
8.09e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.52 E-value: 8.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-ENWTD-YRLNCQMVFQDPysSLDPRMT 375
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDaIALGIGMVHQHF--MLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 iealVEE----ALRPVPG--LDGKAKRKRTLETLEEVGLGVDyAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:COG3845 97 ----VAEnivlGLEPTKGgrLDRKAARARIRELSERYGLDVD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 450 LdvtVRAQVLDLFSDLQ--KRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRD 505
Cdd:COG3845 172 L---TPQEADELFEILRrlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
274-502 |
8.50e-31 |
|
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: 119.39 E-value: 8.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIivdyagRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:cd03266 1 MITADAL------TKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQMVFQDpySSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARA 433
Cdd:cd03266 75 EARRRLGFVSDS--TGLYDRLTARENLEYFAG-LYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDlFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALRE-FIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
295-502 |
1.05e-30 |
|
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: 118.92 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 295 KPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDyrlncQMVFQDPYSSLDPRM 374
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-----RIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TI-EALVEEA-LRpvpGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:cd03269 86 KViDQLVYLAqLK---GLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 453 TVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03269 162 VNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-256 |
1.09e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 119.85 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVadGSVSYKGRDVLKMKENELRHLRgAEIGVVF 96
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPeagTIRV--GDITIDTARSLSQQKGLIRQLR-QHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEpmTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:PRK11264 92 QN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLLS 256
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
293-502 |
1.34e-30 |
|
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: 118.76 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDpySSLDP 372
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQF--DALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 RMTiealVEEALR---PVPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:cd03263 89 ELT----VREHLRfyaRLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 450 LDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03263 164 LDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-257 |
1.36e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 122.22 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRaLISLL-PPTIkvadGSVSYKGRDVLKMKENELRHLRgAEIGVVFQEpmTS 102
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIR-CINLLeRPTS----GRVLVDGQDLTALSEKELRKAR-RQIGMIFQH--FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSMT----IGRQLE-EGLilhtkaSAQERRSLILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK11153 93 LLSSRTvfdnVALPLElAGT------PKAEIKARVTELLELVGLSDKADR---YPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLLSS 257
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
299-497 |
1.40e-30 |
|
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: 119.08 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQgrpRTENWTDyrlncqMVFQDPYSSLD------- 371
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR---HDGGWVD------LAQASPREILAlrrrtig 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 ---------PRMTIEALVEEALRPVpGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLI 442
Cdd:COG4778 97 yvsqflrviPRVSALDVVAEPLLER-GVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 443 ADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
274-500 |
1.87e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 119.42 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:PRK11248 1 MLQISHLYADYGG----------KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYrlncQMVFQDpySSLDPRMTIEALVEEALRpVPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARA 433
Cdd:PRK11248 71 ER----GVVFQN--EGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQ--DGRIIE 500
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-247 |
2.30e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 118.99 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEN 82
Cdd:COG0411 1 SDPLLEVRGLTKRFG--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT----SGRILFDGRDITGLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 ELRHLrgaeiGVV--FQepMTSLNPSMT------IGRQLEEG-----LILHTKASAQERRSLI---LDMLKRVGIRDPEG 146
Cdd:COG0411 75 RIARL-----GIArtFQ--NPRLFPELTvlenvlVAAHARLGrgllaALLRLPRARREEREAReraEELLERVGLADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 147 ALSSyphEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIV 226
Cdd:COG0411 148 EPAG---NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
250 260
....*....|....*....|.
gi 1681691554 227 VMEKGAIVEKGRTEDLLKAPQ 247
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRADPR 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-501 |
2.33e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 124.51 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkeNELRHLRGAE--IGVVFQ 97
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT----KGTITINNINY-----NKLDHKLAAQlgIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMT----SLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGI-RDPEGALSsyphEFSGGMRQRIMLASVMLLK 172
Cdd:PRK09700 88 ELSVidelTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLkVDLDEKVA----NLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 173 PALLIADEPTTALDAViQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLlkapqhpyTK 252
Cdd:PRK09700 164 AKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV--------SN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 253 KLLSSLpFRGRprqiDLTSvpMISARDIIVDYAGRKSLFR-KN---KPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGR 328
Cdd:PRK09700 235 DDIVRL-MVGR----ELQN--RFNAMKENVSNLAHETVFEvRNvtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 329 TIAGLVTESEGRIQFQGR---PR-------------TENWTDyrlncQMVFqdPYSSLDPRMTI-EALVEEALRPVPGLD 391
Cdd:PRK09700 308 CLFGVDKRAGGEIRLNGKdisPRspldavkkgmayiTESRRD-----NGFF--PNFSIAQNMAIsRSLKDGGYKGAMGLF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 392 GKAKRKRTLETLEE-VGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyG 470
Cdd:PRK09700 381 HEVDEQRTAENQRElLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-G 459
|
490 500 510
....*....|....*....|....*....|.
gi 1681691554 471 FSCLFISHDLGVVEQVADRVVVMQDGRIIEE 501
Cdd:PRK09700 460 KVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-231 |
2.65e-30 |
|
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: 115.80 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaEIGVVFQep 99
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT----SGEILIDGKDIAKLPLEELRR----RIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtslnpsmtigrqleeglilhtkasaqerrslildmlkrvgirdpegalssypheFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 180 EPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:cd00267 106 EPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
299-513 |
3.75e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.09 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-ENWTDYRLNCQMVFQDPYSSL------- 370
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVFQNPDNQFvgsivky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 DPRMTIEALV---EEALRPVPgldgkakrkrtlETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:PRK13648 104 DVAFGLENHAvpyDEMHRRVS------------EALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 448 SALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLgvVEQV-ADRVVVMQDGRIIEEGDRDTIFDSPKE 513
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDL--SEAMeADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
300-501 |
5.86e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.61 E-value: 5.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----RTENWTDYRlNCQMVFQDPYSSLDPRMT 375
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsklSSAAKAELR-NQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 ieALVEEALrpvPGLDGKAKRK----RTLETLEEVGLGVDYAGRyPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:PRK11629 104 --ALENVAM---PLLIGKKKPAeinsRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 452 VTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEE 501
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
304-503 |
7.66e-30 |
|
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: 116.50 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 304 SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENwTDYRLNCQMVFQDpySSLDPRMTIEALVEEA 383
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-APYQRPVSMLFQE--NNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 384 LRPvpGLDGKAKRKRTLETL-EEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLF 462
Cdd:TIGR01277 95 LHP--GLKLNAEQQEKVVDAaQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1681691554 463 SDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGD 503
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-255 |
1.49e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLpptiKVADGSVSYKGRDVLKMKENElRHLRgAEIGVVFQEpmT 101
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE----EITSGDLIVDGLKVNDPKVDE-RLIR-QEAGMVFQQ--F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PRK09493 87 YLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 182 TTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLL 255
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
299-508 |
1.50e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 117.64 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP---RTENWTDYRLNCQMVFQDPYSSLdprmt 375
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidySRKGLMKLRESVGMVFQDPDNQL----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALVEEALRPVP---GLDGKAKRKRTLETLEEVGlgVDYAGRYP-HELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:PRK13636 96 FSASVYQDVSFGAvnlKLPEDEVRKRVDNALKRTG--IEHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 452 VTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-256 |
2.01e-29 |
|
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: 122.18 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtrALIS-LLPPTikvaDGSVSYKGRDVLKMKENEL 84
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKsTLL--ALLLrFLDPQ----SGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 85 RHLrgaeIGVVFQEP---MTSLNPSMTIGRQleeglilhtKASAQErrslILDMLKRVGIRD-----PEGaLSSYPHE-- 154
Cdd:COG4987 408 RRR----IAVVPQRPhlfDTTLRENLRLARP---------DATDEE----LWAALERVGLGDwlaalPDG-LDTWLGEgg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 155 --FSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMveLTRAEGTAILLISHDLPMVARYTsRIVVMEKGA 232
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERMD-RILVLEDGR 546
|
250 260
....*....|....*....|....
gi 1681691554 233 IVEKGRTEDLLKapQHPYTKKLLS 256
Cdd:COG4987 547 IVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-253 |
2.18e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 116.69 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRAL---ISLLPPTIKVaDGSVSYKGRDVLKMKENELRHlrgaEIGVVFQ 97
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKIKV-DGKVLYFGKDIFQIDAIKLRK----EVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPmtSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGI-RDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:PRK14246 98 QP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAegTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKK 253
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
297-498 |
2.87e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 115.36 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG----RPRTENWTDYRLNCQMVFQDPYSSLDp 372
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditRLKNREVPFLRRQIGMIFQDHHLLMD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 rmtiEALVEEALRP--VPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:PRK10908 94 ----RTVYDNVAIPliIAGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 451 DVTVRAQVLDLFSDLQkRYGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:PRK10908 169 DDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
277-523 |
3.10e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 117.03 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 277 ARDIIVDYAGRKslFRKNKPK--RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF------QGRPR 348
Cdd:PRK13645 4 SKDIILDNVSYT--YAKKTPFefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 349 TENWTDYRLNCQMVFQDPYSSLDpRMTIEALVeeALRPVP-GLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQR 427
Cdd:PRK13645 82 IKEVKRLRKEIGLVFQFPEYQLF-QETIEKDI--AFGPVNlGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 428 VAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGdrdti 507
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG----- 233
|
250
....*....|....*..
gi 1681691554 508 fdSPKEAYT-RRLLSAI 523
Cdd:PRK13645 234 --SPFEIFSnQELLTKI 248
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-245 |
3.52e-29 |
|
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: 121.40 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEP 99
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY----SGSILINGVDLSDLDPASWRRQ----IAWVPQNP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTslnPSMTIGRQLeegLILHTKASAQErrslILDMLKRVGIRD-----PEGaLSSYPHE----FSGGMRQRIMLASVML 170
Cdd:COG4988 421 YL---FAGTIRENL---RLGRPDASDEE----LEAALEAAGLDEfvaalPDG-LDTPLGEggrgLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 171 LKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYtSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAK 561
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-214 |
3.68e-29 |
|
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: 114.11 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkeNELR 85
Cdd:COG4133 2 MLEAENLS--CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS----AGEVLWNGEPI-----RDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 86 HLRGAEIGVVFQEPMtsLNPSMTigrqLEEGLILHTKASAQER-RSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIM 164
Cdd:COG4133 71 EDYRRRLAYLGHADG--LKPELT----VRENLRFWAALYGLRAdREAIDEALEAVGL---AGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHD 214
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-231 |
3.99e-29 |
|
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: 112.86 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 19 TGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLrgaeIGVVFQE 98
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT----SGEILIDGVDLRDLDLESLRKN----IAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PMtsLnPSMTIgrqleeglilhtkasaqerRSLILdmlkrvgirdpegalssyphefSGGMRQRIMLASVMLLKPALLIA 178
Cdd:cd03228 85 PF--L-FSGTI-------------------RENIL----------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 179 DEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYTsRIVVMEKG 231
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDAD-RIIVLDDG 170
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
293-511 |
4.66e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.44 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLV---TESEGRIQFQGRPRTEN--WtDYRLNCQMVFQDPY 367
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKtvW-DIREKVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SSLdprmtIEALVEEAL------RPVPgldgKAKRKRTL-ETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRF 440
Cdd:PRK13640 95 NQF-----VGATVGDDVafglenRAVP----RPEMIKIVrDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
294-503 |
6.50e-29 |
|
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: 114.64 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 294 NKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPYSSLD- 371
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvRDYTLASLRRQIGLVSQDVFLFNDt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 ---------PRMTIEAlVEEAlrpvpgldgkAKRKRTLETLEEVGLGVD-YAGRYPHELSGGQRQRVAIARAIARRPRFL 441
Cdd:cd03251 92 vaeniaygrPGATREE-VEEA----------ARAANAHEFIMELPEGYDtVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGD 503
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-255 |
7.30e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 28 SFDL--APGEIFGIVGESGSGK-TLAtrALIS-LLPPtikvADGSVSYKGRDVLkmkenelrHLRGAE--IGVVFQEpmT 101
Cdd:COG3840 17 RFDLtiAAGERVAILGPSGAGKsTLL--NLIAgFLPP----DSGRILWNGQDLT--------ALPPAErpVSMLFQE--N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLeeGLILH--TKASAQERRSLIlDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:COG3840 81 NLFPHLTVAQNI--GLGLRpgLKLTAEQRAQVE-QALERVGL---AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLL 255
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-231 |
9.94e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.14 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLRGAEIGVVFQepMTS 102
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT----SGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSMTIGRQLEEGLILHTKASAQERRSlILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPT 182
Cdd:PRK11629 98 LLPDFTALENVAMPLLIGKKKPAEINSR-ALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1681691554 183 TALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKG 231
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR-MSRQLEMRDG 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-245 |
1.19e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.88 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTlaTraLISLLPPTIKVADGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEP 99
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKS--T--LVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ----IGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 M---TSL--NpsMTIGRQleeglilhtKASAQErrslILDMLKRVGIRD-----PEGalssYPHE-------FSGGMRQR 162
Cdd:COG1132 424 FlfsGTIreN--IRYGRP---------DATDEE----VEEAAKAAQAHEfiealPDG----YDTVvgergvnLSGGQRQR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRaeGTAILLISHDLPMVARYtSRIVVMEKGAIVEKGRTEDL 242
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEEL 561
|
...
gi 1681691554 243 LKA 245
Cdd:COG1132 562 LAR 564
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
300-502 |
1.38e-28 |
|
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: 120.43 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNC-QMVFQDPY----------S 368
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSvAMVDQDIFlfegtvrdnlT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 SLDPRMTIEALVEeALRPVPGLDGKAKRKRTLET-LEEVGlgvdyagrypHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:TIGR03796 575 LWDPTIPDADLVR-ACKDAAIHDVITSRPGGYDAeLAEGG----------ANLSGGQRQRLEIARALVRNPSILILDEAT 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 448 SALDVTVRAQVLDLFsdlqKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEG 502
Cdd:TIGR03796 644 SALDPETEKIIDDNL----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
24-242 |
1.45e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 115.57 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmkenELRHLRgAEIGVVFQEPmtsl 103
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT----SGTARVAGYDVVR----EPRKVR-RSIGIVPQYA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 npSMTIGRQLEEGLILHTK---ASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:TIGR01188 76 --SVDEDLTGRENLEMMGRlygLPKDEAEERAEELLELFELGE---AADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 181 PTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-247 |
1.83e-28 |
|
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: 113.20 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMK-ENElrhlrgaEIGVVFQEpmT 101
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD----SGKILLNGKDITNLPpEKR-------DISYVPQN--Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLEEGLIlHTKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:cd03299 81 ALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 182 TTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
273-516 |
2.26e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.33 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYagrkslfrkNKpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL------VTESeGRIQFQGR 346
Cdd:PRK14239 4 PILQVSDLSVYY---------NK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTIT-GSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 347 ----PRTENwTDYRLNCQMVFQDPysslDP-RMTIEALVEEALRpVPGLDGKAKRKRTLET-LEEVGLGVDYAGRYpHE- 419
Cdd:PRK14239 73 niysPRTDT-VDLRKEIGMVFQQP----NPfPMSIYENVVYGLR-LKGIKDKQVLDEAVEKsLKGASIWDEVKDRL-HDs 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 420 ---LSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQVADRVVVMQDG 496
Cdd:PRK14239 146 algLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|
gi 1681691554 497 RIIEEGDRDTIFDSPKEAYT 516
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-247 |
2.79e-28 |
|
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: 112.72 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENElRHlrgaeIGVVFQEp 99
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT----SGEILLDGKDITNLPPHK-RP-----VNTVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLILhTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03300 81 -YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQL---EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 180 EPTTALDAVIQRDV-MELMvELTRAEGTAILLISHD----LPMvaryTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:cd03300 156 EPLGALDLKLRKDMqLELK-RLQKELGITFVFVTHDqeeaLTM----SDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
297-498 |
2.96e-28 |
|
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: 110.98 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenwtdyrlncqmvfqdpYSSLDPRMTI 376
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP-------------------VTRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVeeALrpVPGlDgkakRKR-----TLETLEEVGLgvdyagryPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:cd03215 74 RAGI--AY--VPE-D----RKReglvlDLSVAENIAL--------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 452 VTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:cd03215 137 VGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
290-512 |
3.09e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.11 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 290 LFRKNKP--KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTD-----YRLNCQMV 362
Cdd:PRK13646 11 TYQKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpVRKRIGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 363 FQDPYSSLdprmtIEALVEEALRPVP---GLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPR 439
Cdd:PRK13646 91 FQFPESQL-----FEDTVEREIIFGPknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 440 FLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK 512
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
297-505 |
3.46e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 112.85 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL----VTEseGRIQFQGrprtENWTDY------RLNCQMVFQDP 366
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkyeVTS--GSILLDG----EDILELspderaRAGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 yssldPR---MTIEALVEEALRPVPG--LDGKAKRKRTLETLEEVGLGVDYAGRYPHE-LSGGQRQRVAIARAIARRPRF 440
Cdd:COG0396 87 -----VEipgVSVSNFLRTALNARRGeeLSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 441 LIADEPVSALDV-TVRAqVLDLFSDLQKRyGFSCLFISHDLGVVEQV-ADRVVVMQDGRIIEEGDRD 505
Cdd:COG0396 162 AILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-244 |
4.13e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.16 E-value: 4.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkMKENeLRHLRGaEIGVVFQEPm 100
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ----SGEIKIDGITI--SKEN-LKEIRK-KIGIIFQNP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 tslnPSMTIGRQLEE----GLiLHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:PRK13632 93 ----DNQFIGATVEDdiafGL-ENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-235 |
6.29e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.65 E-value: 6.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMdklLTVCGLSL--EVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLK 78
Cdd:COG4525 1 MSM---LTVRHVSVryPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIAGFLAPSSGEITLDGVPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 mkenelrhlRGAEIGVVFQEpmTSLNPSMTIGRQLEEGLILhTKASAQERRSLILDMLKRVGIRDPEGAlssYPHEFSGG 158
Cdd:COG4525 74 ---------PGADRGVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARR---RIWQLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVM--EKGAIVE 235
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-245 |
6.68e-28 |
|
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: 111.81 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgAEIGVVFQEp 99
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE----NGRVLVDGHDLALADPAWLR----RQVGVVLQE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtslnpSMTIGRQLEEGLILHTKASAQERrslILDMLKRVGIRD-----PEG---ALSSYPHEFSGGMRQRIMLASVMLL 171
Cdd:cd03252 85 ------NVLFNRSIRDNIALADPGMSMER---VIEAAKLAGAHDfiselPEGydtIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
299-519 |
7.02e-28 |
|
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: 111.81 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQ----------DPY 367
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVLQenvlfnrsirDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SSLDPRMTIEALVEEAlrpvpGLDGKAKRKRTLETLEEVGLGVDYAGrypheLSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:cd03252 97 ALADPGMSMERVIEAA-----KLAGAHDFISELPEGYDTIVGEQGAG-----LSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 448 SALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDspKEAYTRRL 519
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA--ENGLYAYL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
275-502 |
7.22e-28 |
|
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: 117.51 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYAGRKslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenWTD 354
Cdd:TIGR02203 331 VEFRNVTFRYPGRD--------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD----LAD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 355 YRLNCQ-----------MVFQDP------YSslDPRMTIEALVEEALRpvpglDGKAKrkrtlETLEEVGLGVDY-AGRY 416
Cdd:TIGR02203 399 YTLASLrrqvalvsqdvVLFNDTianniaYG--RTEQADRAEIERALA-----AAYAQ-----DFVDKLPLGLDTpIGEN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 417 PHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDG 496
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDG 543
|
....*.
gi 1681691554 497 RIIEEG 502
Cdd:TIGR02203 544 RIVERG 549
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-264 |
7.65e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPP---TIKVADgsvsykgrdvLK 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKsTLA-KLLNGLLLPeagTITVGG----------MV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 MKENELRHLRgAEIGVVFQEP-----MTSLNPSMTIGrqLEEGLILHTKAsaQERrslILDMLKRVGIRDpegALSSYPH 153
Cdd:PRK13635 71 LSEETVWDVR-RQVGMVFQNPdnqfvGATVQDDVAFG--LENIGVPREEM--VER---VDQALRQVGMED---FLNREPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAI 233
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 1681691554 234 VEKGRTEDLLKAPQH--------PYTKKLLSSLPFRGRP 264
Cdd:PRK13635 219 LEEGTPEEIFKSGHMlqeigldvPFSVKLKELLKRNGIL 257
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
275-498 |
7.86e-28 |
|
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: 109.61 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYAGRKSLfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWT 353
Cdd:cd03246 1 LEVENVSFRYPGAEPP--------VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADiSQWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQMVFQDpyssldprmtiealveealrpVPGLDGkakrkrtleTLEEvglgvdyagrypHELSGGQRQRVAIARA 433
Cdd:cd03246 73 ELGDHVGYLPQD---------------------DELFSG---------SIAE------------NILSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQvADRVVVMQDGRI 498
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-252 |
1.14e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.51 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRdvlKMKENELRHL------RGaeig 93
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD----SGEVLWDGE---PLDPEDRRRIgylpeeRG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 vvfqepmtsLNPSMTIGRQLE-----EGLilhTKASAQERrslILDMLKRVGIRDPEGALSsypHEFSGGMRQRIMLASV 168
Cdd:COG4152 82 ---------LYPKMKVGEQLVylarlKGL---SKAEAKRR---ADEWLERLGLGDRANKKV---EELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 169 MLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKapQH 248
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QF 220
|
....
gi 1681691554 249 PYTK 252
Cdd:COG4152 221 GRNT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
27-250 |
1.40e-27 |
|
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: 110.89 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMkenelrHLRGAEIGVVFQEpmTSLNPS 106
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD----SGTILFGGEDATDV------PVQERNVGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIGRQLEEGLILHTKA---SAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTT 183
Cdd:cd03296 89 MTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQL---DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 184 ALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPY 250
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
295-512 |
1.56e-27 |
|
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: 110.71 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 295 KPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPYSSLDPRM 374
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TiealVEEALRPV---PGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:cd03218 91 T----VEENILAVleiRGLSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 452 VTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK 512
Cdd:cd03218 166 PIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-234 |
1.59e-27 |
|
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: 109.65 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlpptIKVADGSVSYKGRDvLKMKEnelrhlRGAEIGVVFQEP 99
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL----IKESSGSILLNGKP-IKAKE------RRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSLNpSMTIGRQLEEGLILhtKASAQERRSLILDMLkrvgirDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03226 81 DYQLF-TDSVREELLLGLKE--LDAGNEQAETVLKDL------DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIVVMEKGAIV 234
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
296-515 |
2.28e-27 |
|
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: 110.32 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKR----ALHGVSIDIHEGEVVALVGGSGSGKTTlgrtIAGLVTE----SEGRIQFQGRP-RTENWTDYRLNCQMVFQDP 366
Cdd:cd03249 11 PSRpdvpILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLDGVDiRDLNLRWLRSQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 ------------YSSLDPrmtIEALVEEALRpvpgldgKAKRKRTLETLEEvglGVD-YAGRYPHELSGGQRQRVAIARA 433
Cdd:cd03249 87 vlfdgtiaenirYGKPDA---TDEEVEEAAK-------KANIHDFIMSLPD---GYDtLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVeQVADRVVVMQDGRIIEEGDRDTIFdSPKE 513
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELM-AQKG 229
|
..
gi 1681691554 514 AY 515
Cdd:cd03249 230 VY 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-237 |
2.34e-27 |
|
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: 109.29 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHL---RGaeigvvfqe 98
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD----SGEVLFDGKPLDIAARNRIGYLpeeRG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 pmtsLNPSMTIGRQLEEGLILH--TKASAQERrslILDMLKRVGIRDPEgalSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:cd03269 81 ----LYPKMKVIDQLVYLAQLKglKKEEARRR---IDEWLERLELSEYA---NKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
273-510 |
2.48e-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: 110.56 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEG-RIQFQGRPR-TE 350
Cdd:COG1119 2 PLLELRNVTVRRGGK----------TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 351 NWTDYRLNCQMVFQDPYSSLDPRMTIEALVEEALRPVPGLDGK---AKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQR 427
Cdd:COG1119 72 DVWELRKRIGLVSPALQLRFPRDETVLDVVLSGFFDSIGLYREptdEQRERARELLELLGLA-HLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 428 VAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
...
gi 1681691554 508 FDS 510
Cdd:COG1119 231 LTS 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
279-511 |
2.50e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.25 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 279 DIIVDYAGRKSLFRKNKPK--RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQ-------------- 342
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 343 ---FQGRPRTENWTDYRLNCQMVFQDPYSSLDpRMTIEALVeeALRPVP-GLDGKAKRKRTLETLEEVGLGVDYAGRYPH 418
Cdd:PRK13631 99 litNPYSKKIKNFKELRRRVSMVFQFPEYQLF-KDTIEKDI--MFGPVAlGVKKSEAKKLAKFYLNKMGLDDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 419 ELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDlQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
250
....*....|...
gi 1681691554 499 IEEGDRDTIFDSP 511
Cdd:PRK13631 255 LKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-268 |
3.64e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENE-LRHLRgAEIGVVFQEPMTSLNP 105
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS----SGTITIAGYHITPETGNKnLKKLR-KKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 106 SmTIGRQLEEGlILHTKASAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTAL 185
Cdd:PRK13641 101 N-TVLKDVEFG-PKNFGFSEDEAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 186 DAVIQRDVMELMVELTRAeGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ--------HPYTKKLLSS 257
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyldEPATSRFASK 255
|
250
....*....|....*.
gi 1681691554 258 L-----PFRGRPRQID 268
Cdd:PRK13641 256 LekggfKFSEMPLTID 271
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
293-514 |
5.02e-27 |
|
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: 115.73 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDP---YS 368
Cdd:TIGR03375 474 PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDiRQIDPADLRRNIGYVPQDPrlfYG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 SLDPRMTIEA-LVEEAlrpvpgldgkakrkRTLETLEEVGLGvDYAGRYPH-----------ELSGGQRQRVAIARAIAR 436
Cdd:TIGR03375 554 TLRDNIALGApYADDE--------------EILRAAELAGVT-EFVRRHPDgldmqigergrSLSGGQRQAVALARALLR 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 437 RPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEGDRDTIFDSPKEA 514
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
293-502 |
5.23e-27 |
|
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: 108.83 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDP---YS 368
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDiRQLDPADLRRNIGYVPQDVtlfYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 SLDPRMTIEALVeealrpvpgldgkAKRKRTLETLEEVGLGvDYAGRYPH-----------ELSGGQRQRVAIARAIARR 437
Cdd:cd03245 93 TLRDNITLGAPL-------------ADDERILRAAELAGVT-DFVNKHPNgldlqigergrGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 438 PRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVeQVADRVVVMQDGRIIEEG 502
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
291-510 |
7.27e-27 |
|
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: 108.47 E-value: 7.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP---RTENWtdYRLNCQMVFQDP- 366
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdISRKS--LRSMIGVVLQDTf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 -----------YSSLDPRmtiEALVEEALRPVPGLDGKAKRKRTLETleevglgvdYAGRYPHELSGGQRQRVAIARAIA 435
Cdd:cd03254 88 lfsgtimenirLGRPNAT---DEEVIEAAKEAGAHDFIMKLPNGYDT---------VLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 436 RRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-243 |
1.28e-26 |
|
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: 113.36 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYK-GRDVLKMKEN--ELRHLRGAEIGVVFQEpm 100
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT----SGEVNVRvGDEWVDMTKPgpDGRGRAKRYIGILHQE-- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 TSLNPSMTIGRQLEEGLILHTKASAQERRSLIldMLKRVGIRD--PEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIA 178
Cdd:TIGR03269 374 YDLYPHRTVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDEekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 179 DEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-246 |
1.42e-26 |
|
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: 110.96 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVL--KMKENELRHLRGaeIGVVFQEPmtSLN 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERP----DSGRIRLGGEVLQdsARGIFLPPHRRR--IGYVFQEA--RLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 105 PSMTIGRQLEEGlilHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTA 184
Cdd:COG4148 90 PHLSVRGNLLYG---RKRAPRAERRISFDEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 185 LDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
305-509 |
1.46e-26 |
|
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: 107.63 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 305 IDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDyrlnCQMVFQDPYSSLDPRMTIEALVEEAL 384
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH----IGYVPQRHEFAWDFPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 385 RPVPGL---DGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDL 461
Cdd:TIGR03771 77 TGHIGWlrrPCVADFAAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 462 FSDLQKRyGFSCLFISHDLGVVEQVADRVVVMqDGRIIEEGDRDTIFD 509
Cdd:TIGR03771 156 FIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQD 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
297-515 |
1.60e-26 |
|
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: 106.84 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL--VTESEGRIQFQGRPRTENWTDYRLNCQ--MVFQDPYSsldp 372
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGifLAFQYPPE---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 rmtiealveealrpVPGLdgkakrkRTLETLEEVGLGvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:cd03217 89 --------------IPGV-------KNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 453 TVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQV-ADRVVVMQDGRIIEEGDRDTIFDSPKEAY 515
Cdd:cd03217 138 DALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-247 |
1.71e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 39 IVGESGSGKTLATRALISLLPPTikvaDGSVSYkGRDVL--KMKENELRHLRgAEIGVVFQEPMtslnpsmtigRQLEEG 116
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPT----SGTVTI-GERVItaGKKNKKLKPLR-KKVGIVFQFPE----------HQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 117 LILHTKA--------SAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAV 188
Cdd:PRK13634 102 TVEKDICfgpmnfgvSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 189 IQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-214 |
1.91e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.80 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLE---VARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKvADGSVSYKGRDVLKMKEnELRHl 87
Cdd:COG4136 1 MLSLEnltITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFS-ASGEVLLNGRRLTALPA-EQRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 88 rgaeIGVVFQEPMtsLNPSMTIGRQLeeGLILHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLAS 167
Cdd:COG4136 78 ----IGILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGL---AGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHD 214
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-243 |
2.21e-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: 107.13 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENElRHLRGaeIGVVFQEPMt 101
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR----SGSIRFDGRDITGLPPHE-RARAG--IGYVPEGRR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 sLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRdpegaLSSYPHEFSGGMRQriMLA--SVMLLKPALLIAD 179
Cdd:cd03224 86 -IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKER-----RKQLAGTLSGGEQQ--MLAiaRALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 180 EPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-256 |
2.82e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.75 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQ-QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDV---------LKM-KENELRH 86
Cdd:PRK10619 14 RYGEhEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS----EGSIVVNGQTInlvrdkdgqLKVaDKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRgAEIGVVFQEpmTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLA 166
Cdd:PRK10619 90 LR-TRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI--DERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
250
....*....|
gi 1681691554 247 QHPYTKKLLS 256
Cdd:PRK10619 244 QSPRLQQFLK 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-256 |
2.84e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVADGSVSYKGrdvlKMKENELRHLRGaEIGVVF 96
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPdsgQLNIAGHQFDFSQ----KPSEKAIRLLRQ-KVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEpmTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:COG4161 89 QQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAEGTAIlLISHDLPMVARYTSRIVVMEKGAIVEKGrTEDLLKAPQHPYTKKLLS 256
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAFAHYLS 241
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
13-255 |
4.03e-26 |
|
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: 109.70 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 13 SLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikVADGSVSYKGRDVLKMKEnelrHLRGaeI 92
Cdd:TIGR03258 10 HLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAA--GLTGRIAIADRDLTHAPP----HKRG--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 93 GVVFQEpmTSLNPSMTIGRQLEEGLILHTKASAQERRSlILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLK 172
Cdd:TIGR03258 82 ALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAER-VADALKLVGLGD---AAAHLPAQLSGGMQQRIAIARAIAIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVEL-TRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYT 251
Cdd:TIGR03258 156 PDVLLLDEPLSALDANIRANMREEIAALhEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFA 235
|
....
gi 1681691554 252 KKLL 255
Cdd:TIGR03258 236 AEFL 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
303-502 |
5.18e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 109.35 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIqFQGRPRTENWTDYRLNCQMVFQDpYSsLDPRMTIEALVEE 382
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQS-YA-LYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 383 ALRpVPGLDgKAKRKRTLETLEEVgLGVDYA-GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDL 461
Cdd:PRK11000 99 GLK-LAGAK-KEEINQRVNQVAEV-LQLAHLlDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1681691554 462 FSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:PRK11000 176 ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-237 |
5.47e-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: 105.38 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEnELRHlrgaeIGVVFQEP 99
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD----SGEITFDGKSYQKNIE-ALRR-----IGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMTIgrqlEEGLILHTKAsAQERRSLILDMLKRVGirdpegaLSSYPHE----FSGGMRQRIMLASVMLLKPAL 175
Cdd:cd03268 82 --GFYPNLTA----RENLRLLARL-LGIRKKRIDEVLDVVG-------LKDSAKKkvkgFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 176 LIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-256 |
7.86e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 7.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISL--LPPTIKVAdGSVSYKGRDVLKMKENELRHlrgaE 91
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVS-GEVYLDGQDIFKMDVIELRR----R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 92 IGVVFQEPmtSLNPSMTIGRQLEEGL----ILHTKASAQERrslILDMLKRVGIRDP-EGALSSYPHEFSGGMRQRIMLA 166
Cdd:PRK14247 84 VQMVFQIP--NPIPNLSIFENVALGLklnrLVKSKKELQER---VRWALEKAQLWDEvKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAegTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
250
....*....|
gi 1681691554 247 QHPYTKKLLS 256
Cdd:PRK14247 237 RHELTEKYVT 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
300-502 |
8.04e-26 |
|
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: 105.78 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDP------------ 366
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSLRRAIGVVPQDTvlfndtigynir 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 YSSLDprmTIEALVEEALRpvpgldgKAKRKRTLETLE--------EVGLgvdyagryphELSGGQRQRVAIARAIARRP 438
Cdd:cd03253 97 YGRPD---ATDEEVIEAAK-------AAQIHDKIMRFPdgydtivgERGL----------KLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 439 RFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEG 502
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-231 |
8.39e-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: 105.28 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIkvadGSVSYKGRDVLKMKENELRH 86
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS----GTAYINGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 lrgaeIGVVFQEPMtsLNPSMTIgrqlEEGLILHTKA---SAQERRSLILDMLKRVGIRDPEGALSSyphEFSGGMRQRI 163
Cdd:cd03263 77 -----LGYCPQFDA--LFDELTV----REHLRFYARLkglPKSEIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRKL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 164 MLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRaeGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-237 |
9.03e-26 |
|
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: 105.14 E-value: 9.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgaEIGVVFQEpmT 101
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD----AGFATVDGFDVVKEPAEARR-----RLGFVSDS--T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLEEGLILH-TKASAQERRslILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:cd03266 88 GLYDRLTARENLEYFAGLYgLKGDELTAR--LEELADRLGMEE---LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 181 PTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03266 163 PTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-237 |
9.24e-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: 105.07 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLaPGEIFGIVGESGSGKTLATRALISLLPPT--IKVADGSVSYKGRDVLKMKENELRhlrgaeIGVVFQEpmTSLN 104
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDggTIVLNGTVLFDSRKKINLPPQQRK------IGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 105 PSMTIGRQLEEGLILHtkaSAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTA 184
Cdd:cd03297 88 PHLNVRENLAFGLKRK---RNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 185 LDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-237 |
1.03e-25 |
|
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: 104.97 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGeIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaeIGVVFQEP 99
Cdd:cd03264 12 KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS----SGTIRIDGQDVLKQPQKLRRR-----IGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSlnPSMTIGRQLEEGLILHTKASAQERRsLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03264 82 GVY--PNFTVREFLDYIAWLKGIPSKEVKA-RVDEVLELVNLGD---RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 180 EPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
265-493 |
1.13e-25 |
|
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: 110.45 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 265 RQIDLTSVPMISARDIIVDYAGRKSlfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQ 344
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPGRRP---------ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 345 GRPRTE-NWTDYRLNCQMVFQDPY---SSL-------DPRMTiEALVEEALRPVpGLDgkakrkrtlETLEEVGLGVDY- 412
Cdd:TIGR02857 383 GVPLADaDADSWRDQIAWVPQHPFlfaGTIaenirlaRPDAS-DAEIREALERA-GLD---------EFVAALPQGLDTp 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 413 AGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEqVADRVVV 492
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVV 528
|
.
gi 1681691554 493 M 493
Cdd:TIGR02857 529 L 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-522 |
1.17e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 110.48 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 33 PGEIFGIVGESGSGKTLATRALISllpptIKVAD-GSVSYKGRDVlkmKENELRHLRGAEIGVVFQEpmtsLN--PSMTI 109
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTG-----IYTRDaGSILYLGKEV---TFNGPKSSQEAGIGIIHQE----LNliPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 110 ------GRQLEE--GLILHTKASAQERRslildMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PRK10762 97 aeniflGREFVNrfGRIDWKKMYAEADK-----LLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 182 TTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGA-IVEKG---RTEDLLKapQHPYTKKLLSS 257
Cdd:PRK10762 169 TDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIAEREvadLTEDSLI--EMMVGRKLEDQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 258 LPFRGRPRqidltsvpmisardiivdyaGRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES 337
Cdd:PRK10762 246 YPRLDKAP--------------------GEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 338 EGRIQFQGRPRTENWTDYRLNCQMVfqdpYSSLDPR---MTIEALVEE-----ALRPVPGLDGKAKRKRTLETLEE---- 405
Cdd:PRK10762 306 SGYVTLDGHEVVTRSPQDGLANGIV----YISEDRKrdgLVLGMSVKEnmsltALRYFSRAGGSLKHADEQQAVSDfirl 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 406 -----------VGLgvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLqKRYGFSCL 474
Cdd:PRK10762 382 fniktpsmeqaIGL-----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSII 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1681691554 475 FISHDLGVVEQVADRVVVMQDGRIIEEGDRdtifdspKEAYTRRLLSA 522
Cdd:PRK10762 450 LVSSEMPEVLGMSDRILVMHEGRISGEFTR-------EQATQEKLMAA 490
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
273-512 |
1.36e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTeNW 352
Cdd:COG1137 2 MTLEAENLVKSYGKR----------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRlNCQM----------VFQdpyssldpRMTIE----ALVEeaLRPVPgldgKAKRKRTLETL-EEVGLGvDYAGRYP 417
Cdd:COG1137 71 PMHK-RARLgigylpqeasIFR--------KLTVEdnilAVLE--LRKLS----KKEREERLEELlEEFGIT-HLRKSKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 418 HELSGGQRQRVAIARAIARRPRFLIADEPVSALD-VTVrAQVLDLFSDLQKRyGFSCLFISHD----LGVVeqvaDRVVV 492
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIGVLITDHNvretLGIC----DRAYI 208
|
250 260
....*....|....*....|
gi 1681691554 493 MQDGRIIEEGDRDTIFDSPK 512
Cdd:COG1137 209 ISEGKVLAEGTPEEILNNPL 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
275-502 |
1.38e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYAGrkslfrKNKPkrALHGVSIDIHEGEVVALVGGSGSGKTTlgrtIAGLVTE----SEGRIQFQGRprte 350
Cdd:PRK11176 342 IEFRNVTFTYPG------KEVP--ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGH---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 351 NWTDYRL-----NCQMVFQD------------PYSSLDpRMTIEAlVEEALRPVPGLDGKAKRKRTLETLeevglgvdyA 413
Cdd:PRK11176 406 DLRDYTLaslrnQVALVSQNvhlfndtianniAYARTE-QYSREQ-IEEAARMAYAMDFINKMDNGLDTV---------I 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 414 GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQvADRVVVM 493
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVV 551
|
....*....
gi 1681691554 494 QDGRIIEEG 502
Cdd:PRK11176 552 EDGEIVERG 560
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-244 |
1.39e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.09 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTI-------------KVADGSVSYKGRDVLKM-------KE 81
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTgtiewifkdeknkKKTKEKEKVLEKLVIQKtrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 82 NELRHlrgaEIGVVFQEPMTSLNPSmTIGRQLEEGLILH--TKASAQERrslILDMLKRVGIrdPEGALSSYPHEFSGGM 159
Cdd:PRK13651 101 KEIRR----RVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMgvSKEEAKKR---AAKYIELVGL--DESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 160 RQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRT 239
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
....*
gi 1681691554 240 EDLLK 244
Cdd:PRK13651 250 YDILS 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
298-502 |
1.59e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.87 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVT---ESEGRIQFQGRP------RTENWTDYRLNCQMVFQDpyS 368
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTvqregrLARDIRKSRANTGYIFQQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 SLDPRMTI-EALVEEALRPVP------GLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFL 441
Cdd:PRK09984 96 NLVNRLSVlENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-232 |
1.60e-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: 104.82 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGR----DVLKMKENELRHLRGAEIGVVFQ 97
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREILALRRRTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 ---------------EPMtslnpsmtigrqLEEGLilhTKASAQERRSlilDMLKRVGIrdPEGALSSYPHEFSGGMRQR 162
Cdd:COG4778 101 flrviprvsaldvvaEPL------------LERGV---DREEARARAR---ELLARLNL--PERLWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGA 232
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
298-508 |
2.69e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-----ENWTDYRLNCQMVFQDPYSSLdp 372
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLVFQFPESQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 rmtieaLVEEALRPVP------GLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:PRK13649 99 ------FEETVLKDVAfgpqnfGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 447 VSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
291-534 |
3.09e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKP--KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF-----QGRPRTENWTDYRLNCQMVF 363
Cdd:PRK13643 11 YQPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 364 QDPYSSLDPRMTIEalvEEALRPVP-GLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLI 442
Cdd:PRK13643 91 QFPESQLFEETVLK---DVAFGPQNfGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 443 ADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK--EAYTRRLL 520
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDflKAHELGVP 246
|
250
....*....|....
gi 1681691554 521 SAIPALDQNEKGGV 534
Cdd:PRK13643 247 KATHFADQLQKTGA 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-240 |
3.57e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.80 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHLRgAEIGVVFQEP 99
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSLNpsMTIGRQLEEGLILhTKASAQERRSLILDMLKRVGIRDPEgalSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK10908 89 HLLMD--RTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLDKA---KNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAeGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTE 240
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
299-538 |
4.05e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.07 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE--NWTDYRLNCQMVFQDPYSSLDPRMti 376
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVGIVFQNPETQFVGRT-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 ealVEEALRPVPG---LDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:PRK13644 95 ---VEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 454 VRAQVLDLFSDLQKRyGFSCLFISHDLGVVeQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLSAIPALDQN-EKG 532
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLIELAENlKMH 248
|
....*.
gi 1681691554 533 GVTLKW 538
Cdd:PRK13644 249 GVVIPW 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
299-493 |
4.69e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenwtdyrlncQMVFQdpYSSLDPRM--TI 376
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----------AYVPQ--RSEVPDSLplTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRPVPGLDG---KAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:NF040873 75 RDLVAMGRWARRGLWRrltRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1681691554 454 VRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQvADRVVVM 493
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-237 |
8.12e-25 |
|
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: 102.33 E-value: 8.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENElrhlRGaeIGVVFQEp 99
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT----SGRIYIGGRDVTDLPPKD----RD--IAMVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03301 81 -YALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
300-508 |
9.95e-25 |
|
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: 107.91 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrTENWTDYRLNC------QMV----------- 362
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD-LSQWDREELGRhigylpQDVelfdgtiaeni 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 363 --FQDPysslDPRMTIEAL----VEEALRPVPglDGkakrkrtLETleEVGlgvdyAGRYPheLSGGQRQRVAIARAIAR 436
Cdd:COG4618 427 arFGDA----DPEKVVAAAklagVHEMILRLP--DG-------YDT--RIG-----EGGAR--LSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 437 RPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVeQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-237 |
1.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmkENELRHLRGAEiGVVFQEPMTS 102
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS----EGKVYVDGLDTSD--EENLWDIRNKA-GMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LnpSMTIgrqLEEGLIL---HTKASAQERRSLILDMLKRVGirdpegaLSSY----PHEFSGGMRQRIMLASVMLLKPAL 175
Cdd:PRK13633 98 I--VATI---VEEDVAFgpeNLGIPPEEIRERVDESLKKVG-------MYEYrrhaPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 176 LIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKG 237
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-533 |
1.33e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.64 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 271 SVPMISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEG-----RIQFQG 345
Cdd:PRK14271 18 AAPAMAAVNLTLGFAG----------KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 346 RP--RTENWTDYRLNCQMVFQDPysslDP-RMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLG---VDYAGRYPHE 419
Cdd:PRK14271 88 RSifNYRDVLEFRRRVGMLFQRP----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWdavKDRLSDSPFR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 420 LSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRygFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
250 260 270
....*....|....*....|....*....|....
gi 1681691554 500 EEGDRDTIFDSPKEAYTRRLLSAIPALDQNEKGG 533
Cdd:PRK14271 242 EEGPTEQLFSSPKHAETARYVAGLSGDVKDAKRG 275
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-243 |
1.33e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.74 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHlrgaEIGVVFQEPM- 100
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR----NIAVVFQDAGl 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 --TSLNPSMTIGRQ--LEEGLILHTKASAQ----ERRSLILDMlkRVGIRDpegalssypHEFSGGMRQRIMLASVMLLK 172
Cdd:PRK13657 421 fnRSIEDNIRVGRPdaTDEEMRAAAERAQAhdfiERKPDGYDT--VVGERG---------RQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELTRAEGTAIllISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTV-RNADRILVFDNGRVVESGSFDELV 557
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-256 |
1.91e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 13 SLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISL--LPPTIKVaDGSVSYKGRDVLKMKENELRHLRga 90
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEARV-EGEVRLFGRNIYSPDVDPIEVRR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 EIGVVFQEPmtSLNPSMTIGRQLEEGLILHTKASAQERRSLILD-MLKRVGIRDP-EGALSSYPHEFSGGMRQRIMLASV 168
Cdd:PRK14267 86 EVGMVFQYP--NPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALWDEvKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 169 MLLKPALLIADEPTTALDAVIQRDVMELMVELTraEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQH 248
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
....*...
gi 1681691554 249 PYTKKLLS 256
Cdd:PRK14267 242 ELTEKYVT 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-517 |
2.04e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.42 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLvTESEGRIQFQGR---------PRTENWTDYRLNCQMVFQDP- 366
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffnqniyERRVNLNRLRRQVSMVHPKPn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 ------YSSL---------DPRMTIEALVEEALRPVPGLDgKAKRKRTLETLEevglgvdyagrypheLSGGQRQRVAIA 431
Cdd:PRK14258 99 lfpmsvYDNVaygvkivgwRPKLEIDDIVESALKDADLWD-EIKHKIHKSALD---------------LSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 432 RAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQD-----GRIIEEGDRDT 506
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKK 242
|
250
....*....|.
gi 1681691554 507 IFDSPKEAYTR 517
Cdd:PRK14258 243 IFNSPHDSRTR 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
274-509 |
2.28e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 102.08 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDY--------AGRKSLFRKNKPKR----ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRI 341
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrSLKELLLRRRRTRReefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 342 QFQGRPrtenwtdyrlncqmvfqdpySSL-------DPRMTiealVEEALRPVPGLDGkAKRKRTLETLEEVglgVDYA- 413
Cdd:COG1134 84 EVNGRV--------------------SALlelgagfHPELT----GRENIYLNGRLLG-LSRKEIDEKFDEI---VEFAe 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 414 -GRYPHE----LSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVAD 488
Cdd:COG1134 136 lGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCD 214
|
250 260
....*....|....*....|.
gi 1681691554 489 RVVVMQDGRIIEEGDRDTIFD 509
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
298-499 |
2.30e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.55 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES--EGRIQFQGRP-RTENWTDY-RLNCQMVFQDpySSLDPR 373
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEElQASNIRDTeRAGIAIIHQE--LALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTiealVEEAL----RPVPG--LDGKAKRKRTLETLEEVGLGVDYAGRYpHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:PRK13549 97 LS----VLENIflgnEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPV-GNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 448 SALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:PRK13549 172 ASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-256 |
2.38e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.16 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVARtgQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRAL--ISLLPPTIKVAdGSVSYKGRDVLKMK 80
Cdd:PRK14239 2 TEPILQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTIT-GSIVYNGHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 81 EN--ELRHlrgaEIGVVFQEPmtslNP-SMTIGRQLEEGLIL---HTKASAQE--RRSLI-LDMLKRVGIRDPEGALSsy 151
Cdd:PRK14239 79 TDtvDLRK----EIGMVFQQP----NPfPMSIYENVVYGLRLkgiKDKQVLDEavEKSLKgASIWDEVKDRLHDSALG-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 152 pheFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTraEGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:PRK14239 149 ---LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|....*
gi 1681691554 232 AIVEKGRTEDLLKAPQHPYTKKLLS 256
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKETEDYIS 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-247 |
2.76e-24 |
|
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: 101.21 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLslEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELR 85
Cdd:COG0410 3 MLEVENL--HAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR----SGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 86 HLrgaeiGV--------VFqepmtslnPSMTIgrqlEEGLIL-----HTKASAQERRSLILDMLKRVG--IRDPEGALSs 150
Cdd:COG0410 77 RL-----GIgyvpegrrIF--------PSLTV----EENLLLgayarRDRAEVRADLERVYELFPRLKerRRQRAGTLS- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 151 yphefsGGMRQriMLA--SVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVM 228
Cdd:COG0410 139 ------GGEQQ--MLAigRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVL 209
|
250
....*....|....*....
gi 1681691554 229 EKGAIVEKGRTEDLLKAPQ 247
Cdd:COG0410 210 ERGRIVLEGTAAELLADPE 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
300-501 |
3.32e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRL-----NCQMVFQDpySSLDPrm 374
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakHVGFVFQS--FMLIP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALvEEALRP--VPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:PRK10584 102 TLNAL-ENVELPalLRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 453 TVRAQVLDLFSDLQKRYGFSCLFISHDlgvvEQVA---DRVVVMQDGRIIEE 501
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHD----LQLAarcDRRLRLVNGQLQEE 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-244 |
3.35e-24 |
|
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: 101.15 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEP 99
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKT----TLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM----IGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSlnpSMTIgrqlEEGLILHTKASAQERrslILDMLKRVG----IRDPEGALSSYPHE----FSGGMRQRIMLASVMLL 171
Cdd:cd03254 87 FLF---SGTI----MENIRLGRPNATDEE---VIEAAKEAGahdfIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 172 KPALLIADEPTTALD----AVIQRDVMELMveltraEGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:cd03254 157 DPKILILDEATSNIDteteKLIQEALEKLM------KGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-244 |
3.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.43 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENeLRHLRgAEIGVVFQEPMTSL 103
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT----SGKIIIDGVDITDKKVK-LSDIR-KKVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSmTIGRQLEEGLIlHTKASAQERRSLILDMLKRVGIrDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTT 183
Cdd:PRK13637 97 FEE-TIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 184 ALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-498 |
4.13e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.78 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvadgSVSYKGRDVLKMKENELRHLRGAE---IGVVFQEPMtsL 103
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--------HGTYEGEIIFEGEELQASNIRDTEragIAIIHQELA--L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTI------GRQLEEGLILHTKASAQERRSLildmLKRVGIR-DPEGALSSYphefSGGMRQRIMLASVMLLKPALL 176
Cdd:PRK13549 94 VKELSVleniflGNEITPGGIMDYDAMYLRAQKL----LAQLKLDiNPATPVGNL----GLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGaivekgrtedllkapQHPYTKKLLS 256
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDG---------------RHIGTRPAAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 257 slpfrgrprqidltsvpmISARDIIVDYAGR--KSLFRK---------------------NKPKRALHGVSIDIHEGEVV 313
Cdd:PRK13549 230 ------------------MTEDDIITMMVGRelTALYPRephtigevilevrnltawdpvNPHIKRVDDVSFSLRRGEIL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 314 ALVGGSGSGKTTLGRTIAGLVT-ESEGRIQFQGRPRTENwtdyrlNCQ--------MVFQD-------PYSSLDPRMTIE 377
Cdd:PRK13549 292 GIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIR------NPQqaiaqgiaMVPEDrkrdgivPVMGVGKNITLA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 ALVEEALRPVpgLDGKAKRKRTLETLEEVGLgvdyagRYPH------ELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:PRK13549 366 ALDRFTGGSR--IDDAAELKTILESIQRLKV------KTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1681691554 452 VTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-245 |
4.28e-24 |
|
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: 100.77 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 19 TGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVlkmKENELRHLRgAEIGVVFQE 98
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLR-RQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PM---TSLNPSMTIGR------QLEEGLILhtkASAQErrsLILDMlkrvgirdPEG---ALSSYPHEFSGGMRQRIMLA 166
Cdd:cd03251 85 VFlfnDTVAENIAYGRpgatreEVEEAARA---ANAHE---FIMEL--------PEGydtVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-234 |
4.62e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSLEVARtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENE 83
Cdd:COG3845 255 EVVLEVENLSVRDDR-GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA----SGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRgaeIGVVFQEPM-TSLNPSMTIgrqlEEGLILHTKASAQERRSLILD----------MLKRVGIR--DPEGALSS 150
Cdd:COG3845 330 RRRLG---VAYIPEDRLgRGLVPDMSV----AENLILGRYRRPPFSRGGFLDrkairafaeeLIEEFDVRtpGPDTPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 151 ypheFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEK 230
Cdd:COG3845 403 ----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
....
gi 1681691554 231 GAIV 234
Cdd:COG3845 478 GRIV 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-498 |
4.67e-24 |
|
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: 105.29 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtiKVADGSVSYKGRDvlkMKENELRHLRGAEIGVVFQEP 99
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH--GTWDGEIYWSGSP---LKASNIRDTERAGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MtsLNPSMTIGRQLEEGLILHTKASAQERRSLIL---DMLKRVGIRDPEGALSSypHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:TIGR02633 88 T--LVPELSVAENIFLGNEITLPGGRMAYNAMYLrakNLLRELQLDADNVTRPV--GDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV----EKGRTEDLLKAPQhpyTK 252
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVatkdMSTMSEDDIITMM---VG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 253 KLLSSLpFRGRPRQI--DLTSVPMISARDIIvdyagrkslfrkNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTI 330
Cdd:TIGR02633 240 REITSL-YPHEPHEIgdVILEARNLTCWDVI------------NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 331 AGLVT-ESEGRIQFQGRPrtenwTDYRlNCQ--------MVFQD-------PYSSLDPRMTIEALVEEALRPVpgLDGKA 394
Cdd:TIGR02633 307 FGAYPgKFEGNVFINGKP-----VDIR-NPAqairagiaMVPEDrkrhgivPILGVGKNITLSVLKSFCFKMR--IDAAA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 395 KRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCL 474
Cdd:TIGR02633 379 ELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAII 457
|
490 500
....*....|....*....|....
gi 1681691554 475 FISHDLGVVEQVADRVVVMQDGRI 498
Cdd:TIGR02633 458 VVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
300-496 |
7.95e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.27 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQfqgRPRTEnwtdyrlncQMVF--QDPYssldprmtie 377
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---RPAGA---------RVLFlpQRPY---------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 aLVEEALRPV---PGLDGKAKRKRTLETLEEVGLGvDYAGRY------PHELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:COG4178 437 -LPLGTLREAllyPATAEAFSDAELREALEAVGLG-HLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 449 ALDVTVRAQVLDLFsdLQKRYGFSCLFISHDlGVVEQVADRVVVMQDG 496
Cdd:COG4178 515 ALDEENEAALYQLL--REELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
261-502 |
9.21e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.04 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 261 RGRPRQIDLTSVP-MISARDIIVDYAGRKslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEG 339
Cdd:PRK13657 320 RDPPGAIDLGRVKgAVEFDDVSFSYDNSR---------QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 340 RIQFQGRP-RTENWTDYRLNCQMVFQDPyssldprMTIEALVEEALRPvpgldGK-----------AKRKRTLETLEEVG 407
Cdd:PRK13657 391 RILIDGTDiRTVTRASLRRNIAVVFQDA-------GLFNRSIEDNIRV-----GRpdatdeemraaAERAQAHDFIERKP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 408 LGVD-YAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQv 486
Cdd:PRK13657 459 DGYDtVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN- 535
|
250
....*....|....*.
gi 1681691554 487 ADRVVVMQDGRIIEEG 502
Cdd:PRK13657 536 ADRILVFDNGRVVESG 551
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-525 |
9.31e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.61 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRdvlKMKENELRHLRGAEIGVVFQEp 99
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD----AGSILIDGQ---EMRFASTTAALAAGVAIIYQE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLiLHTKASAQERRSLI---LDMLKRVGIR-DPEGALSsyphEFSGGMRQRIMLASVmLLKPAL 175
Cdd:PRK11288 88 -LHLVPEMTVAENLYLGQ-LPHKGGIVNRRLLNyeaREQLEHLGVDiDPDTPLK----YLSIGQRQMVEIAKA-LARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 176 LIA-DEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVekgRTEDLLKapqhpytkkl 254
Cdd:PRK11288 161 VIAfDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYV---ATFDDMA---------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 255 lsslpfrgrprqiDLTSVPMISA---RDI--IVDYAGRK----SLFRKNKPKRALHG-VSIDIHEGEVVALVGGSGSGKT 324
Cdd:PRK11288 227 -------------QVDRDQLVQAmvgREIgdIYGYRPRPlgevRLRLDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 325 TLGRTIAGLVTESEGRIQFQGRPRTENwtdyrlncqmvfqdpysslDPRMTIEALVeeALRP--------VPG------- 389
Cdd:PRK11288 294 ELMKLLYGATRRTAGQVYLDGKPIDIR-------------------SPRDAIRAGI--MLCPedrkaegiIPVhsvadni 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 390 --------------LDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR 455
Cdd:PRK11288 353 nisarrhhlragclINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 456 AQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDtifdspkEAYTRRLLS-AIPA 525
Cdd:PRK11288 433 HEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGELARE-------QATERQALSlALPR 495
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
285-502 |
1.01e-23 |
|
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: 99.53 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 285 AGRKSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenwtdyrlncqmvFQ 364
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-------------LL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 365 DPYSSLDPRMTiealVEEALR---PVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFL 441
Cdd:cd03220 90 GLGGGFNPELT----GRENIYlngRLLGLSRKEIDEKIDEIIEFSELG-DFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-233 |
1.14e-23 |
|
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: 99.02 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHLRgAEIGVVFQEpmTSLNPS 106
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD--FRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIGRQLEEGLILhTKASAQERRSLILDMLKRVGIRDPEgalSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALD 186
Cdd:cd03292 93 RNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKH---RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 187 AVIQRDVMELMVELTRAeGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:cd03292 169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-248 |
1.22e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.07 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENElrhlRGaeIGVVFQEP 99
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT----SGEILIGGRDVTDLPPKD----RN--IAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MtsLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:COG3839 85 A--LYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGL---EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 180 EPTTALDAVIqRDVM--ELMvELTRAEGTAILLISHD----LPMvArytSRIVVMEKGAIVEKGRTEDLLKAPQH 248
Cdd:COG3839 159 EPLSNLDAKL-RVEMraEIK-RLHRRLGTTTIYVTHDqveaMTL-A---DRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-215 |
1.22e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 6 LLTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKmkenelr 85
Cdd:PRK11248 1 MLQISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGSITLDGKPVEG------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 86 hlRGAEIGVVFQEpmTSLNPSMTIGRQLEEGLILHTKASAQeRRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIML 165
Cdd:PRK11248 68 --PGAERGVVFQN--EGLLPWRNVQDNVAFGLQLAGVEKMQ-RLEIAHQMLKKVGL---EGAEKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 166 ASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDL 215
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
294-498 |
1.28e-23 |
|
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: 99.47 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 294 NKPKR-ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDY-RLNCQMVFQDPysSLD 371
Cdd:cd03248 23 TRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVSLVGQEP--VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRmTIEALVEEALRPVPGLDGK--AKRKRTLETLEEVGLGVDY-AGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:cd03248 101 AR-SLQDNIAYGLQSCSFECVKeaAQKAHAHSFISELASGYDTeVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 449 ALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQvADRVVVMQDGRI 498
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
300-499 |
1.32e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.81 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTD-----YRLNCQMVFQDPYssLDPRM 374
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlRREHFGFIFQRYH--LLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEealrpVP----GLDGKAKRKRTLETLEEVGLG--VDYagrYPHELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:PRK10535 102 TAAQNVE-----VPavyaGLERKQRLLRAQELLQRLGLEdrVEY---QPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 449 ALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQvADRVVVMQDGRII 499
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-258 |
1.52e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 100.56 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 9 VCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlppTIKVA----DGSVSYKGRDVLKMKEN-E 83
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM---NDKVSgyrySGDVLLGGRSIFNYRDVlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHlrgaEIGVVFQEPmtslNP-SMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDP-EGALSSYPHEFSGGMRQ 161
Cdd:PRK14271 99 FRR----RVGMLFQRP----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 162 RIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTED 241
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
250
....*....|....*..
gi 1681691554 242 LLKAPQHPYTKKLLSSL 258
Cdd:PRK14271 249 LFSSPKHAETARYVAGL 265
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
291-502 |
1.53e-23 |
|
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: 104.65 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQD---- 365
Cdd:TIGR03797 461 YRPDGP-LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGlDVQAVRRQLGVVLQNgrlm 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 PYSSLD-----PRMTIEAlVEEALRPVpGLDGKAKR-KRTLETLEEVGLGvdyagryphELSGGQRQRVAIARAIARRPR 439
Cdd:TIGR03797 540 SGSIFEniaggAPLTLDE-AWEAARMA-GLAEDIRAmPMGMHTVISEGGG---------TLSGGQRQRLLIARALVRKPR 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 440 FLIADEPVSALDVTVRAQVLDLFSDLQkrygFSCLFISHDLGVVeQVADRVVVMQDGRIIEEG 502
Cdd:TIGR03797 609 ILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTI-RNADRIYVLDAGRVVQQG 666
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
288-509 |
1.68e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.32 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLF-RKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVF-QD 365
Cdd:COG4586 25 KGLFrREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 pySSLDPRMT-IEALveEALRPVPGLDgKAKRKRTLETLEEVgLGV-DYAGRYPHELSGGQRQRVAIARAIARRPRFLIA 443
Cdd:COG4586 105 --SQLWWDLPaIDSF--RLLKAIYRIP-DAEYKKRLDELVEL-LDLgELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 444 DEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
288-502 |
1.77e-23 |
|
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: 99.33 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLF-RKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVF--- 363
Cdd:cd03267 24 KSLFkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgqk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 364 QDPYSSLDPRMTIEALveealRPVPGLDgKAKRKRTLETLEE---VGLGVDYAGRyphELSGGQRQRVAIARAIARRPRF 440
Cdd:cd03267 104 TQLWWDLPVIDSFYLL-----AAIYDLP-PARFKKRLDELSElldLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-244 |
1.82e-23 |
|
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: 99.15 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLP----PTikvaDGSVSYKGRDvlkMKENELRHLRgAEIG 93
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLErfydPT----SGEILLDGVD---IRDLNLRWLR-SQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQEPMTSlnpSMTIgrqLEEglILHTKASAQErrSLILDMLKRVGIRDpegALSSYPHEF-----------SGGMRQR 162
Cdd:cd03249 81 LVSQEPVLF---DGTI---AEN--IRYGKPDATD--EEVEEAAKKANIHD---FIMSLPDGYdtlvgergsqlSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDEL 224
|
..
gi 1681691554 243 LK 244
Cdd:cd03249 225 MA 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
299-515 |
1.92e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.68 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrTENWTDY---RLNCQMVFQDpySSLDPRMT 375
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH-IEGLPGHqiaRMGVVRTFQH--VRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 -IEALVEEALRPV-----PGL-DGKAKRK-------RTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFL 441
Cdd:PRK11300 97 vIENLLVAQHQQLktglfSGLlKTPAFRRaesealdRAATWLERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPK--EAY 515
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDviKAY 251
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
274-523 |
2.08e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.39 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP------ 347
Cdd:COG4604 1 MIEIKNVSKRYGG----------KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattps 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 348 ----------RTENWTDYRLNC-QMV----FqdPYSSldPRMTIE--ALVEEALrpvpgldgkakrkrtletlEEVGLGv 410
Cdd:COG4604 71 relakrlailRQENHINSRLTVrELVafgrF--PYSK--GRLTAEdrEIIDEAI-------------------AYLDLE- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 411 DYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRV 490
Cdd:COG4604 127 DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHI 206
|
250 260 270
....*....|....*....|....*....|...
gi 1681691554 491 VVMQDGRIIEEGdrdtifdSPKEAYTRRLLSAI 523
Cdd:COG4604 207 VAMKDGRVVAQG-------TPEEIITPEVLSDI 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-250 |
2.63e-23 |
|
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: 100.65 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 39 IVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKEnelrHLRGaeIGVVFQEpmTSLNPSMTIGRQLEEGLI 118
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLAGFEQPDSGSIMLDGEDVTNVPP----HLRH--INMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 119 LHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIqRDVMEL-M 197
Cdd:TIGR01187 69 MR-KVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKL-RDQMQLeL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 198 VELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPY 250
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-237 |
2.66e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDvLKMKENELRHLRgAEIGVVFQEP 99
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT----SGEVLIKGEP-IKYDKKSLLEVR-KTVGIVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSLNpSMTIGRQLEEGlILHTKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK13639 88 DDQLF-APTVEEDVAFG-PLNLGLSKEEVEKRVKEALKAVGM---EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-250 |
2.69e-23 |
|
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: 101.34 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIK--VADGSVSYKGRDVLKMKENELRhlrgaeIGVVFQEpmTSLN 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeiVLNGRTLFDSRKGIFLPPEKRR------IGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 105 PSMTIGRQLEEGLILHTKASAQERRSLILDMLkrvGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTA 184
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELL---GI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 185 LDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPY 250
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-233 |
3.11e-23 |
|
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: 96.73 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVAR-TGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVlkmKENELRHLRGAEI 92
Cdd:cd03215 5 LEVRGlSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP----ASGEITLDGKPV---TRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 93 GVVFQEPmtslnpsmtigrqLEEGLILhtkasaqeRRSLILDMlkrvgirdpegALSSYpheFSGGMRQRIMLASVMLLK 172
Cdd:cd03215 78 AYVPEDR-------------KREGLVL--------DLSVAENI-----------ALSSL---LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-256 |
3.29e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVADGSVSYKGrdvlKMKENELRHLRgAEIGVVFQE 98
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPrsgTLNIAGNHFDFSK----TPSDKAIRELR-RNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 pmTSLNPSMTIGRQLEE------GLilhTKASAQERRSLILDMLKRVGIRDpegalsSYPHEFSGGMRQRIMLASVMLLK 172
Cdd:PRK11124 91 --YNLWPHLTVQQNLIEapcrvlGL---SKDQALARAEKLLERLRLKPYAD------RFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELtraEGTAI--LLISHDLPMVARYTSRIVVMEKGAIVEKGrTEDLLKAPQHPY 250
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIREL---AETGItqVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQTEA 235
|
....*.
gi 1681691554 251 TKKLLS 256
Cdd:PRK11124 236 FKNYLS 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-518 |
7.06e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNC-------QMVFQDPYSS 369
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 ldPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRY---PHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 447 VSALDVTVRAQVLDLFSDLQKRygFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRR 518
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-256 |
7.95e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRAL--ISLLPPTIKVaDGSVSYKGRDVL--KMKENELRhlrgAEIGVV 95
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGARV-EGEILLDGEDIYdpDVDVVELR----RRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 96 FQEPmtslNP-SMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDpE--GALSSYPHEFSGGMRQRIMLASVMLLK 172
Cdd:COG1117 98 FQKP----NPfPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWD-EvkDRLKKSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTK 252
Cdd:COG1117 173 PEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
....
gi 1681691554 253 KLLS 256
Cdd:COG1117 251 DYIT 254
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-246 |
9.00e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.79 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmkenelRHLRGAEIGVVFQEpmTS 102
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT----EGQIFIDGEDVTH------RSIQQRDICMVFQS--YA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVgirDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPT 182
Cdd:PRK11432 89 LFPHMSLGENVGYGLKML-GVPKEERKQRVKEALELV---DLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 183 TALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
300-521 |
9.69e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.29 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLV-----TESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDPysslDPR 373
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKmDVIELRRRVQMVFQIP----NPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEALVEEALRPVPGLDGKAKRK---RTLETLEEVGLGVDYAGRY---PHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 448 SALDVTVRAQVLDLFSDLQKRygFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLS 521
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVT 246
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-268 |
1.14e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEnelrHLRgaEIGVVFQEp 99
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT----AGQIMLDGVDLSHVPP----YQR--PINMMFQS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLiLHTKASAQERRSLILDMLKRVGIRDPEGalsSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK11607 100 -YALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAK---RKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 180 EPTTALDAVIqRDVMEL-MVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKLLSSL 258
Cdd:PRK11607 175 EPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
250
....*....|...
gi 1681691554 259 P-FRG--RPRQID 268
Cdd:PRK11607 254 NvFEGvlKERQED 266
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
298-499 |
1.29e-22 |
|
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: 101.05 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES--EGRIQFQGRP-RTENWTDY-RLNCQMVFQDpySSLDPR 373
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPlKASNIRDTeRAGIVIIHQE--LTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEA---LVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:TIGR02633 93 LSVAEnifLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1681691554 451 DVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:TIGR02633 173 TEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-234 |
1.40e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSlevartGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkenE 83
Cdd:COG1129 254 EVVLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD----SGEIRLDGKPV------R 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGA-EIGVVF------QEpmtSLNPSMTIG--------RQLEEGLILHTKAsaqeRRSLILDMLKRVGIR--DPEG 146
Cdd:COG1129 318 IRSPRDAiRAGIAYvpedrkGE---GLVLDLSIRenitlaslDRLSRGGLLDRRR----ERALAEEYIKRLRIKtpSPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 147 ALSSypheFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIV 226
Cdd:COG1129 391 PVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISSELPELLGLSDRIL 465
|
....*...
gi 1681691554 227 VMEKGAIV 234
Cdd:COG1129 466 VMREGRIV 473
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
297-520 |
1.42e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEnWTDYRLNCQMVFQdPYSSLDPR-MT 375
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM-LSSRQLARRLALL-PQHHLTPEgIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALVEEALRPVPGLDGK---AKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:PRK11231 93 VRELVAYGRSPWLSLWGRlsaEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 453 TVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGdrdtifdSPKEAYTRRLL 520
Cdd:PRK11231 172 NHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
300-521 |
2.59e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.45 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLV-----TESEGRIQFQGR---PRTENWTDYRLNCQMVFQdpYSSLD 371
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRniySPDVDPIEVRREVGMVFQ--YPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMTIEALVEEALRpvpgLDGKAKRKRTLE-----TLEEVGLGVDYAGR---YPHELSGGQRQRVAIARAIARRPRFLIA 443
Cdd:PRK14267 98 PHLTIYDNVAIGVK----LNGLVKSKKELDervewALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 444 DEPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPKEAYTRRLLS 521
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVT 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
290-508 |
2.69e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.61 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 290 LFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenwTDY--------RLNCQM 361
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-----LDYskrgllalRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 362 VFQDP-----YSSLDPRMTIealveeALRPVpGLDGKAKRKRTLETLEEVGlgvdyAGRYPHE----LSGGQRQRVAIAR 432
Cdd:PRK13638 82 VFQDPeqqifYTDIDSDIAF------SLRNL-GVPEAEITRRVDEALTLVD-----AQHFRHQpiqcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 433 AIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-233 |
3.85e-22 |
|
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: 93.43 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELrh 86
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT----SGRVRLDGADISQWDPNEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 lrGAEIGVVFQEPmtslnpsmtigrQLEEGLIlhtkasaqerRSLILdmlkrvgirdpegalssyphefSGGMRQRIMLA 166
Cdd:cd03246 75 --GDHVGYLPQDD------------ELFSGSI----------AENIL----------------------SGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDlPMVARYTSRIVVMEKGAI 233
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
273-502 |
3.91e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.76 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrTENw 352
Cdd:PRK09536 2 PMIDVSDLSVEFGD----------TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD-VEA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLNCQMVFQDPY-SSLDPRMTIEALVEEALRPVPG---LDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRV 428
Cdd:PRK09536 70 LSARAASRRVASVPQdTSLSFEFDVRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVA-QFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 429 AIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
292-468 |
4.62e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.65 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 292 RKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESE---GRIQFQGRPRT-ENWTDyrlNCQMVFQDPY 367
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKpDQFQK---CVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 ssLDPRMTiealVEEALRPVPGL------DGKAKRKRT-LETLEEVGLGVdYAGRYPHELSGGQRQRVAIARAIARRPRF 440
Cdd:cd03234 92 --LLPGLT----VRETLTYTAILrlprksSDAIRKKRVeDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180
....*....|....*....|....*...
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKR 468
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARR 192
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
312-511 |
5.55e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 97.25 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 312 VVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR-----PRTENWTDYRLNCQMVFQDpySSLDPRMTIEAlveealrp 386
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaEKGICLPPEKRRIGYVFQD--ARLFPHYKVRG-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 387 vpGLDGKAKRKRTLETLEEVG-LGVDYA-GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSD 464
Cdd:PRK11144 96 --NLRYGMAKSMVAQFDKIVAlLGIEPLlDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 465 LQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
300-511 |
6.42e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrTENWTDYRLNCQMVF---QDPYSSldpRMTI 376
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-LESWSSKAFARKVAYlpqQLPAAE---GMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRPVPGLDGK---AKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVT 453
Cdd:PRK10575 103 RELVAIGRYPWHGALGRfgaADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 454 VRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-225 |
7.07e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLEVARTGQQ--VVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLK 78
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHElsILTGVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 79 MKENELRHLRGAEIGVVFQEPMtsLNPSMTIGRQLEEGLILHTKASAQERRSLIlDMLKRVGIrdpEGALSSYPHEFSGG 158
Cdd:PRK10584 77 MDEEARAKLRAKHVGFVFQSFM--LIPTLNALENVELPALLRGESSRQSRNGAK-ALLEQLGL---GKRLDHLPAQLSGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRI 225
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
22-228 |
7.33e-22 |
|
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: 94.38 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISllppTIKVADGSVSYKGR----DVLKMKENELRHLRGAEIGVVFQ 97
Cdd:TIGR02324 22 PVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYA----NYLPDSGRILVRHEgawvDLAQASPREVLEVRRKTIGYVSQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 epMTSLNPSMTIGRQLEEGLIL----HTKASAQERrslilDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKP 173
Cdd:TIGR02324 98 --FLRVIPRVSALEVVAEPLLErgvpREAARARAR-----ELLARLNI--PERLWHLPPATFSGGEQQRVNIARGFIADY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVM 228
Cdd:TIGR02324 169 PILLLDEPTASLDAANRQVVVELIAEA-KARGAALIGIFHDEEVRELVADRVMDV 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
303-523 |
9.03e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.22 E-value: 9.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR-----PRTENWTdYRLNCQMVFQDpySSLDPRMTIE 377
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamSRSRLYT-VRKRMSMLFQS--GALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 ALVEEALRPVPGLDGKAKRKRTLETLEEVGL-GVdyAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRA 456
Cdd:PRK11831 103 DNVAYPLREHTQLPAPLLHSTVMMKLEAVGLrGA--AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 457 QVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDSPkEAYTRRLLSAI 523
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-244 |
1.04e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTlaTraLISLLPPTIKVADGSVSYKGRDVLKMKEnelrHLRGAEIGVVFQEPMTS 102
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKS--T--LLNAIAGSLPPDSGSILIDGKDVTKLPE----YKRAKYIGRVFQDPMMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSMTIgrqlEEGLILHTK---------ASAQERRSLILDMLKRVG------IRDPEGALSsyphefsGGMRQRIMLas 167
Cdd:COG1101 93 TAPSMTI----EENLALAYRrgkrrglrrGLTKKRRELFRELLATLGlglenrLDTKVGLLS-------GGQRQALSL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 168 VM--LLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV------EKGR- 238
Cdd:COG1101 160 LMatLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIldvsgeEKKKl 239
|
....*..
gi 1681691554 239 -TEDLLK 244
Cdd:COG1101 240 tVEDLLE 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
292-511 |
1.23e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.03 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 292 RKNKPkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDPyssL 370
Cdd:TIGR00958 491 RPDVP--VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEP---V 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 DPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDY---AGRYPHELSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:TIGR00958 566 LFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 448 SALDvtvrAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:TIGR00958 646 SALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
288-507 |
1.50e-21 |
|
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: 97.95 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL--VTESEGRI----------------QFQGRP-- 347
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEPcp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 348 ---------RTENWT-------DYRLNCQMVFQDPYSSLDPRMTIEAlVEEALRPVpGLDGKAKRKRTLETLEEVGLGvd 411
Cdd:TIGR03269 84 vcggtlepeEVDFWNlsdklrrRIRKRIAIMLQRTFALYGDDTVLDN-VLEALEEI-GYEGKEAVGRAVDLIEMVQLS-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 412 yaGRYPH---ELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVAD 488
Cdd:TIGR03269 160 --HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*....
gi 1681691554 489 RVVVMQDGRIIEEGDRDTI 507
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-231 |
1.90e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 93.30 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKmkenelrhlRGAEIGVVFQEpmTSL 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLISGLAQPTSGGVILEGKQITE---------PGPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTIgRQ---LEEGLILHTkASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:TIGR01184 66 LPWLTV-REniaLAVDRVLPD-LSKSERRAIVEEHIALVGLTE---AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 181 PTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKG 231
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-243 |
2.45e-21 |
|
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: 93.06 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 19 TGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgAEIGVVFQE 98
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS----SGSILIDGQDIREVTLDSLR----RAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 pmTSL-NPsmTIGRQLEEGLIlhtKASAQErrslILDMLKRVGIRD-----PEGalssYPHE-------FSGGMRQRIML 165
Cdd:cd03253 84 --TVLfND--TIGYNIRYGRP---DATDEE----VIEAAKAAQIHDkimrfPDG----YDTIvgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 166 ASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
298-506 |
2.63e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 97.17 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVT--ESEGRIQFQGRPRTenwtdyrlncqmvFQDPYSS------ 369
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCR-------------FKDIRDSealgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 -------LDPRMTI-EALV---EEALRPVpgLDGKAKRKRTLETLEEVGLGVDyagryPHELSG----GQRQRVAIARAI 434
Cdd:NF040905 82 iihqelaLIPYLSIaENIFlgnERAKRGV--IDWNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 435 ARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDT 506
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
297-507 |
2.84e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTeSEGRIQFQGRPRTE-NWTDYRLNCQMVFQDP---YSSL-- 370
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRElDPESWRKHLSWVGQNPqlpHGTLrd 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 -----DPRMTIEALvEEALrpvpgldgkaKRKRTLETLEEVGLGVDY-----AGRypheLSGGQRQRVAIARAIARRPRF 440
Cdd:PRK11174 442 nvllgNPDASDEQL-QQAL----------ENAWVSEFLPLLPQGLDTpigdqAAG----LSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQVaDRVVVMQDGRIIEEGDRDTI 507
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
291-511 |
3.32e-21 |
|
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: 92.17 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPY-- 367
Cdd:cd03244 12 YRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiSKIGLHDLRSRISIIPQDPVlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 -----SSLDPR------MTIEALVEEALRPV-----PGLDGKakrkrtletLEEVGLGvdyagrypheLSGGQRQRVAIA 431
Cdd:cd03244 91 sgtirSNLDPFgeysdeELWQALERVGLKEFveslpGGLDTV---------VEEGGEN----------LSVGQRQLLCLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 432 RAIARRPRFLIADEPVSALDVTVRAQVLDL----FSDlqkrygfsC--LFISHDLGVVEQvADRVVVMQDGRIIEegdrd 505
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTireaFKD--------CtvLTIAHRLDTIID-SDRILVLDKGRVVE----- 217
|
....*.
gi 1681691554 506 tiFDSP 511
Cdd:cd03244 218 --FDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
292-497 |
3.42e-21 |
|
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: 91.76 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 292 RKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR----PRT---------ENwtdyrln 358
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvSQEpwiqngtirEN------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 359 cqMVFQDPYSSLDPRMTIEALveeALRP----VPGLDgkakrkrtlETleEVG-LGVDyagrypheLSGGQRQRVAIARA 433
Cdd:cd03250 86 --ILFGKPFDEERYEKVIKAC---ALEPdleiLPDGD---------LT--EIGeKGIN--------LSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLD--LFSDLQKryGFSCLFISHDLGVVEQvADRVVVMQDGR 497
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
297-507 |
3.77e-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: 97.03 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGrPRTENW-------------TDYRLNCQMV- 362
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG-ADLKQWdretfgkhigylpQDVELFPGTVa 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 363 -----FQDpysSLDPRMTIEAL----VEEALRPVPglDGKakrkrtletleEVGLGVDYAGrypheLSGGQRQRVAIARA 433
Cdd:TIGR01842 410 eniarFGE---NADPEKIIEAAklagVHELILRLP--DGY-----------DTVIGPGGAT-----LSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEGDRDTI 507
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDEV 540
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
275-502 |
5.11e-21 |
|
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: 90.45 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYagrkslfrKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTD 354
Cdd:cd03247 1 LSINNVSFSY--------PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 355 YRLNCQMVFQDPYssldprmtieaLVEEALRpvpgldgkakrkrtletlEEVGLgvdyagryphELSGGQRQRVAIARAI 434
Cdd:cd03247 73 LSSLISVLNQRPY-----------LFDTTLR------------------NNLGR----------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 435 ARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEG 502
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
268-509 |
5.69e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 268 DLTSVPMISARDIIVDYAGrkslfrknkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP 347
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSG----------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 348 RTeNWTD---YRLNCQMVFQDPYssLDPRMTIEalvEEALRpvpGLDGKAKRKRTLETL-EEVGLGVDyagryPHELSG- 422
Cdd:PRK15439 75 CA-RLTPakaHQLGIYLVPQEPL--LFPNLSVK---ENILF---GLPKRQASMQKMKQLlAALGCQLD-----LDSSAGs 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 423 ---GQRQRVAIARAIARRPRFLIADEPVSALdvtVRAQVLDLFSDLQK--RYGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:PRK15439 141 levADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
250
....*....|..
gi 1681691554 498 IIEEGDRDTIFD 509
Cdd:PRK15439 218 IALSGKTADLST 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-237 |
6.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKT----LATRALISLLPPTIkVADgsvsYKGRDVLKmKENELRHLRgAEIGVVFQ 97
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKStmiqLTNGLIISETGQTI-VGD----YAIPANLK-KIKEVKRLR-KEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMTSLNPSmTIGRQLEEGLIlHTKASAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK13645 98 FPEYQLFQE-TIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-244 |
6.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmKENELRHLRgAEIGVVFQEPMTSL 103
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK----SGEIFYNNQAI---TDDNFEKLR-KHIGIVFQNPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMT---IGRQLEEGLILHTKASAQERRSLI-LDMLKRvgiRDPEgalssyPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK13648 97 VGSIVkydVAFGLENHAVPYDEMHRRVSEALKqVDMLER---ADYE------PNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDL--PMVARYtsrIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLseAMEADH---VIVMNKGTVYKEGTPTEIFD 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-245 |
9.57e-21 |
|
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: 95.59 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTIkvadGSVSYKGRDVLKMKENELr 85
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKsTLA-RLLVGVWPPTA----GSVRLDGADLSQWDREEL- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 86 hlrGAEIGVVFQEPmtslnpsmtigrQLEEGLI-----LHTKASAQErrslILDMLKRVGIRD-----PEG---ALSSYP 152
Cdd:COG4618 405 ---GRHIGYLPQDV------------ELFDGTIaeniaRFGDADPEK----VVAAAKLAGVHEmilrlPDGydtRIGEGG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 153 HEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDlPMVARYTSRIVVMEKGA 232
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHR-PSLLAAVDKLLVLRDGR 543
|
250
....*....|...
gi 1681691554 233 IVEKGRTEDLLKA 245
Cdd:COG4618 544 VQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-237 |
1.01e-20 |
|
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: 90.73 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaEIGVVFQEPMT- 101
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT----SGSVLLDGTDIRQLDPADLRR----NIGYVPQDVTLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 --SLNPSMTIGRQleeglilhtkaSAQERRslILDMLKRVGI-----RDPEG---ALSSYPHEFSGGMRQRIMLASVMLL 171
Cdd:cd03245 91 ygTLRDNITLGAP-----------LADDER--ILRAAELAGVtdfvnKHPNGldlQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELTRaeGTAILLISHDLPMVArYTSRIVVMEKGAIVEKG 237
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-237 |
1.10e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 91.24 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgaEIGVVF-QEPMT 101
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT----SGEVRVAGLVPWKRRKKFLR-----RIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLN-PSMtigrqleEGLILH------TKASAQERRSLILDMLkrvgirDPEGALSSYPHEFSGGMRQRIMLASVMLLKPA 174
Cdd:cd03267 107 WWDlPVI-------DSFYLLaaiydlPPARFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-245 |
1.41e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGK-TLaTRALISLLPPTikvaDGSVSYKGRdvlkmkenelrhlrgaeIGVVFqEPMT 101
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKsTL-LKLIAGILEPT----SGRVEVNGR-----------------VSALL-ELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTiGRQLEE--GLIL-HTKASAQERRSLILDMlkrVGIRD----PEGALSSyphefsgGMRQRIMLASVMLLKPA 174
Cdd:COG1134 98 GFHPELT-GRENIYlnGRLLgLSRKEIDEKFDEIVEF---AELGDfidqPVKTYSS-------GMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-237 |
1.41e-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: 89.29 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMkENELRHLrgaeIGVVFQEPM 100
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSL----ISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 ---TSLnpsmtigrqleeglilhtkasaqerrslildmLKRVGIRdpegalssypheFSGGMRQRIMLASVMLLKPALLI 177
Cdd:cd03247 86 lfdTTL--------------------------------RNNLGRR------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVArYTSRIVVMEKGAIVEKG 237
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEV--LKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-237 |
1.48e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.90 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtralisllpPTI------KVADGSVSYKGRDVLKM 79
Cdd:COG0396 1 LEIKNLHVSVE--GKEILKGVNLTIKPGEVHAIMGPNGSGKsTLA---------KVLmghpkyEVTSGSILLDGEDILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 80 KENElRHLRGaeIGVVFQEP--------MTSLNPSMTIGRQLEEglilhtkaSAQERRSLILDMLKRVGIrdPEGALSSY 151
Cdd:COG0396 70 SPDE-RARAG--IFLAFQYPveipgvsvSNFLRTALNARRGEEL--------SAREFLKLLKEKMKELGL--DEDFLDRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 152 PHE-FSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHdlpmvarYT-------- 222
Cdd:COG0396 137 VNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITH-------YQrildyikp 208
|
250
....*....|....*
gi 1681691554 223 SRIVVMEKGAIVEKG 237
Cdd:COG0396 209 DFVHVLVDGRIVKSG 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-242 |
1.92e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.82 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 5 KLLTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENEL 84
Cdd:PRK11300 4 PLLSVSGLMMRFG--GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPT----GGTILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 85 rhlrgAEIGVV--FQEpmTSLNPSMTI--------GRQLEEGLI---LHTKA------SAQERRSLILDmlkRVGIRD-- 143
Cdd:PRK11300 78 -----ARMGVVrtFQH--VRLFREMTVienllvaqHQQLKTGLFsglLKTPAfrraesEALDRAATWLE---RVGLLEha 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 144 --PEGALSsYphefsgGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARY 221
Cdd:PRK11300 148 nrQAGNLA-Y------GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGI 220
|
250 260
....*....|....*....|.
gi 1681691554 222 TSRIVVMEKGAIVEKGRTEDL 242
Cdd:PRK11300 221 SDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-234 |
2.16e-20 |
|
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: 88.25 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmkeNELRHLRGAEIGVVFQep 99
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD----SGEILVDGKEVSF---ASPRDARRAGIAMVYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtslnpsmtigrqleeglilhtkasaqerrslildmlkrvgirdpegalssypheFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:cd03216 83 -------------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 180 EPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV 234
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-237 |
2.27e-20 |
|
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: 89.86 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEP 99
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS----SGSILIDGVDISKIGLHDLRSR----ISIIPQDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtslnpsmtigrQLEEGLI-----LHTKASAQErrslILDMLKRVGIRD----PEGALSSYPHE----FSGGMRQRIMLA 166
Cdd:cd03244 88 ------------VLFSGTIrsnldPFGEYSDEE----LWQALERVGLKEfvesLPGGLDTVVEEggenLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 167 SVMLLKPALLIADEPTTALD----AVIQRDVMELMVELTraegtaILLISHDLPMVARYtSRIVVMEKGAIVEKG 237
Cdd:cd03244 152 RALLRKSKILVLDEATASVDpetdALIQKTIREAFKDCT------VLTIAHRLDTIIDS-DRILVLDKGRVVEFD 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
291-502 |
2.32e-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: 89.15 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES--EGRIQFQGRPRTENWtdYRLNCQMVFQDPYs 368
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRS--FRKIIGYVPQDDI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 sLDPRMTiealVEEALRPVPGLDGkakrkrtletleevglgvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:cd03213 93 -LHPTLT----VRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 449 ALDVTVRAQVLDLFSDLQKRyGFSCLFISHDL-GVVEQVADRVVVMQDGRIIEEG 502
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-246 |
2.34e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIkvadGSVSYKGRDVLKMKENELrh 86
Cdd:PRK09536 4 IDVSDLS--VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA----GTVLVAGDDVEALSARAA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 lrGAEIGVVFQEpmTSLNPSMTIGRQLEEGLILHTK---ASAQERRSLILDMLKRVGIrdpeGALSSYP-HEFSGGMRQR 162
Cdd:PRK09536 76 --SRRVASVPQD--TSLSFEFDVRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGV----AQFADRPvTSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLIsHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
....
gi 1681691554 243 LKAP 246
Cdd:PRK09536 227 LTAD 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-244 |
2.35e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVADGSVSYKGRdvlkmkenelrhLRGAEIGVVF 96
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdagKITVLGVPVPARAR------------LARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QepMTSLNPSMTIgrqlEEGLILHTK---ASAQERRSLILDMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKP 173
Cdd:PRK13536 121 Q--FDNLDLEFTV----RENLLVFGRyfgMSTREIEAVIPSLLEFARLESKADARVS---DLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-237 |
2.44e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPT---IKVADGSVSYKGRDVLKMKENelrhlrgaeIGVVF 96
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSsgrILFDGKPIDYSRKGLMKLRES---------VGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEPMTSLNpSMTIGRQLEEGlILHTKASAQERRSLILDMLKRVGIrdpeGALSSYP-HEFSGGMRQRIMLASVMLLKPAL 175
Cdd:PRK13636 89 QDPDNQLF-SASVYQDVSFG-AVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 176 LIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-237 |
3.00e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGK-TLATR--ALISLLPPTIKVADGSVSYKGRDVLKMKENELRHLRGAE-----IGV 94
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKsTLVTHfnGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 95 VFQEPMTSLNPSmTIGRQLEEGLIlHTKASAQERRSLILDMLKRVGIRDPegALSSYPHEFSGGMRQRIMLASVMLLKPA 174
Cdd:PRK13631 121 VFQFPEYQLFKD-TIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVElTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-225 |
4.33e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIkvadGSVsykgrdvlkmkenelRHLRGAEIGVVFQEp 99
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS----GTV---------------RRAGGARVAYVPQR- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPS--------MTIGRQLEEGLILHTKASAqerRSLILDMLKRVGIRDPEG-ALSsyphEFSGGMRQRIMLASVML 170
Cdd:NF040873 64 -SEVPDSlpltvrdlVAMGRWARRGLWRRLTRDD---RAAVDDALERVGLADLAGrQLG----ELSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 171 LKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRI 225
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-258 |
4.41e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKM-KENELRHLrgaeIGVVFQE 98
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ----KGKVLVSGIDTGDFsKLQGIRKL----VGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PMTSLnpsmtIGRQLEEGLilhtkASAQERRSLI-LDMLKRVGIRDPEGALSSY----PHEFSGGMRQRIMLASVMLLKP 173
Cdd:PRK13644 86 PETQF-----VGRTVEEDL-----AFGPENLCLPpIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKK 253
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
....*
gi 1681691554 254 LLSSL 258
Cdd:PRK13644 234 TPPSL 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-244 |
4.45e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENEL-RHLrgaei 92
Cdd:PRK11231 8 LTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ----SGTVFLGDKPISMLSSRQLaRRL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 93 GVVFQEPMTslnPSMTIGRQL-EEG----LILHTKASaQERRSLILDMLKRVGIRD-PEGALSsyphEFSGGMRQRIMLA 166
Cdd:PRK11231 79 ALLPQHHLT---PEGITVRELvAYGrspwLSLWGRLS-AEDNARVNQAMEQTRINHlADRRLT----DLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGR-----TED 241
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmTPG 229
|
...
gi 1681691554 242 LLK 244
Cdd:PRK11231 230 LLR 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-215 |
5.59e-20 |
|
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: 93.19 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 19 TGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgAEIGVVFQE 98
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL----QGEVTLDGVPVSSLDQDEVR----RRVSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PM---TSLNPSMTIGRQleeglilhtKASAQErrslILDMLKRVG----IRDPEGALSSYPHE----FSGGMRQRIMLAS 167
Cdd:TIGR02868 418 AHlfdTTVRENLRLARP---------DATDEE----LWAALERVGladwLRALPDGLDTVLGEggarLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVMELMVELTraEGTAILLISHDL 215
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
300-490 |
5.86e-20 |
|
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: 87.93 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQmvfqdpYSSLDPRMTIEAL 379
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL------YLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 VEEALRPVPGLDGkakRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVL 459
Cdd:cd03231 90 VLENLRFWHADHS---DEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180 190
....*....|....*....|....*....|.
gi 1681691554 460 DLFSDLQKRYGFSCLFISHDLGVVEQVADRV 490
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-243 |
6.91e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 28 SFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDvlkmkenelrHLRGA----EIGVVFQEpmTSL 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGFLTPASGSLTLNGQD----------HTTTPpsrrPVSMLFQE--NNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 NPSMTIGRQLeeGLILHT--KASAQERRSLIlDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PRK10771 83 FSHLTVAQNI--GLGLNPglKLNAAQREKLH-AIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 182 TTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
299-521 |
7.11e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL--VTES---EGRIQFQGRPRTENWTD---YRLNCQMVFQDPYS-- 368
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDVDpveVRRRIGMVFQKPNPfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 -------SLDPRMT-----IEALVEEALRPVPGLDgKAKRKrtletLEEVGLGvdyagrypheLSGGQRQRVAIARAIAR 436
Cdd:PRK14243 105 ksiydniAYGARINgykgdMDELVERSLRQAALWD-EVKDK-----LKQSGLS----------LSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 437 RPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYgfSCLFISHDLGVVEQVADRVVVM---------QDGRIIEEGDRDTI 507
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKI 246
|
250
....*....|....
gi 1681691554 508 FDSPKEAYTRRLLS 521
Cdd:PRK14243 247 FNSPQQQATRDYVS 260
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
298-484 |
7.72e-20 |
|
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: 87.80 E-value: 7.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPysSLDPRMTie 377
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP--GLKPELS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 alVEEALRPVPGLDGKAKRKrTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQ 457
Cdd:TIGR01189 90 --ALENLHFWAAIHGGAQRT-IEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|....*..
gi 1681691554 458 VLDLFSDLQKRYGFSCLFISHDLGVVE 484
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-228 |
7.80e-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: 92.73 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgAEIGVVFQepmts 102
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT----EGSIAVNGVPLADADADSWR----DQIAWVPQ----- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 lNPSMTIGRQLEEglILHTKASAQErrSLILDMLKRVGIRD-----PEGA---LSSYPHEFSGGMRQRIMLASVMLLKPA 174
Cdd:TIGR02857 404 -HPFLFAGTIAEN--IRLARPDASD--AEIREALERAGLDEfvaalPQGLdtpIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYtSRIVVM 228
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
296-502 |
8.45e-20 |
|
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: 92.96 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRA-LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDP------- 366
Cdd:COG5265 369 PERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDiRDVTQASLRAAIGIVPQDTvlfndti 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 -----YSSLDPRmtiEALVEEALRP------VPGL-DGkakrkrtLETL-EEVGLgvdyagryphELSGGQRQRVAIARA 433
Cdd:COG5265 449 ayniaYGRPDAS---EEEVEAAARAaqihdfIESLpDG-------YDTRvGERGL----------KLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLG-VVEqvADRVVVMQDGRIIEEG 502
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStIVD--ADEILVLEAGRIVERG 574
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-240 |
1.00e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 87.20 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVArtGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLlpPTIKVADGSVSYKGRDVLKMKENElR 85
Cdd:cd03217 1 LEIKDLHVSVG--GKEILKGVNLTIKKGEVHALMGPNGSGKsTLA-KTIMGH--PKYEVTEGEILFKGEDITDLPPEE-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 86 HLRGaeIGVVFQEPMTSlnPSMTIGrqleeglilhtkasaqerrslilDMLKRVGirdpEGalssypheFSGGMRQRIML 165
Cdd:cd03217 75 ARLG--IFLAFQYPPEI--PGVKNA-----------------------DFLRYVN----EG--------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 166 ASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHdLPMVARY--TSRIVVMEKGAIVEKGRTE 240
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
301-526 |
1.40e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 301 HGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRpRTENWTDYRLNCQMVFQDPYSSLDPRMTIEALV 380
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-HIQHYASKEVARRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 381 EEALRPVPGLDGKAKRK---RTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQ 457
Cdd:PRK10253 103 ARGRYPHQPLFTRWRKEdeeAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 458 VLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGdrdtifdSPKEAYTRRLLSAIPAL 526
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERIYGL 243
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-237 |
2.25e-19 |
|
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: 86.78 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 29 FDL--APGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENElrhlrgAEIGVVFQEpmTSLNPS 106
Cdd:cd03298 17 FDLtfAQGEITAIVGPSGSGKS----TLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIGRQLEEGLILHTKASAQERRSlILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALD 186
Cdd:cd03298 85 LTVEQNVGLGLSPGLKLTAEDRQA-IEVALARVGL---AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 187 AVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-245 |
2.64e-19 |
|
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: 91.32 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKeneLRHLRgA 90
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR-R 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 EIGVVFQEPM---TSLNPSMTIGRqleegliLHTKASAQERRSLILDMLKRVGIRDPEG---ALSSYPHEFSGGMRQRIM 164
Cdd:TIGR02203 407 QVALVSQDVVlfnDTIANNIAYGR-------TEQADRAEIERALAAAYAQDFVDKLPLGldtPIGENGVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTaiLLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
.
gi 1681691554 245 A 245
Cdd:TIGR02203 557 R 557
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-233 |
2.67e-19 |
|
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: 86.76 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDvLKMKENELRHlrgAEIGVVFQ 97
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ----GGQVLLDGKP-ISQYEHKYLH---SKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMT---SLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKrvGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKPA 174
Cdd:cd03248 96 EPVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELAS--GYDTEVGEKGS---QLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVEltRAEGTAILLISHDLPMVARyTSRIVVMEKGAI 233
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
274-464 |
2.94e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.01 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 274 MISARDIIVDYAGRKsLFrknkpkralHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWT 353
Cdd:PRK13538 1 MLEARNLACERDERI-LF---------SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYrlNCQMVFQDPYSSLDPRMTiealVEEALRPVPGLDGKAKRKRTLETLEEVGLgvdyAGR--YP-HELSGGQRQRVAI 430
Cdd:PRK13538 71 EY--HQDLLYLGHQPGIKTELT----ALENLRFYQRLHGPGDDEALWEALAQVGL----AGFedVPvRQLSAGQQRRVAL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1681691554 431 AR-AIARRPrfL-IADEPVSALDVTVRAQVLDLFSD 464
Cdd:PRK13538 141 ARlWLTRAP--LwILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-258 |
3.02e-19 |
|
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: 87.06 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 16 VARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLL----PPTikvADGSVSYKGRDvlKMKEN--ELRHLrg 89
Cdd:COG1119 11 VRRGGKTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLItgdlPPT---YGNDVRLFGER--RGGEDvwELRKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 90 aeIGVVFQEPMTSLNPSMT------------IGrqleegliLHTKASAQERRsLILDMLKRVGIRD----PEGALSSyph 153
Cdd:COG1119 80 --IGLVSPALQLRFPRDETvldvvlsgffdsIG--------LYREPTDEQRE-RARELLELLGLAHladrPFGTLSQ--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 efsgGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:COG1119 146 ----GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250 260
....*....|....*....|....*
gi 1681691554 234 VEKGRTEDLLkapqhpyTKKLLSSL 258
Cdd:COG1119 222 VAAGPKEEVL-------TSENLSEA 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-261 |
3.98e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.51 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLevARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMK 80
Cdd:PRK11831 2 QSVANLVDMRGVSF--TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD----HGEILFDGENIPAMS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 81 ENELRHLRgAEIGVVFQEP--MTSLNPSMTIGRQLEEglilHTKASAQERRSLILDMLKRVGIRdpeGALSSYPHEFSGG 158
Cdd:PRK11831 76 RSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLR---GAAKLMPSELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGR 238
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250 260
....*....|....*....|....*...
gi 1681691554 239 TEDlLKAPQHPYTKKLLSSL-----PFR 261
Cdd:PRK11831 228 AQA-LQANPDPRVRQFLDGIadgpvPFR 254
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-239 |
4.37e-19 |
|
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: 86.07 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 29 FDL--APGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENElrhlrgAEIGVVFQEpmTSLNPS 106
Cdd:TIGR01277 17 FDLnvADGEIVAIMGPSGAGKS----TLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIGRQLEEGLILHTKASAQERRSlILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALD 186
Cdd:TIGR01277 85 LTVRQNIGLGLHPGLKLNAEQQEK-VVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 187 AVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRT 239
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-238 |
4.40e-19 |
|
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: 85.54 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKeneLRH 86
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE----EGKIEIDGIDISTIP---LED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGAeIGVVFQEPMtslnpsmtigrqleegLILHTKASAQERRSLILDMLKRVGIRDPEGALSsypheFSGGMRQRIMLA 166
Cdd:cd03369 80 LRSS-LTIIPQDPT----------------LFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLN-----LSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 167 SVMLLKPALLIADEPTTALD----AVIQRDVMELMveltraEGTAILLISHDLPMVARYtSRIVVMEKGAIVEKGR 238
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDyatdALIQKTIREEF------TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-245 |
4.53e-19 |
|
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: 86.06 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 29 FDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVAdGSVSYKGRdvlkmkenelrhlrgAEIGVVFQE------- 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPakgTVKVA-GASPGKGW---------------RHIGYVPQRhefawdf 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PMTSLNPSMTiGRQleeGLILHTKASAQERRSLILDMLKRVGIRDpegaLSSYP-HEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:TIGR03771 65 PISVAHTVMS-GRT---GHIGWLRRPCVADFAAVRDALRRVGLTE----LADRPvGELSGGQRQRVLVARALATRPSVLL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIVVMeKGAIVEKGRTEDLLKA 245
Cdd:TIGR03771 137 LDEPFTGLDMPTQELLTELFIELA-GAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDP 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
299-508 |
4.54e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 87.25 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPrtenwTDYRLNCQMVFQDPYSSlDPRMTIEA 378
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-----TRQALQKNLVAYVPQSE-EVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEAL------------RPVPgldgkAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:PRK15056 96 LVEDVVmmgryghmgwlrRAKK-----RDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 447 VSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADrVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
298-501 |
4.81e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.47 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEnWTDYRLNCQMVFQDPYS-SLDPRMTi 376
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKIMREAVAIVPEGrRVFSRMT- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 ealVEEALrpvpGLDG-KAKRKRTLETLEEV-GLGVDYAGRYPHE---LSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:PRK11614 97 ---VEENL----AMGGfFAERDQFQERIKWVyELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 452 VTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEE 501
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-492 |
6.00e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.25 E-value: 6.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 33 PGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSykgrdvlkmKENELRHLRGAEIGVVFQ-----EPMTSLNPSM 107
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS---------WDEVLKRFRGTELQNYFKklyngEIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 108 ----------TIGRQLEEglilhtkasAQERRSLiLDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK13409 169 vdlipkvfkgKVRELLKK---------VDERGKL-DEVVERLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDaVIQR-DVMELMVELtrAEGTAILLISHDLpMVARYTSRIVVM---EKGA--IVekgrtedllkapQHP-- 249
Cdd:PRK13409 236 FDEPTSYLD-IRQRlNVARLIREL--AEGKYVLVVEHDL-AVLDYLADNVHIaygEPGAygVV------------SKPkg 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 250 -------YTKKLLSSLPFRGRPRQI--DLTSVPMISARDIIVDYagrkSLFRKNKPKRALHGVSIDIHEGEVVALVGGSG 320
Cdd:PRK13409 300 vrvgineYLKGYLPEENMRIRPEPIefEERPPRDESERETLVEY----PDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 321 SGKTTLGRTIAGLVTESEGRIQFQGR----PRtenwtdyrlncqmvfqdpYSSLDPRMTIEALVEEAlrpVPGLDGK--- 393
Cdd:PRK13409 376 IGKTTFAKLLAGVLKPDEGEVDPELKisykPQ------------------YIKPDYDGTVEDLLRSI---TDDLGSSyyk 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 394 ---AKRKRtLETLEEvglgvdyagRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYG 470
Cdd:PRK13409 435 seiIKPLQ-LERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERE 504
|
490 500
....*....|....*....|..
gi 1681691554 471 FSCLFISHDLGVVEQVADRVVV 492
Cdd:PRK13409 505 ATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
294-506 |
7.98e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 7.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 294 NKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLgrtiAGLVTE----SEGRIQFQGRPRTEnWTDYRLNCQM--VFQDPY 367
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTRawdpQQGEILLNGQPIAD-YSEAALRQAIsvVSQRVH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 ---SSL-------DPRMTIEALVEeALRPVpgldgkakrkrTLETLEEVGLGVDY----AGRyphELSGGQRQRVAIARA 433
Cdd:PRK11160 425 lfsATLrdnlllaAPNASDEALIE-VLQQV-----------GLEKLLEDDKGLNAwlgeGGR---QLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEGDRDT 506
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-244 |
9.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 86.34 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEN-ELRHLRgAEIGVVFQEPMTslnp 105
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT----QGSVRVDDTLITSTSKNkDIKQIR-KKVGLVFQFPES---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 106 smtigrQLEEGLILHTKA--------SAQERRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK13649 97 ------QLFEETVLKDVAfgpqnfgvSQEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRAeGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-246 |
1.28e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmKENELRHLRgAEIGVVFQ 97
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT----GGQVLLDGVPL---VQYDHHYLH-RQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMT---SLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKrvGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKPA 174
Cdd:TIGR00958 563 EPVLfsgSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN--GYDTEVGEKGS---QLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMveltRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESR----SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
238-502 |
1.46e-18 |
|
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: 89.42 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 238 RTEDLLKAPQHPYTKKLLSSLPFRGRprqidltsvpmISARDIIVDYagrkslfRKNKPKrALHGVSIDIHEGEVVALVG 317
Cdd:TIGR01846 430 RLGDILNSPTEPRSAGLAALPELRGA-----------ITFENIRFRY-------APDSPE-VLSNLNLDIKPGEFIGIVG 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 318 GSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE---NWtdYRLNCQMVFQ----------DPYSSLDPRMTIEALVEEAl 384
Cdd:TIGR01846 491 PSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIadpAW--LRRQMGVVLQenvlfsrsirDNIALCNPGAPFEHVIHAA- 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 385 RPVPGLDGKAKRKRTLET-LEEVGLGvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFS 463
Cdd:TIGR01846 568 KLAGAHDFISELPQGYNTeVGEKGAN----------LSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMR 637
|
250 260 270
....*....|....*....|....*....|....*....
gi 1681691554 464 DLQKryGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEG 502
Cdd:TIGR01846 638 EICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-268 |
1.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENE 83
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPD----DNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRgAEIGVVFQEPMTSLnPSMTIGRQLEEGLiLHTKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRI 163
Cdd:PRK13640 79 VWDIR-EKVGIVFQNPDNQF-VGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLD---YIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 164 MLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMvARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIF 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1681691554 244 KAPQH--------PYTKKLLSSLPFRG--RPRQID 268
Cdd:PRK13640 232 SKVEMlkeigldiPFVYKLKNKLKEKGisVPQEIN 266
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-267 |
1.64e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHLRGAEIGVVFQEpmT 101
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQR--Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLEEGLIlHTKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PRK10535 96 HLLSHLTAAQNVEVPAV-YAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 182 TTALDAVIQRDVMELMVELtRAEGTAILLISHDlPMVARYTSRIVVMEKGAIVEKGRTEdllkaPQHPYTKKLLSSLPFR 261
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQ-----EKVNVAGGTEPVVNTA 244
|
....*.
gi 1681691554 262 GRPRQI 267
Cdd:PRK10535 245 SGWRQF 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-492 |
1.68e-18 |
|
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: 88.69 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 33 PGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYKgrDVLKmkenelrHLRGAEIGVVFQ-----EPMTSLNPSM 107
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWD--EVLK-------RFRGTELQDYFKklangEIKVAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 108 ----------TIGRQLEeglilhtkaSAQERRSLiLDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:COG1245 169 vdlipkvfkgTVRELLE---------KVDERGKL-DELAEKLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDaVIQR-DVMELMVELTRaEGTAILLISHDLP---MVARYtsrIVVM--EKGA--IVEKGRTedlLKAPQHP 249
Cdd:COG1245 236 FDEPSSYLD-IYQRlNVARLIRELAE-EGKYVLVVEHDLAildYLADY---VHILygEPGVygVVSKPKS---VRVGINQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 250 YTKKLLSSLPFRGRPRQI--DLTSVPMISARDIIVDYagrkSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLG 327
Cdd:COG1245 308 YLDGYLPEENVRIRDEPIefEVHAPRREKEEETLVEY----PDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 328 RTIAGLVTESEGRIQFQGR----PrtenwtdyrlncQMVFQDpyssldprmtIEALVEEALRPV--PGLDGK------AK 395
Cdd:COG1245 384 KILAGVLKPDEGEVDEDLKisykP------------QYISPD----------YDGTVEEFLRSAntDDFGSSyykteiIK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 396 RKRtLETLEEvglgvdyagRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLF 475
Cdd:COG1245 442 PLG-LEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMV 511
|
490
....*....|....*..
gi 1681691554 476 ISHDLGVVEQVADRVVV 492
Cdd:COG1245 512 VDHDIYLIDYISDRLMV 528
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
288-502 |
1.71e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKP-KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLV---TESEGRIQFQGRPRTENwtDYRLNCQMVF 363
Cdd:TIGR00955 28 RGCFCRERPrKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPIDAK--EMRAISAYVQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 364 QDpySSLDPRMTI-EALVEEA-LRPVPGLDGKAKRKRTLETLEEVGLG------VDYAGRYpHELSGGQRQRVAIARAIA 435
Cdd:TIGR00955 106 QD--DLFIPTLTVrEHLMFQAhLRMPRRVTKKEKRERVDEVLQALGLRkcantrIGVPGRV-KGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 436 RRPRFLIADEPVSALDVTVRAQVLDLFSDL------------QKRYGFSCLFishdlgvveqvaDRVVVMQDGRIIEEG 502
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaqkgktiictihQPSSELFELF------------DKIILMAEGRVAYLG 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-244 |
1.99e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPT---IKVADGSVSYKGrdvlkmKENELRHLRgAEIGVVFQEPMTsl 103
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkVTVGDIVVSSTS------KQKEIKPVR-KKVGVVFQFPES-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 npsmtigrQLEEGLILHTKA--------SAQERRSLILDMLKRVGIRDPEGALSsyPHEFSGGMRQRIMLASVMLLKPAL 175
Cdd:PRK13643 96 --------QLFEETVLKDVAfgpqnfgiPKEKAEKIAAEKLEMVGLADEFWEKS--PFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 176 LIADEPTTALDAVIQRDVMELMvELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-246 |
3.27e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.29 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 12 LSLEVARTGQ-----QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMkenelrH 86
Cdd:PRK10851 1 MSIEIANIKKsfgrtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT----SGHIRFHGTDVSRL------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGAEIGVVFQEpmTSLNPSMTIGRQLEEGLIL---HTKASAQERRSLILDMLKRVGIrdpeGALSS-YPHEFSGGMRQR 162
Cdd:PRK10851 71 ARDRKVGFVFQH--YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL----AHLADrYPAQLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 163 IMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
....
gi 1681691554 243 LKAP 246
Cdd:PRK10851 225 WREP 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-237 |
3.50e-18 |
|
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: 83.35 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMkenelrhlrgaeigvvfqEPMT 101
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD----SGTVTVRGRVSSLL------------------GLGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTiGRQ--LEEGLIL-HTKASAQERRSLILDM--LKRVgIRDPEGALSSyphefsgGMRQRIMLASVMLLKPALL 176
Cdd:cd03220 94 GFNPELT-GREniYLNGRLLgLSRKEIDEKIDEIIEFseLGDF-IDLPVKTYSS-------GMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
272-480 |
3.60e-18 |
|
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: 87.42 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 272 VPMISARDIIVDYAGRKslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTEN 351
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAP---------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 352 WTDYRLNCQMVF-QDPYssldprmTIEALVEEALRPVpglDGKAKRKRTLETLEEVGLGvDYAGRYPH-----------E 419
Cdd:TIGR02868 403 DQDEVRRRVSVCaQDAH-------LFDTTVRENLRLA---RPDATDEELWAALERVGLA-DWLRALPDgldtvlgeggaR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 420 LSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVL-DLFSDLQKRygfSCLFISHDL 480
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSGR---TVVLITHHL 530
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
273-463 |
3.77e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVdYAGRKSLFRknkpkralhGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGrprtENW 352
Cdd:PRK13539 1 MMLEGEDLAC-VRGGRVLFS---------GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLNCQMVFQDPYSSLDPRMTiealVEEALRPVPGLDGkAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIAR 432
Cdd:PRK13539 67 DDPDVAEACHYLGHRNAMKPALT----VAENLEFWAAFLG-GEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALAR 140
|
170 180 190
....*....|....*....|....*....|..
gi 1681691554 433 -AIARRPRFLIaDEPVSALDVTVRAQVLDLFS 463
Cdd:PRK13539 141 lLVSNRPIWIL-DEPTAALDAAAVALFAELIR 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
296-503 |
3.84e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR--PRTENWTDYRLNCQMVFQ-----DPYS 368
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQLGIGIIYQelsviDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 SLDpRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPhELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:PRK09700 97 VLE-NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 449 ALdvtVRAQVLDLFSDLQ--KRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGD 503
Cdd:PRK09700 175 SL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
297-491 |
4.03e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRprtenwtdyrLNCQMVFQDPYssLDPrmTI 376
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIGYVPQKLY--LDT--TL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRPVPGLdgkaKRKRTLETLEEVGLGvdYAGRYP-HELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR 455
Cdd:PRK09544 83 PLTVNRFLRLRPGT----KKEDILPALKRVQAG--HLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1681691554 456 AQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVV 491
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-262 |
4.74e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLrgaeIGVVFQ 97
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT----SGSVLIRGEPITKENIREVRKF----VGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMTSL-NPSMT-------IGRQLEEGLILHTKASAqerrslildmLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVM 169
Cdd:PRK13652 86 NPDDQIfSPTVEqdiafgpINLGLDEETVAHRVSSA----------LHMLGLEE---LRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 170 LLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ-- 247
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDll 232
|
250 260
....*....|....*....|.
gi 1681691554 248 ------HPYTKKLLSSLPFRG 262
Cdd:PRK13652 233 arvhldLPSLPKLIRSLQAQG 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-245 |
4.91e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVLKMKENELrhlrGA 90
Cdd:PRK10253 10 GEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP----AHGHVWLDGEHIQHYASKEV----AR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 EIGVVFQEPMTSLNpsMTIGRQLEEGLILHTKASAQERR---SLILDMLKRVGIRDPegALSSYpHEFSGGMRQRIMLAS 167
Cdd:PRK10253 82 RIGLLAQNATTPGD--ITVQELVARGRYPHQPLFTRWRKedeEAVTKAMQATGITHL--ADQSV-DTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-523 |
5.69e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.77 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGK-TLatralisllpptIKVADGsV----SYKGRDVLKMKENELRHLRGAE---IGVVFQE 98
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKsTL------------MKVLSG-VyphgSYEGEILFDGEVCRFKDIRDSEalgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 pmTSLNPSMTIGrqleEGLILhtkASAQERRSLI---------LDMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVM 169
Cdd:NF040905 87 --LALIPYLSIA----ENIFL---GNERAKRGVIdwnetnrraRELLAKVGLDESPDTLVT---DIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 170 LLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEkgrTEDLLKAPqhp 249
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE---TLDCRADE--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 250 ytkkllsslpfrgrprqidltsvpmISARDIIVDYAGR--KSLFRKNKPK---------------------RALHGVSID 306
Cdd:NF040905 228 -------------------------VTEDRIIRGMVGRdlEDRYPERTPKigevvfevknwtvyhplhperKVVDDVSLN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 307 IHEGEVVALVGGSGSGKTTL---------GRTIAGLVTESEGRIQFQGRPR---------TENWTDYRLNcqmvfqdpys 368
Cdd:NF040905 283 VRRGEIVGIAGLMGAGRTELamsvfgrsyGRNISGTVFKDGKEVDVSTVSDaidaglayvTEDRKGYGLN---------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 sldprmtieaLVEEALRPV--PGLDGKAKRkRTLETLEEVGLGVDY--------------AGRypheLSGGQRQRVAIAR 432
Cdd:NF040905 353 ----------LIDDIKRNItlANLGKVSRR-GVIDENEEIKVAEEYrkkmniktpsvfqkVGN----LSGGNQQKVVLSK 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 433 AIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDtifdspk 512
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITGELPRE------- 489
|
570
....*....|.
gi 1681691554 513 EAYTRRLLSAI 523
Cdd:NF040905 490 EASQERIMRLI 500
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
300-497 |
7.59e-18 |
|
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: 80.19 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQfqgrprtenwtdyrlncqmvfqdpyssLDPRMTIeal 379
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------------------WGSTVKI--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 veealrpvpgldgkakrkrtletleevglgvdyaGRYPHeLSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVL 459
Cdd:cd03221 66 ----------------------------------GYFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 1681691554 460 DLFsdlqKRYGFSCLFISHDLGVVEQVADRVVVMQDGR 497
Cdd:cd03221 111 EAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-218 |
7.96e-18 |
|
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: 82.02 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkeNELRHLRGAEIG 93
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD----SGEVRWNGTPL-----AEQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 VVFQEPmtSLNPSMTIgrqlEEGLILHTKASAQERRSlILDMLKRVGIRDPEGALSsypHEFSGGMRQRIMLASVMLLKP 173
Cdd:TIGR01189 77 YLGHLP--GLKPELSA----LENLHFWAAIHGGAQRT-IEDALAAVGLTGFEDLPA---AQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1681691554 174 ALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMV 218
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-244 |
9.12e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKmkeNELRHLRgaEIGVVF-QEpmTS 102
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPT----SGEVRVLGYVPFK---RRKEFAR--RIGVVFgQR--SQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSMTigrqLEEGLILH------TKASAQERRSLILDMLkrvgirDPEGALSSYPHEFSGGMRQRIMLASVMLLKPALL 176
Cdd:COG4586 107 LWWDLP----AIDSFRLLkaiyriPDAEYKKRLDELVELL------DLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 177 IADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-245 |
1.37e-17 |
|
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: 86.03 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYKGRDVLKMKENELRhlrgAEIGVVFQEpm 100
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKsTLA-RLLFRFYDVT----SGRILIDGQDIRDVTQASLR----AAIGIVPQD-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 TSL-NpsMTIGRQLEEGlilHTKASAQE-----RRSLILDMLK--------RVGirdpEGALssyphEFSGGMRQRIMLA 166
Cdd:COG5265 441 TVLfN--DTIAYNIAYG---RPDASEEEveaaaRAAQIHDFIEslpdgydtRVG----ERGL-----KLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
304-478 |
1.45e-17 |
|
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: 80.28 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 304 SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIqfqGRPRtenwtdyrlNCQMVF--QDPYssldprMTiealve 381
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE---------GEDLLFlpQRPY------LP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 382 ealrpvPGldgkakrkrtleTLEEVGLgvdyagrYP--HELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVL 459
Cdd:cd03223 77 ------LG------------TLREQLI-------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 1681691554 460 DLFSDLqkryGFSCLFISH 478
Cdd:cd03223 132 QLLKEL----GITVISVGH 146
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-258 |
1.64e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRhlrgAEIGVVFQEP 99
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSEAALR----QAISVVSQRV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTsLNPSmtigrqLEEGLILhtkASAQERRSLILDMLKRVGIR----DPEGaLSSYPHE----FSGGMRQRIMLASVmLL 171
Cdd:PRK11160 424 HL-FSAT------LRDNLLL---AAPNASDEALIEVLQQVGLEklleDDKG-LNAWLGEggrqLSGGEQRRLGIARA-LL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 172 KPA-LLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVARYtSRIVVMEKGAIVEKGRTEDLLKapQHPY 250
Cdd:PRK11160 492 HDApLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA--QQGR 566
|
....*...
gi 1681691554 251 TKKLLSSL 258
Cdd:PRK11160 567 YYQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-246 |
2.62e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.90 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSLEV-ARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvadgsvsYKGRdvLKMKEN 82
Cdd:PRK11174 345 NDPVTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----------YQGS--LKINGI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 ELRHLRGAE----IGVVFQEPM---TSLNPSMTIGR-QLEEGLILHTKASAQerrslILDMLKRVG------IRDPEGAL 148
Cdd:PRK11174 412 ELRELDPESwrkhLSWVGQNPQlphGTLRDNVLLGNpDASDEQLQQALENAW-----VSEFLPLLPqgldtpIGDQAAGL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 149 ssyphefSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTaiLLISHDLPMVARYtSRIVVM 228
Cdd:PRK11174 487 -------SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQW-DQIWVM 556
|
250
....*....|....*...
gi 1681691554 229 EKGAIVEKGRTEDLLKAP 246
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAG 574
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-245 |
2.64e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVlkmkENELRHLRgAEIGVVFQepM 100
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP----DAGSISLCGEPV----PSRARHAR-QRVGVVPQ--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 TSLNPSMTIgrqlEEGLILHTK---ASAQERRSLILDMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK13537 89 DNLDPDFTV----RENLLVFGRyfgLSAAAARALVPPLLEFAKLENKADAKVG---ELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
300-509 |
3.79e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLvTESEGRIQFQGRPRTEnWTDYRLN------CQ-------M-VFQd 365
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSD-WSAAELArhraylSQqqsppfaMpVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 pYSSLD-PRMTIEALVEEALrpvpgldgkakrkrtLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIAR-------R 437
Cdd:COG4138 89 -YLALHqPAGASSEAVEQLL---------------AQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 438 PRFLIADEPVSALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:COG4138 152 GQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
297-502 |
4.16e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.41 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESegriqfqGRPRTENWT-DYRLNcqmvfQDPYSSLDPR-- 373
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG-------GAPRGARVTgDVTLN-----GEPLAAIDAPrl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTIEALVEEALRPV-------------------PGLDGKAKRKRTLETLEEVGlGVDYAGRYPHELSGGQRQRVAIARAI 434
Cdd:PRK13547 82 ARLRAVLPQAAQPAfafsareivllgrypharrAGALTHRDGEIAWQALALAG-ATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 435 A---------RRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-245 |
4.71e-17 |
|
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: 84.41 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEP 99
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR----SGEILLNGFSLKDIDRHTLRQF----INYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MtslnpsMTIGRQLEEgLILHTKASAQERRslILDMLKRVGIRD-----PEG---ALSSYPHEFSGGMRQRIMLASVMLL 171
Cdd:TIGR01193 558 Y------IFSGSILEN-LLLGAKENVSQDE--IWAACEIAEIKDdienmPLGyqtELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELTRaegTAILLISHDLPmVARYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-246 |
5.63e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.51 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGK-TLATraLIS-LLPPTikvaDGSVSYKGRDVLKMKENEL-RHLrgaeiGVVF 96
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKsTLLS--MISrLLPPD----SGEVLVDGLDVATTPSRELaKRL-----AILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEPmtSLNPSMTIgRQLEE-GLILHTKA--SAQERRsLILDMLKRVGIRDPEGAlssYPHEFSGGMRQRIMLASV----- 168
Cdd:COG4604 82 QEN--HINSRLTV-RELVAfGRFPYSKGrlTAEDRE-IIDEAIAYLDLEDLADR---YLDELSGGQRQRAFIAMVlaqdt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 169 --MLLkpalliaDEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:COG4604 155 dyVLL-------DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
297-495 |
7.71e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQgrprtenwtdyrlncqmVFQDPYSsldprmti 376
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDNQFG-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 ealveealRPVPGLDGKAKRKRTLETLE---EVGLGVDYA-GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV 452
Cdd:COG2401 98 --------REASLIDAIGRKGDFKDAVEllnAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1681691554 453 TVrAQVLDL-FSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQD 495
Cdd:COG2401 170 QT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-243 |
9.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.55 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRhlrgAEIGVVFQ 97
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKS----TLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR----SKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMTSLNpSMTIGRQLEEGLIlHTKASAQERRSLILDMLKRVGIRDPEgalSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK13647 87 DPDDQVF-SSTVWDDVAFGPV-NMGLDKDEVERRVEEALKAVRMWDFR---DKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-247 |
1.03e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 26 SVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvADGSVSYKGRDVLKMKENELRHLRGaeigVVFQEPMTSlnP 105
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRA----YLSQQQTPP--F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 106 SMTIGRQLEegLILHTKASAQERRSLILDMLKRVGIRDpegALSSYPHEFSGGMRQRIMLASVML-----LKPA--LLIA 178
Cdd:PRK03695 83 AMPVFQYLT--LHQPDKTRTEAVASALNEVAEALGLDD---KLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 179 DEPTTALDaVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:PRK03695 158 DEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-262 |
1.10e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVARTGQ-QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLpptiKVADGSVSYKGRdvlKMKE 81
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF----EEFEGKVKIDGE---LLTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 82 NELRHLRgAEIGVVFQEPMTSLnpsmtIGRQLEEGLILHTKASAQERRSLIL---DMLKRVGIRDPEgalSSYPHEFSGG 158
Cdd:PRK13642 74 ENVWNLR-RKIGMVFQNPDNQF-----VGATVEDDVAFGMENQGIPREEMIKrvdEALLAVNMLDFK---TREPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKGR 238
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA 223
|
250 260 270
....*....|....*....|....*....|..
gi 1681691554 239 TEDLLKAPQH--------PYTKKLLSSLPFRG 262
Cdd:PRK13642 224 PSELFATSEDmveigldvPFSSNLMKDLRKNG 255
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-296 |
1.42e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKEnELRHlrgaeIGVVFQEp 99
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD----SGRIMLDGQDITHVPA-ENRH-----VNTVFQS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK09452 95 -YALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQL---EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 180 EPTTALDAVIqRDVMEL-MVELTRAEGTAILLISHD----LPMvaryTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKKl 254
Cdd:PRK09452 170 ESLSALDYKL-RKQMQNeLKALQRKLGITFVFVTHDqeeaLTM----SDRIVVMRDGRIEQDGTPREIYEEPKNLFVAR- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1681691554 255 lsslpFRGRPRQIDLTSVPMISARDIIVDYAGRKSLFRKNKP 296
Cdd:PRK09452 244 -----FIGEINIFDATVIERLDEQRVRANVEGRECNIYVNFA 280
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
298-537 |
1.88e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenwtdyrlncqmvFQDPYSS-------- 369
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-------------FNGPKSSqeagigii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 -----LDPRMTIEA---LVEEALRPVPGLDGKAKRKRTLETLEEvgLGVDYAGRYP-HELSGGQRQRVAIARAIARRPRF 440
Cdd:PRK10762 85 hqelnLIPQLTIAEnifLGREFVNRFGRIDWKKMYAEADKLLAR--LNLRFSSDKLvGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGD-RDTIFDSPKEAYT-RR 518
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREvADLTEDSLIEMMVgRK 241
|
250
....*....|....*....
gi 1681691554 519 LLSAIPALDQnEKGGVTLK 537
Cdd:PRK10762 242 LEDQYPRLDK-APGEVRLK 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-252 |
3.09e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.93 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRAL--ISLLPPTIKVaDGSVSYKGRDVLKMKENeLRHLRgAEIGVVFQE 98
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRV-EGRVEFFNQNIYERRVN-LNRLR-RQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PmtSLNPsMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDP-EGALSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PRK14258 97 P--NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYT----------SRIvvmekGAIVEKGRTEDLLKAPQ 247
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSdftaffkgneNRI-----GQLVEFGLTKKIFNSPH 248
|
....*
gi 1681691554 248 HPYTK 252
Cdd:PRK14258 249 DSRTR 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
300-494 |
3.46e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRlncQMVfqdPYSSLDPRMTIEA 378
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYR---QQV---SYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1681691554 459 LDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQ 494
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-214 |
4.60e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.45 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIkvadGSVSYKGRDVLKMKENELRHlrgaEIGVVFQEP 99
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS----GTLLFEGEDISTLKPEIYRQ----QVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTslnpsmtIGRQLEEGLILHTKASAQE-RRSLILDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIA 178
Cdd:PRK10247 91 TL-------FGDTVYDNLIFPWQIRNQQpDPAIFLDDLERFAL--PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1681691554 179 DEPTTALDAVIQRDVMELMVELTRAEGTAILLISHD 214
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-510 |
5.78e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 302 GVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQdpYSSLDPRMTiealVE 381
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ--FDNLDPDFT----VR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 382 EALRPVP---GLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQV 458
Cdd:PRK13537 99 ENLLVFGryfGLSAAAARALVPPLLEFAKLE-NKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 459 LDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:PRK13537 178 WERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-218 |
5.78e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 3 MDKLLTVCGLSLEVARtgQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvadgsvsykgrdvlkmkEN 82
Cdd:PRK09544 1 MTSLVSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-------------------EG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 ELRHLRGAEIGVVFQEpmTSLNPSM--TIGR--QLEEGLilhtkasaqeRRSLILDMLKRVgirdPEGALSSYP-HEFSG 157
Cdd:PRK09544 60 VIKRNGKLRIGYVPQK--LYLDTTLplTVNRflRLRPGT----------KKEDILPALKRV----QAGHLIDAPmQKLSG 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMV 218
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
303-500 |
5.80e-16 |
|
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: 80.61 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-ENWTDYRlncQM---VFQDPYssldprmtiea 378
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYR---QLfsaVFSDFH----------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALrpvpGLDGKAKRKRTLETLEEVGLG--VDYA-GRY-PHELSGGQRQRVAIARAIA-RRPrFLIADEPVSALDVT 453
Cdd:COG4615 417 LFDRLL----GLDGEADPARARELLERLELDhkVSVEdGRFsTTDLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPE 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 454 VRA----QVLdlfSDLQKRyGFSCLFISHDlgvvEQ---VADRVVVMQDGRIIE 500
Cdd:COG4615 492 FRRvfytELL---PELKAR-GKTVIAISHD----DRyfdLADRVLKMDYGKLVE 537
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
303-507 |
6.42e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLvTESEGRIQFQGRPrtenWTDYRLN---------CQ-------M-VFQd 365
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQP----LEAWSAAelarhraylSQqqtppfaMpVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 pYSSLD-PRMTIEALVEEALRpvpgldgkakrkrtlETLEEVGLGvDYAGRYPHELSGGQRQRVAIA-------RAIARR 437
Cdd:PRK03695 89 -YLTLHqPDKTRTEAVASALN---------------EVAEALGLD-DKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 438 PRFLIADEPVSALDVTVRAqVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-258 |
1.95e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHlrgaEIGVVFQEPMTSL 103
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE----SGQIIIDGDLLTEENVWDIRH----KIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 npsmtIGRQLEEGLI--LHTKA-SAQERRSLILDMLKRVGIRDPEgalSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:PRK13650 95 -----VGATVEDDVAfgLENKGiPHEEMKERVNEALELVGMQDFK---EREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 181 PTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVArYTSRIVVMEKGAiVEK--------GRTEDLLK-APQHPYT 251
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VEStstprelfSRGNDLLQlGLDIPFT 244
|
....*..
gi 1681691554 252 KKLLSSL 258
Cdd:PRK13650 245 TSLVQSL 251
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
288-508 |
2.11e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQDPY 367
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SSLDPRMTIEALVEEALRPVPGLDGKAKRKRTLETLEEVGLG--VDYAGRyphELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQ---SLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 446 PVSALDVTvraQVLDLFSDLQ--KRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIF 508
Cdd:PRK10895 164 PFAGVDPI---SVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-478 |
2.72e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.52 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 28 SFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVLKMKENELRHLRGAEigvvFQE---PMTSLN 104
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL----LSGERQSQFSHITRLSFEQLQKLVSDE----WQRnntDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 105 PSMTiGRQLEEGLILHTKASAqerrsLILDMLKRVGIrdpeGALSSYPHEF-SGGMRQRIMLASVMLLKPALLIADEPTT 183
Cdd:PRK10938 95 EDDT-GRTTAEIIQDEVKDPA-----RCEQLAQQFGI----TALLDRRFKYlSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 184 ALDAVIQRDVMELMVELTrAEGTAILLIS---HDLPMVARYtsrIVVMEKGAIVEKGRTEDLLK---APQHPYTKKLL-S 256
Cdd:PRK10938 165 GLDVASRQQLAELLASLH-QSGITLVLVLnrfDEIPDFVQF---AGVLADCTLAETGEREEILQqalVAQLAHSEQLEgV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 257 SLPFRGRPRQIDL--TSVPMISARDIIVDYAGRkslfrknkpkRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLV 334
Cdd:PRK10938 241 QLPEPDEPSARHAlpANEPRIVLNNGVVSYNDR----------PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 335 TE--SEGRIQFqGRPRTENWT-----------------DYRLNCQmVFQDPYSSLDPRMTIEALVEEALrpvpgldgkak 395
Cdd:PRK10938 311 PQgySNDLTLF-GRRRGSGETiwdikkhigyvssslhlDYRVSTS-VRNVILSGFFDSIGIYQAVSDRQ----------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 396 RKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRaQVLDLFSDLQKRYGFS-CL 474
Cdd:PRK10938 378 QKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLISEGETqLL 456
|
....
gi 1681691554 475 FISH 478
Cdd:PRK10938 457 FVSH 460
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
298-511 |
3.10e-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: 74.76 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPY-------SS 369
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDiSTIPLEDLRSSLTIIPQDPTlfsgtirSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 LDP-RMTIEALVEEALRpvpgldgkakrkrtletLEEVGLgvdyagryphELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:cd03369 102 LDPfDEYSDEEIYGALR-----------------VSEGGL----------NLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 449 ALDVTVRAQ----VLDLFSDLqkrygfSCLFISHDLGVVEQVaDRVVVMQDGRIIEegdrdtiFDSP 511
Cdd:cd03369 155 SIDYATDALiqktIREEFTNS------TILTIAHRLRTIIDY-DKILVMDAGEVKE-------YDHP 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
291-500 |
3.31e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.48 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT-ENWTDYRLNCQMVFQDPY-- 367
Cdd:PRK10522 330 FAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSAVFTDFHlf 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 -SSLDPRMTI--EALVEEALRPVpgldgKAKRKRTLETLEEVGLgvdyagryphELSGGQRQRVAIARAIARRPRFLIAD 444
Cdd:PRK10522 410 dQLLGPEGKPanPALVEKWLERL-----KMAHKLELEDGRISNL----------KLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 445 EPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIE 500
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-509 |
5.09e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 276 SARDIIVDYAGRKSLFRKnkpKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDY 355
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGD---KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 356 RLNCQMVFQdpYSSLDPRMTiealVEEALRPVPGLDGKAKRK--RTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARA 433
Cdd:PRK13536 113 RARIGVVPQ--FDNLDLEFT----VRENLLVFGRYFGMSTREieAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 434 IARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-240 |
6.76e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTiKVADGSVSYKGRDVLKMKE--NELRHLRgAEIGVVFQEp 99
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-KSAGSHIELLGRTVQREGRlaRDIRKSR-ANTGYIFQQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIgrqLEEGLILHTKAS----------AQERRSLILDMLKRVGirdpegaLSSYPHE----FSGGMRQRIML 165
Cdd:PRK09984 95 -FNLVNRLSV---LENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVG-------MVHFAHQrvstLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 166 ASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTE 240
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-241 |
7.46e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRdVLKMKEN------ELRHlrgaeIGVVFQEpm 100
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKT----SLINAISGLTRPQKGRIVLNGR-VLFDAEKgiclppEKRR-----IGYVFQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 TSLNPSMTIGRQLEEGLilhtKASAQERRSLILDMLkrvGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIADE 180
Cdd:PRK11144 85 ARLFPHYKVRGNLRYGM----AKSMVAQFDKIVALL---GI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 181 PTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTED 241
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-235 |
8.16e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSleVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtRALISLLPPTikvaDGSVSYkGRDVlkmken 82
Cdd:COG0488 313 KKVLELEGLS--KSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKsTLL-KLLAGELEPD----SGTVKL-GETV------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 elrhlrgaEIGVVFQEpMTSLNPSMTIGRQLEEGlilHTKASAQERRSLILDML-------KRVGirdpegalssyphEF 155
Cdd:COG0488 379 --------KIGYFDQH-QEELDPDKTVLDELRDG---APGGTEQEVRGYLGRFLfsgddafKPVG-------------VL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALDavIQ-RDVMELMveLTRAEGTaILLISHDLPMVARYTSRIVVMEKGAIV 234
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLD--IEtLEALEEA--LDDFPGT-VLLVSHDRYFLDRVATRILEFEDGGVR 508
|
.
gi 1681691554 235 E 235
Cdd:COG0488 509 E 509
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-244 |
8.40e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVaDGSVSYKGRdvlKMKENELRhlrgAEIGVVFQEPMt 101
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKG-SGSVLLNGM---PIDAKEMR----AISAYVQQDDL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 sLNPSMTIgrqlEEGLI------LHTKASAQERRSLILDMLKRVGIRDPEGALSSYPHE---FSGGMRQRIMLASVMLLK 172
Cdd:TIGR00955 110 -FIPTLTV----REHLMfqahlrMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
300-503 |
1.17e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAG--LVTESEGRIQFQGRPRTENWTDYR--LNCQMVFQDPyssldprmt 375
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERahLGIFLAFQYP--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEalveealrpVPGLDG--------KAKRKRT--------------LETLEEVGLGVDYAGRYPHE-LSGGQRQRVAIAR 432
Cdd:CHL00131 94 IE---------IPGVSNadflrlayNSKRKFQglpeldplefleiiNEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 433 AIARRPRFLIADEPVSALDV---TVRAQVLDLFSDLQKrygfSCLFISHDLGVVEQVA-DRVVVMQDGRIIEEGD 503
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKTGD 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
307-514 |
1.42e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 307 IHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQF----------QGRPRTENWT-----------------DYRLNC 359
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarlqQDPPRNVEGTvydfvaegieeqaeylkRYHDIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 360 QMVFQDPYSSLDPRMtieALVEEALRpvpGLDGKAKRKRTLETLEEVGLGVDYAgryPHELSGGQRQRVAIARAIARRPR 439
Cdd:PRK11147 106 HLVETDPSEKNLNEL---AKLQEQLD---HHNLWQLENRINEVLAQLGLDPDAA---LSSLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 440 FLIADEPVSALDVTvraqVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIE-EGDRDTIFDSPKEA 514
Cdd:PRK11147 177 VLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSyPGNYDQYLLEKEEA 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-237 |
1.77e-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: 72.69 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTlATRALISLLPPTIKVADGSVSYKGRdvlKMKenelRHLRGAEIGVVFQEpmT 101
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKT-TLLDAISGRVEGGGTTSGQILFNGQ---PRK----PDQFQKCVAYVRQD--D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIgrqlEEGLI------LHTKASAQERRSLILDM-LKRVGIRDPEGALSSYpheFSGGMRQRIMLASVMLLKPA 174
Cdd:cd03234 91 ILLPGLTV----RETLTytailrLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-245 |
4.28e-14 |
|
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: 74.69 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELrhlrGAEIGVVFQepm 100
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT----SGSVRLDGADLKQWDRETF----GKHIGYLPQ--- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 tslnpsmtiGRQLEEGLILHTKA----SAQERRslILDMLKRVGIRD-----PEG---ALSSYPHEFSGGMRQRIMLASV 168
Cdd:TIGR01842 400 ---------DVELFPGTVAENIArfgeNADPEK--IIEAAKLAGVHElilrlPDGydtVIGPGGATLSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 169 MLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDlPMVARYTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHR-PSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-225 |
5.71e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 28 SFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELR------HLRGaeigvvfqepmt 101
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD----AGEVLWQGEPIRRQRDEYHQdllylgHQPG------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 sLNPSMTIgrqlEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYpheFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PRK13538 85 -IKTELTA----LENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1681691554 182 TTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRI 225
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-225 |
7.91e-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: 70.21 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELR--HLRGAE 91
Cdd:cd03231 6 LTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL----AGRVLLNGGPLDFQRDSIARglLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 92 IGVvfqepMTSLNPsmtigrqLEEGLILHTKASaqerRSLILDMLKRVGIRDPEGALSsypHEFSGGMRQRIMLASVMLL 171
Cdd:cd03231 82 PGI-----KTTLSV-------LENLRFWHADHS----DEQVEEALARVGLNGFEDRPV---AQLSAGQQRRVALARLLLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRI 225
Cdd:cd03231 143 GRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-246 |
8.20e-14 |
|
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: 71.03 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTgqQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENElRH 86
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD----SGKILLDGQDITKLPMHK-RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGaeIGVVFQEPmtslnpsmTIGRQL--EEGLIL---HTKASAQERRSLILDMLKRVGIRDPEGALSSYpheFSGGMRQ 161
Cdd:cd03218 74 RLG--IGYLPQEA--------SIFRKLtvEENILAvleIRGLSKKEREEKLEELLEEFHITHLRKSKASS---LSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 162 RIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTED 241
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
....*
gi 1681691554 242 LLKAP 246
Cdd:cd03218 220 IAANE 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-246 |
8.42e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.98 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRhlrgAEIGVVFQEPM-- 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR----SRLAVVSQTPFlf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 -TSLNPSMTIGR------QLEEGLILhtkASAQErrslilDMLkrvgiRDPEGalssYPHE-------FSGGMRQRIMLA 166
Cdd:PRK10789 402 sDTVANNIALGRpdatqqEIEHVARL---ASVHD------DIL-----RLPQG----YDTEvgergvmLSGGQKQRISIA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 167 SVMLLKPALLIADEpttALDAVIQRDVMELMVELTR-AEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:PRK10789 464 RALLLNAEILILDD---ALSAVDGRTEHQILHNLRQwGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQ 539
|
.
gi 1681691554 246 P 246
Cdd:PRK10789 540 S 540
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
300-508 |
8.99e-14 |
|
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: 74.60 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR----PRTENWTDYRLNCQMVFQDPYSSLDPRMT 375
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvPQQAWIQNDSLRENILFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALveeALRP----VPGLDgkakrkRTletleEVG-LGVDyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:TIGR00957 734 LEAC---ALLPdleiLPSGD------RT-----EIGeKGVN--------LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 451 DVTVRAQVLD-LFSDLQKRYGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEG------DRDTIF 508
Cdd:TIGR00957 792 DAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGsyqellQRDGAF 855
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
306-492 |
1.56e-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: 70.51 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 306 DIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFqgrprtenwtdyrLNCQMVFQDPYSSLDPRMTIEALveealr 385
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------------ELDTVSYKPQYIKADYEGTVRDL------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 386 pvpgLDGKAKRKRTL-----ETLEEVGLGVDYAGRYPhELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVR---AQ 457
Cdd:cd03237 82 ----LSSITKDFYTHpyfktEIAKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmaSK 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1681691554 458 VLDLFSDLQKRYGFsclFISHDLGVVEQVADRVVV 492
Cdd:cd03237 157 VIRRFAENNEKTAF---VVEHDIIMIDYLADRLIV 188
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
297-530 |
1.62e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.21 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP----RTENWtdyRLNCQMVFQDPYSSLD- 371
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPltklQLDSW---RSRLAVVSQTPFLFSDt 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 ---------PRMTIEAlVEEALRPVPGLDGKAKRKRTLETleEVG-LGVdyagryphELSGGQRQRVAIARAIARRPRFL 441
Cdd:PRK10789 405 vannialgrPDATQQE-IEHVARLASVHDDILRLPQGYDT--EVGeRGV--------MLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSdlQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDSP---KEAYTRR 518
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQSgwyRDMYRYQ 550
|
250
....*....|..
gi 1681691554 519 LLSAipALDQNE 530
Cdd:PRK10789 551 QLEA--ALDDAP 560
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-256 |
2.43e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISL--LPPTIKVaDGSVSYKGRDVL--KMKENELRHlrgaEIGVVFQEP 99
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRV-EGKVTFHGKNLYapDVDPVEVRR----RIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtslNP-SMTIGRQLEEGL-ILHTKASAQE--RRSL--------ILDMLKRVGIrdpegalssyphEFSGGMRQRIMLAS 167
Cdd:PRK14243 101 ----NPfPKSIYDNIAYGArINGYKGDMDElvERSLrqaalwdeVKDKLKQSGL------------SLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVMELMVELtrAEGTAILLISHDLPMVAR---YTS--RIVVMEKGA----IVEKGR 238
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARvsdMTAffNVELTEGGGrygyLVEFDR 242
|
250
....*....|....*...
gi 1681691554 239 TEDLLKAPQHPYTKKLLS 256
Cdd:PRK14243 243 TEKIFNSPQQQATRDYVS 260
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
299-493 |
3.06e-13 |
|
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: 69.70 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 299 ALHGVSIdIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRiqFQGRPrteNWTDyrlncqmvFQDPYSSLDPRMTIEA 378
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPP---DWDE--------ILDEFRGSELQNYFTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRPV----------PGLDGKA----KRKRTLETLEEVGLGVDYAG---RYPHELSGGQRQRVAIARAIARRPRFL 441
Cdd:cd03236 82 LLEGDVKVIvkpqyvdlipKAVKGKVgellKKKDERGKLDELVDQLELRHvldRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 442 IADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVM 493
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
291-507 |
3.38e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.84 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenwtdYRLNcqmvfqdpySSL 370
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV-----IAIS---------AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 371 DPRMT-IEALVEEALrpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:PRK13546 97 SGQLTgIENIEFKML--CMGFKRKEIKAMTPKIIEFSELG-EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 450 LDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-258 |
3.56e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRdVLKMKENELRHLRgAEIGVVFQEP- 99
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ----KGAVLWQGK-PLDYSKRGLLALR-QQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 ----MTSLN------------PSMTIGRQLEEGLILhtkASAQERRSLILDMLkrvgirdpegalssyphefSGGMRQRI 163
Cdd:PRK13638 88 qqifYTDIDsdiafslrnlgvPEAEITRRVDEALTL---VDAQHFRHQPIQCL-------------------SHGQKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 164 MLASVMLLKPALLIADEPTTALDAViQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG------ 237
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPA-GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGapgevf 224
|
250 260
....*....|....*....|...
gi 1681691554 238 -RTEDLLKAP-QHPYTKKLLSSL 258
Cdd:PRK13638 225 aCTEAMEQAGlTQPWLVKLHTQL 247
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-237 |
3.69e-13 |
|
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: 68.35 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKvaDGSVSYKGRDVlkmKENELRhlrgAEIGVVFQ 97
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV--SGEVLINGRPL---DKRSFR----KIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMtsLNPSMTIgrqlEEGLILhtkaSAQERrslildmlkrvGIrdpegalssyphefSGGMRQRIMLASVMLLKPALLI 177
Cdd:cd03213 90 DDI--LHPTLTV----RETLMF----AAKLR-----------GL--------------SGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDlPMVARYTS--RIVVMEKGAIVEKG 237
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQ-PSSEIFELfdKLLLLSQGRVIYFG 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-233 |
4.02e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKE--------- 81
Cdd:PRK10762 255 EVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT----SGYVTLDGHEVVTRSPqdglangiv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 82 --NELRHLRGAEIGVVFQEPMtslnpSMTIGRQLEE--GLILHtkasaQERRSLILDMLKRVGIRDPE-----GALSsyp 152
Cdd:PRK10762 331 yiSEDRKRDGLVLGMSVKENM-----SLTALRYFSRagGSLKH-----ADEQQAVSDFIRLFNIKTPSmeqaiGLLS--- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 153 hefsGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGA 232
Cdd:PRK10762 398 ----GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
.
gi 1681691554 233 I 233
Cdd:PRK10762 473 I 473
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-213 |
4.68e-13 |
|
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: 67.18 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLeVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvadgsvSYKGRdvlkmkeneLRH 86
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP----------WGSGR---------IGM 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGAEIGVVFQEPMtslnpsMTIGRqLEEGLIlhtkasaqerrslildmlkrvgirdpegalssYP--HEFSGGMRQRIM 164
Cdd:cd03223 61 PEGEDLLFLPQRPY------LPLGT-LREQLI--------------------------------YPwdDVLSGGEQQRLA 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAVIQRDVMELMveltRAEGTAILLISH 213
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-233 |
6.60e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 16 VARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvadgsvSYKGRDVLKMKENELRHLRGA-EIGV 94
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG---------RWEGEIFIDGKPVKIRNPQQAiAQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 95 VfqepMTS-------LNPSMTIG--------RQLEEGLILHTKASAQErrslILDMLKRVGIR--DPEGALSSypheFSG 157
Cdd:PRK13549 341 A----MVPedrkrdgIVPVMGVGknitlaalDRFTGGSRIDDAAELKT----ILESIQRLKVKtaSPELAIAR----LSG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
300-502 |
7.81e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAG-LVTESEGRIQFQGR----PRTeNW---TDYRLNcqMVFQDPYSSLD 371
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvPQV-SWifnATVRDN--ILFGSPFDPER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMTIE-ALVEEALRPVPGLDgkakrkrtletLEEVG-LGVDyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:PLN03130 710 YERAIDvTALQHDLDLLPGGD-----------LTEIGeRGVN--------ISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 450 LDVTVRAQVLD--LFSDLQKRygfSCLFISHDLGVVEQVaDRVVVMQDGRIIEEG 502
Cdd:PLN03130 771 LDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-213 |
9.63e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 24 VKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlKMKENELRHlrgaEIGVvfqepMT-- 101
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS----EGEAWLFGQPV-DAGDIATRR----RVGY-----MSqa 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 -SLNPSMTIgRQleeGLILHTK---ASAQERRSLILDMLKRVGIRDPEGALssyPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:NF033858 348 fSLYGELTV-RQ---NLELHARlfhLPAAEIAARVAEMLERFDLADVADAL---PDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190
....*....|....*....|....*....|....*..
gi 1681691554 178 ADEPTTALDAViQRDVM-ELMVELTRAEGTAILLISH 213
Cdd:NF033858 421 LDEPTSGVDPV-ARDMFwRLLIELSREDGVTIFISTH 456
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-245 |
9.69e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlpptIKVADGSVSYKGRDVLK-MKENELRHLRGAEiGVVF 96
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF----VRLASGKISILGQPTRQaLQKNLVAYVPQSE-EVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEPMTSLNPSMtIGRQLEEGLILHTKAsaqERRSLILDMLKRVGIRDpegalssYPH----EFSGGMRQRIMLASVMLLK 172
Cdd:PRK15056 92 SFPVLVEDVVM-MGRYGHMGWLRRAKK---RDRQIVTAALARVDMVE-------FRHrqigELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 173 PALLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSrIVVMEKGAIVEKGRTEDLLKA 245
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTA 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
228-502 |
1.17e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 228 MEKGAIVEKGRTEDLLKAPQHPYtkkllsslpfrGRPRQidltsvPMISARDIIVDYAgrkslFRKNKPKRALHGVSIDI 307
Cdd:PRK10790 307 MLQQAVVAGERVFELMDGPRQQY-----------GNDDR------PLQSGRIDIDNVS-----FAYRDDNLVLQNINLSV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 308 HEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPYSSLDP--------RMTIEA 378
Cdd:PRK10790 365 PSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlSSLSHSVLRQGVAMVQQDPVVLADTflanvtlgRDISEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRPVPGLDGKAKRKRTLET-LEEVGlgvdyagrypHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQ 457
Cdd:PRK10790 445 QVWQALETVQLAELARSLPDGLYTpLGEQG----------NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1681691554 458 VLDLFSDLQKRYgfSCLFISHDLG-VVEqvADRVVVMQDGRIIEEG 502
Cdd:PRK10790 515 IQQALAAVREHT--TLVVIAHRLStIVE--ADTILVLHRGQAVEQG 556
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-212 |
1.39e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikvADGSVSYKGRDVLKMKENELRHLRGaeig 93
Cdd:PRK13539 8 LACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP----AAGTIKLDGGDIDDPDVAEACHYLG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 vvfqePMTSLNPSMTIgrqlEEGLILHTKASAQERRSlILDMLKRVGIRD----PEGALSSyphefsgGMRQRIMLASVM 169
Cdd:PRK13539 80 -----HRNAMKPALTV----AENLEFWAAFLGGEELD-IAAALEAVGLAPlahlPFGYLSA-------GQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1681691554 170 LLKPALLIADEPTTALDAVIQRDVMELMveLTRAEGTAILLIS 212
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELI--RAHLAQGGIVIAA 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-498 |
1.55e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.27 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRAL----ISLLPPTIKVADGSVSYKGRDV-------------LKMKEN 82
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaIDGIPKNCQILHVEQEVVGDDTtalqcvlntdierTQLLEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 83 ELRHL---RGAEIGVVFQEPMTSLNPSM---TIGRQLEE---GLILHTKASAQERRSLILDMLKRVgirdPEGALSSyPH 153
Cdd:PLN03073 269 EAQLVaqqRELEFETETGKGKGANKDGVdkdAVSQRLEEiykRLELIDAYTAEARAASILAGLSFT----PEMQVKA-TK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLASVMLLKPALLIADEPTTALDAviqRDVMELMVELTRAEGTAILlISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIV-VSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 234 V---------EKGRTEDLL----------KAPQH--------PYTKKLLSSLPFRGR---------------------PR 265
Cdd:PLN03073 420 VtykgdydtfERTREEQLKnqqkafesneRSRSHmqafidkfRYNAKRASLVQSRIKaldrlghvdavvndpdykfefPT 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 266 QIDLTSVPMISARDIIVDYAGRKSLFRKNKpkralHGVSIDIHegevVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG 345
Cdd:PLN03073 500 PDDRPGPPIISFSDASFGYPGGPLLFKNLN-----FGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 346 RPRTEnwtdyrlncqmVF-QDPYSSLDprMTIEALVEeALRPVPGLDGKAKRKRtletLEEVGLGVDYAGRYPHELSGGQ 424
Cdd:PLN03073 571 KVRMA-----------VFsQHHVDGLD--LSSNPLLY-MMRCFPGVPEQKLRAH----LGSFGVTGNLALQPMYTLSGGQ 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 425 RQRVAIARAIARRPRFLIADEPVSALD---VTVRAQVLDLFSDlqkrygfSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDldaVEALIQGLVLFQG-------GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
156-246 |
2.07e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVE 235
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
90
....*....|.
gi 1681691554 236 KGRTEDLLKAP 246
Cdd:PRK10575 229 QGTPAELMRGE 239
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-240 |
2.14e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKLLTVCGLSLEVARTgqQVVKSVSFDLAPGEIFGIVGESGSGKTlaTRALISLLPPTIKVADGSVSYKGRDVLKMk 80
Cdd:CHL00131 2 NKNKPILEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKS--TLSKVIAGHPAYKILEGDILFKGESILDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 81 ENELRHLRGaeIGVVFQEP------------MTSLNpsmtiGRQLEEGLilhTKASAQERRSLILDMLKRVGIRdpEGAL 148
Cdd:CHL00131 77 EPEERAHLG--IFLAFQYPieipgvsnadflRLAYN-----SKRKFQGL---PELDPLEFLEIINEKLKLVGMD--PSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 149 SSYPHE-FSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEgTAILLISHdlpmVARYTSRIV- 226
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSE-NSIILITH----YQRLLDYIKp 219
|
250
....*....|....*...
gi 1681691554 227 ----VMEKGAIVEKGRTE 240
Cdd:CHL00131 220 dyvhVMQNGKIIKTGDAE 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-498 |
2.21e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.43 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 13 SLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHLRGAEI 92
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKS----TLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 93 GVVFQ--EPMTSLNPSMTIGRQLEEG---LILHTKASA------QERRSLILDMLkrvGIRDPEgaLSSYPHEFSGGMRQ 161
Cdd:PRK10636 82 EYVIDgdREYRQLEAQLHDANERNDGhaiATIHGKLDAidawtiRSRAASLLHGL---GFSNEQ--LERPVSDFSGGWRM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 162 RIMLASVMLLKPALLIADEPTTA--LDAVIQrdvmeLMVELTRAEGTAIlLISHDLPMVARYTSRIVVMEKGAI------ 233
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHldLDAVIW-----LEKWLKSYQGTLI-LISHDRDFLDPIVDKIIHIEQQSLfeytgn 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 234 ---VEKGRTEDLL----------------------------KAPQHPYTKKLLSSL----------PFRGRPRQIDLTSV 272
Cdd:PRK10636 231 yssFEVQRATRLAqqqamyesqqervahlqsyidrfrakatKAKQAQSRIKMLERMeliapahvdnPFHFSFRAPESLPN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 273 PMISARDIIVDYAGRKslfrknkpkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENW 352
Cdd:PRK10636 311 PLLKMEKVSAGYGDRI----------ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 353 TDYRLNCQMVFQDP---YSSLDPRMTiealvEEALRPVPGLDGKAKRKRTLETleevglgvdyaGRYphelSGGQRQRVA 429
Cdd:PRK10636 381 AQHQLEFLRADESPlqhLARLAPQEL-----EQKLRDYLGGFGFQGDKVTEET-----------RRF----SGGEKARLV 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKrygfSCLFISHDLGVVEQVADRVVVMQDGRI 498
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-498 |
2.85e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDV-LKMKENELRHlrgaEIGVVFQE 98
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD----SGSILFQGKEIdFKSSKEALEN----GISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 ----PMTSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSSYphefsggMRQRIMLASVMLLKPA 174
Cdd:PRK10982 82 lnlvLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVS-------QMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 175 LLIADEPTTALDaviQRDVMEL--MVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLlkapqhpYTK 252
Cdd:PRK10982 155 IVIMDEPTSSLT---EKEVNHLftIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL-------TMD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 253 KLLSSLPFRG-RPRQIDLTSVPmisaRDIIVDYagrKSLFRKNKPkrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIA 331
Cdd:PRK10982 225 KIIAMMVGRSlTQRFPDKENKP----GEVILEV---RNLTSLRQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 332 GLVTESEGRIQFQGRPRTENWTDYRLN--CQMVFQDP-----YSSLDprMTIEALV---EEALRPVPGLDGKAKRKRTLE 401
Cdd:PRK10982 296 GIREKSAGTITLHGKKINNHNANEAINhgFALVTEERrstgiYAYLD--IGFNSLIsniRNYKNKVGLLDNSRMKSDTQW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 402 TLEevGLGVDYAGRYPH--ELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHD 479
Cdd:PRK10982 374 VID--SMRVKTPGHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSE 450
|
490
....*....|....*....
gi 1681691554 480 LGVVEQVADRVVVMQDGRI 498
Cdd:PRK10982 451 MPELLGITDRILVMSNGLV 469
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
300-518 |
4.16e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRP-RTENWTDYRLNCQMVFQDPY-------SSLD 371
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREiGAYGLRELRRQFSMIPQDPVlfdgtvrQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PrmTIEALVEE---ALRPVpGLDGKAKRK------RTLETleevglGVDYagryphelSGGQRQRVAIARAIARRPR-FL 441
Cdd:PTZ00243 1406 P--FLEASSAEvwaALELV-GLRERVASEsegidsRVLEG------GSNY--------SVGQRQLMCMARALLKKGSgFI 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 442 IADEPVS----ALDVTVRAQVLDLFSdlqkryGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEG-------DRDTIFDS 510
Cdd:PTZ00243 1469 LMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGsprelvmNRQSIFHS 1541
|
....*...
gi 1681691554 511 PKEAYTRR 518
Cdd:PTZ00243 1542 MVEALGRS 1549
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
297-510 |
4.16e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESE-GRIQFQGR----PRTENWTDYRLNCQMVFQDPYSSLD 371
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSvayvPQVSWIFNATVRENILFGSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMTIEAL-VEEALRPVPGLDgkakrkrtletLEEVG-LGVDyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:PLN03232 710 YWRAIDVTaLQHDLDLLPGRD-----------LTEIGeRGVN--------ISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 450 LDVTVRAQVLD--LFSDLQkryGFSCLFISHDLGVVEQVaDRVVVMQDGRIIEEGDRDTIFDS 510
Cdd:PLN03232 771 LDAHVAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-231 |
5.08e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSLEVARtGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvadgsvSYKGRdvlkmkene 83
Cdd:COG4178 360 DGALALEDLTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP----------YGSGR--------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGAEIGVVFQEPMtslnpsMTIGRqLEEGLI---LHTKASAQErrslILDMLKRVGIRDPEGALS---SYPHEFSG 157
Cdd:COG4178 420 IARPAGARVLFLPQRPY------LPLGT-LREALLypaTAEAFSDAE----LREALEAVGLGHLAERLDeeaDWDQVLSL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 158 GMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVEltRAEGTAILLISHDlPMVARYTSRIVVMEKG 231
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
275-513 |
5.16e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.00 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 275 ISARDIIVDYagrkslfRKNKPKrALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG-RPRTENWT 353
Cdd:PLN03130 1238 IKFEDVVLRY-------RPELPP-VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcDISKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 354 DYRLNCQMVFQDP--YS-----SLDP-RMTIEALVEEALrpvpgldgkaKRKRTLETLEEVGLGVDY----AGRyphELS 421
Cdd:PLN03130 1310 DLRKVLGIIPQAPvlFSgtvrfNLDPfNEHNDADLWESL----------ERAHLKDVIRRNSLGLDAevseAGE---NFS 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 422 GGQRQRVAIARAIARRPRFLIADEPVSALDvtVRAQVLdlfsdLQK--RYGF-SC--LFISHDLGVVEQvADRVVVMQDG 496
Cdd:PLN03130 1377 VGQRQLLSLARALLRRSKILVLDEATAAVD--VRTDAL-----IQKtiREEFkSCtmLIIAHRLNTIID-CDRILVLDAG 1448
|
250
....*....|....*..
gi 1681691554 497 RIIEegdrdtiFDSPKE 513
Cdd:PLN03130 1449 RVVE-------FDTPEN 1458
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
296-514 |
5.43e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRI----QFQGRPRTENWTDYRLNCQMVFQDPYSSLD 371
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAYVPQQAWIMNATVRGNILFFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 372 PRMTIEALVEEA-LRPVPGldgkakrkrTLETleEVG-LGVDyagrypheLSGGQRQRVAIARAIARRPRFLIADEPVSA 449
Cdd:PTZ00243 752 LADAVRVSQLEAdLAQLGG---------GLET--EIGeKGVN--------LSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 450 LDVTVRAQVL-DLFsdLQKRYGFSCLFISHDLGVVEQvADRVVVMQDGRIIEEGDRDTIFDSPKEA 514
Cdd:PTZ00243 813 LDAHVGERVVeECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYA 875
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-233 |
9.91e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvadGSVSYKGRDVLKMKENELRhlrgaeigVVFQEp 99
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS-----AGELLAGTAPLAEAREDTR--------LMFQD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLILHTKASAqerrsliLDMLKRVGIRDPEGalsSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK11247 90 -ARLLPWKKVIDNVGLGLKGQWRDAA-------LQALAAVGLADRAN---EWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 180 EPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-243 |
1.01e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.35 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 25 KSVSFDLAPGEIFGIVGESGSGK-TLAtraliSLLPPTIKVADGSVSYKGRDVlkmKENELRHLRgAEIGVVFQEPmtsl 103
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKsTIA-----NLLTRFYDIDEGEILLDGHDL---RDYTLASLR-NQVALVSQNV---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 104 npsmtigrQLEEGLILHTKASAQErrslilDMLKRVGIRdpEGALSSYPHEF-------------------SGGMRQRIM 164
Cdd:PRK11176 427 --------HLFNDTIANNIAYART------EQYSREQIE--EAARMAYAMDFinkmdngldtvigengvllSGGQRQRIA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEgtAILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
288-502 |
1.39e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKP--KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLNCQMVFQd 365
Cdd:TIGR01257 932 KNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQ- 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 pYSSLDPRMTiealVEEALRPVPGLDGKAKRKRTLET---LEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLI 442
Cdd:TIGR01257 1011 -HNILFHHLT----VAEHILFYAQLKGRSWEEAQLEMeamLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 443 ADEPVSALDVTVRAQVLDLFsdLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
22-242 |
1.48e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.91 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTLATralislLPPTIKVAD-GSVSYK------GRDVLKMKENELRHLRGAEigv 94
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGA------LPAHV*GPDaGRRPWRf*twcaNRRALRRTIG*HRPVR*GR--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 95 vfQEPMTSLNPSMTIGRQLEeglilhtkASAQERRSLILDMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVMLLKPA 174
Cdd:NF000106 98 --RESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 175 LLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDL 242
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-245 |
1.57e-11 |
|
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: 67.28 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLpptiKVADGSVSYKGRDVLKMKENELRhlrgAEIGVVFQEPM-- 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN----ESAEGEIIIDGLNIAKIGLHDLR----FKITIIPQDPVlf 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 -----TSLNPsmtIGRQLEEGLI-------LHTKASAQERRsliLDMlkrvgiRDPEGAlssypHEFSGGMRQRIMLASV 168
Cdd:TIGR00957 1373 sgslrMNLDP---FSQYSDEEVWwalelahLKTFVSALPDK---LDH------ECAEGG-----ENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 169 MLLKPALLIADEPTTALDavIQRDVMELMVELTRAEGTAILLISHDLPMVARYTsRIVVMEKGAIVEKGRTEDLLKA 245
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVD--LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
288-509 |
1.59e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.84 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 288 KSLFRKNKPKR---ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTdyrlncqmvfq 364
Cdd:PRK13545 25 KDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 365 dpySSLDPRMT-IEALveealrPVPGLDGKAKRKRTLETLEEVglgVDYA--GRYPHE----LSGGQRQRVAIARAIARR 437
Cdd:PRK13545 94 ---SGLNGQLTgIENI------ELKGLMMGLTKEKIKEIIPEI---IEFAdiGKFIYQpvktYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 438 PRFLIADEPVSALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTIFD 509
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
289-499 |
1.66e-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: 63.44 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 289 SLFRKNKPKRA-LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES---EGRIQFQGRPRTENWTDYRLNCQMVFQ 364
Cdd:cd03233 11 FTTGKGRSKIPiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 365 DpySSLDPRMTIEALVEEALRpvpgLDGkakrkrtletleevglgvdyaGRYPHELSGGQRQRVAIARAIARRPRFLIAD 444
Cdd:cd03233 91 E--DVHFPTLTVRETLDFALR----CKG---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 445 EPVSALDvtvRAQVLDLFSDLQKrygfsclfISHDLGVVEQVA------------DRVVVMQDGRII 499
Cdd:cd03233 144 NSTRGLD---SSTALEILKCIRT--------MADVLKTTTFVSlyqasdeiydlfDKVLVLYEGRQI 199
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
292-502 |
1.75e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 292 RKNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES--EGRIQFQGRPRTENwTDYRLNcqMVFQDpySS 369
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ-ILKRTG--FVTQD--DI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 LDPRMTI-EALVEEALRPVPGLDGKAKRKRTLET-LEEVGL----GVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIA 443
Cdd:PLN03211 151 LYPHLTVrETLVFCSLLRLPKSLTKQEKILVAESvISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 444 DEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEG 502
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
300-528 |
1.77e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQ-------------D 365
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQspvlfsgtvrfniD 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 PYSSLDPRMTIEAL----VEEALRPVP-GLDGkakrkrtletleEVGLGVDyagryphELSGGQRQRVAIARAIARRPRF 440
Cdd:PLN03232 1332 PFSEHNDADLWEALerahIKDVIDRNPfGLDA------------EVSEGGE-------NFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDLQKrygfSC--LFISHDLGVVEQvADRVVVMQDGRIIEegdrdtiFDSPKE----- 513
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIREEFK----SCtmLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQEllsrd 1460
|
250
....*....|....*..
gi 1681691554 514 --AYTRRLLSAIPALDQ 528
Cdd:PLN03232 1461 tsAFFRMVHSTGPANAQ 1477
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-234 |
2.22e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 22 QVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENelRHLRGAeIGVVFQEpmT 101
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIMREA-VAIVPEG--R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSsypheFSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PRK11614 90 RVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 182 TTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV 234
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
298-507 |
2.29e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTlGRTIAGLVTESEGRiqfqgRP-RTENWTDYRLNCQMVF----------QDP 366
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR-----RPwRF*TWCANRRALRRTIg*hrpvr*grRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 YSSLDPRMTIEALVEealrpvpgLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEP 446
Cdd:NF000106 101 FSGRENLYMIGR*LD--------LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 447 VSALDVTVRAQVLDLFSDLQkRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-213 |
2.42e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 11 GLSLEVARtgQQVVKSVSFDLAPGEIFGIVGESGSGKTlatralisllppTIkvadgsvsykgrdvlkmkeneLRHLRGA 90
Cdd:COG2401 35 GVELRVVE--RYVLRDLNLEIEPGEIVLIVGASGSGKS------------TL---------------------LRLLAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 EIGV----VFQEPMTSLNPSMTIgrqLEEGLILHTKASAQERrslildmLKRVGIRDPEGALSSYpHEFSGGMRQRIMLA 166
Cdd:COG2401 80 LKGTpvagCVDVPDNQFGREASL---IDAIGRKGDFKDAVEL-------LNAVGLSDAVLWLRRF-KELSTGQKFRFRLA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 167 SVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISH 213
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-249 |
2.97e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKgrDVLKMKENELRHLRgAEIGVVFQ 97
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT----EGDIIIN--DSHNLKDINLKWWR-SKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMT--------------SLNPSMTIGRQLEE---------------------------------GLILHTKASAQERRS 130
Cdd:PTZ00265 468 DPLLfsnsiknnikyslySLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsnELIEMRKNYQTIKDS 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 131 LILDMLKRVGIRDPEGAL--------SSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTR 202
Cdd:PTZ00265 548 EVVDVSKKVLIHDFVSALpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1681691554 203 AEGTAILLISHDLPMVaRYTSRIVVMEKGaivEKGRTEDLLKAPQHP 249
Cdd:PTZ00265 628 NENRITIIIAHRLSTI-RYANTIFVLSNR---ERGSTVDVDIIGEDP 670
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
298-507 |
3.24e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQ--FQGRPR----------TENWTdyRLNCQMVFQD 365
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFSHITRlsfeqlqklvSDEWQ--RNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 366 PYSSldPRMTIEALveealrpvpgLDGKAKRKRTLETLEEVGLGVDYAGRYPHeLSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK10938 95 EDDT--GRTTAEII----------QDEVKDPARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVMQDGRIIEEGDRDTI 507
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-248 |
3.40e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLP----PTIKVADGSVSYKGRDVLKMKENELRHLRG 89
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaPRGARVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 90 -----AEIGVVFqepmtSLNPSMTIGRqleeglILHTK---ASAQERRSLILDMLKRVGirdPEGALSSYPHEFSGGMRQ 161
Cdd:PRK13547 87 vlpqaAQPAFAF-----SAREIVLLGR------YPHARragALTHRDGEIAWQALALAG---ATALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 162 RIMLASVM---------LLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGA 232
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGA 232
|
250
....*....|....*.
gi 1681691554 233 IVEKGRTEDLLKaPQH 248
Cdd:PRK13547 233 IVAHGAPADVLT-PAH 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-231 |
3.96e-11 |
|
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: 60.93 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVarTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLpptikvADGSVSYKGrdvlkmkenELRH 86
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI------AGELEPDEG---------IVTW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGAEIGVVFQepmtslnpsmtigrqleeglilhtkasaqerrslildmlkrvgirdpegalssypheFSGGMRQRIMLA 166
Cdd:cd03221 60 GSTVKIGYFEQ---------------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 167 SVMLLKPALLIADEPTTALDaVIQRDVMElmVELTRAEGTaILLISHDLPMVARYTSRIVVMEKG 231
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLD-LESIEALE--EALKEYPGT-VILVSHDRYFLDQVATKIIELEDG 143
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-263 |
4.01e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlpptIKVADGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEPMTS 102
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI----VELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 lnpSMTIGRQLEEgLILHTKASAQE--RRSLILDMLKrvgiRDPEG---ALSSYPHEFSGGMRQRIMLASVMLLKPALLI 177
Cdd:PLN03232 1323 ---SGTVRFNIDP-FSEHNDADLWEalERAHIKDVID----RNPFGldaEVSEGGENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTAL----DAVIQRDVMELMVELTraegtaILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLKAPQHPYTKK 253
Cdd:PLN03232 1395 LDEATASVdvrtDSLIQRTIREEFKSCT------MLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
250
....*....|
gi 1681691554 254 LLSSLPFRGR 263
Cdd:PLN03232 1468 VHSTGPANAQ 1477
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-247 |
4.05e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDV--LKMKEnelRHLRGaeIGVVFQ 97
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD----SGRIFLDGEDIthLPMHK---RARLG--IGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPmtslnpsmTIGRQL--EEGL--IL-HTKASAQERRSLILDMLKRVGI---RD-PEGALssyphefSGGMRQRIMLASV 168
Cdd:COG1137 86 EA--------SIFRKLtvEDNIlaVLeLRKLSKKEREERLEELLEEFGIthlRKsKAYSL-------SGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 169 MLLKPALLIADEPTTALD--AVIqrDVMELMVELtRAEGTAILLISHDlpmvARYTSRIV----VMEKGAIVEKGRTEDL 242
Cdd:COG1137 151 LATNPKFILLDEPFAGVDpiAVA--DIQKIIRHL-KERGIGVLITDHN----VRETLGICdrayIISEGKVLAEGTPEEI 223
|
....*
gi 1681691554 243 LKAPQ 247
Cdd:COG1137 224 LNNPL 228
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-273 |
4.19e-11 |
|
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: 59.30 E-value: 4.19e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1681691554 233 IVEKGRTEDLLKAPQHPYTKKLLSSLPFRGRPRQiDLTSVP 273
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDR-KLISIP 41
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
309-493 |
7.73e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 309 EGEVVALVGGSGSGKTTLGRTIAGLVTESEGRiqFQGRPRTENWTDY----RLncQMVFQDPYS-----SLDPRMtIEAL 379
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSWDEVLKRfrgtEL--QNYFKKLYNgeikvVHKPQY-VDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 -------VEEALRPVpglDgkaKRKRTLETLEEVGLG--VDyagRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSAL 450
Cdd:PRK13409 173 pkvfkgkVRELLKKV---D---ERGKLDEVVERLGLEniLD---RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1681691554 451 DVTVRAQVLDLFSDLQKryGFSCLFISHDLGVVEQVADRVVVM 493
Cdd:PRK13409 244 DIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-247 |
9.87e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 13 SLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVADGSVSykgrdVLKMKEnelRHLRG 89
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdagNIIIDDEDIS-----LLPLHA---RARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 90 aeIGVVFQEPmtSLNPSMTIGRQLEEGLILHTKASAQERRSLILDMLKRVGIRDPEGALSsypHEFSGGMRQRIMLASVM 169
Cdd:PRK10895 80 --IGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 170 LLKPALLIADEPTTALDAVIQRDVMELmVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRI-IEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-247 |
1.07e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGRDVLKMKENELRHlrgaeigvvfQEPMTS 102
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKS----TLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR----------QFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 LNPSM---TIGRQLEEGLilhtKASAQErrslILDMLKRVGIRD----PEGALSSYPHE----FSGGMRQRIMLASVMLL 171
Cdd:PTZ00243 1391 QDPVLfdgTVRQNVDPFL----EASSAE----VWAALELVGLRErvasESEGIDSRVLEggsnYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 172 K-PALLIADEPTT----ALDAVIQRDVMELMVELTraegtaILLISHDLPMVARYtSRIVVMEKGAIVEKGRTEDLLKAP 246
Cdd:PTZ00243 1463 KgSGFILMDEATAnidpALDRQIQATVMSAFSAYT------VITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
.
gi 1681691554 247 Q 247
Cdd:PTZ00243 1536 Q 1536
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
124-451 |
1.21e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 124 SAQERRSLILDMLKRVGI---RD-PEGALSsyphefsGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVE 199
Cdd:NF033858 109 DAAERRRRIDELLRATGLapfADrPAGKLS-------GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 200 LtRAEGTAILLIshdlpmVA--------RYtSRIVVMEKGAIVEKGRTEDLLKAPQhpyTKKL----LSSLPFRGR---- 263
Cdd:NF033858 182 I-RAERPGMSVL------VAtaymeeaeRF-DWLVAMDAGRVLATGTPAELLARTG---ADTLeaafIALLPEEKRrghq 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 264 -----PRQIDLTSVPMISARDIIvdyagrkslfrknkpKR-----ALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL 333
Cdd:NF033858 251 pvvipPRPADDDDEPAIEARGLT---------------MRfgdftAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 334 VTESEGRIQFQGRPrtenwtdyrlncqmVfqDPySSLDPRMTI-----------EALVEEAL----RpVPGLDGKAKRKR 398
Cdd:NF033858 316 LPASEGEAWLFGQP--------------V--DA-GDIATRRRVgymsqafslygELTVRQNLelhaR-LFHLPAAEIAAR 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 399 TLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:NF033858 378 VAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
293-451 |
1.30e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTL-----GRTIAGLVTeseGRIQFQGRPRTENWTDYRLNCQMvfQDPY 367
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlaGRKTAGVIT---GEILINGRPLDKNFQRSTGYVEQ--QDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 368 SSldprmtiEALVEEALRPVPGLDGkakrkrtletleevglgvdyagrypheLSGGQRQRVAIARAIARRPRFLIADEPV 447
Cdd:cd03232 91 SP-------NLTVREALRFSALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
....
gi 1681691554 448 SALD 451
Cdd:cd03232 137 SGLD 140
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-243 |
1.70e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlpptIKVADGSVSYKGRDVLKMKENELRHLrgaeIGVVFQEPMTS 102
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI----VELERGRILIDGCDISKFGLMDLRKV----LGIIPQAPVLF 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 lnpSMTIGRQLEEgLILHTKASAQErrSLILDMLKRVGIRDPEG---ALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PLN03130 1326 ---SGTVRFNLDP-FNEHNDADLWE--SLERAHLKDVIRRNSLGldaEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 180 EPTTAL----DAVIQRDVMELMVELTraegtaILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLL 243
Cdd:PLN03130 1400 EATAAVdvrtDALIQKTIREEFKSCT------MLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-479 |
1.93e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 29 FDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKgRDVL--KMKENELRHLRG----------AEIG--- 93
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKS----TLMKILNGEVLLDDGRIIYE-QDLIvaRLQQDPPRNVEGtvydfvaegiEEQAeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 94 --------VVFQEPMTS-LNPSMTIGRQLEeglilHTKASAQERRslILDMLKRVGIrDPEGALSsyphEFSGGMRQRIM 164
Cdd:PRK11147 99 kryhdishLVETDPSEKnLNELAKLQEQLD-----HHNLWQLENR--INEVLAQLGL-DPDAALS----SLSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAviqrDVMELMVELTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIV---------- 234
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVsypgnydqyl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 235 ----EKGRTEDLLKApqhPYTKKLLSS-------LPFR-----GRPRQIDLTSVPMISARDII------VDYAGR--KSL 290
Cdd:PRK11147 243 lekeEALRVEELQNA---EFDRKLAQEevwirqgIKARrtrneGRVRALKALRRERSERREVMgtakmqVEEASRsgKIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 291 FRKNK------PKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRlncqmvfq 364
Cdd:PRK11147 320 FEMENvnyqidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 365 dpySSLDPRMTIEALVEEALRPVPgLDGKA--------------KRKRTletleevglgvdyagryP-HELSGGQRQRVA 429
Cdd:PRK11147 392 ---AELDPEKTVMDNLAEGKQEVM-VNGRPrhvlgylqdflfhpKRAMT-----------------PvKALSGGERNRLL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 430 IARAIARRPRFLIADEPVSALDVtvraQVLDLFSDLQKRYGFSCLFISHD 479
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
300-460 |
2.01e-10 |
|
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: 61.80 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR----PRTENWTDYRLNCQMVFQDPYSSLDPRMT 375
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfsSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEAL-VEEALRPVPGLDGKakrkrtleTLEEVGLgvdyagryphELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:cd03291 133 VKACqLEEDITKFPEKDNT--------VLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
....*.
gi 1681691554 455 RAQVLD 460
Cdd:cd03291 195 EKEIFE 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
300-478 |
2.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLncQMVFQDPYSSLDPRMTieaL 379
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK--QLCFVGHRSGINPYLT---L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 380 VEEALRPVPGLDGkAKRKRTLETLEEVGLGVDYAGRYpheLSGGQRQRVAIARAIARRPRFLIADEPVSALDvtvRAQVL 459
Cdd:PRK13540 92 RENCLYDIHFSPG-AVGITELCRLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLL 164
|
170 180
....*....|....*....|.
gi 1681691554 460 DLFSDLQ--KRYGFSCLFISH 478
Cdd:PRK13540 165 TIITKIQehRAKGGAVLLTSH 185
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-491 |
2.55e-10 |
|
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: 63.11 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVM--LLKPALLIADEPTTALDaviQRDVMELMVELT--RAEGTAILLISHDLPMVaRYTSRIVVMEKG 231
Cdd:TIGR00630 490 SGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLH---QRDNRRLINTLKrlRDLGNTLIVVEHDEDTI-RAADYVIDIGPG 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 232 A------IVEKGRTEDLLKAPQHpytkklLSSLPFRGRpRQIdltSVPMISARdiivdyAGRKSLFRKNKPKRALHGVSI 305
Cdd:TIGR00630 566 AgehggeVVASGTPEEILANPDS------LTGQYLSGR-KKI---EVPAERRP------GNGKFLTLKGARENNLKNITV 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 306 DIHEGEVVALVGGSGSGKTTL---------------GRTIAGLVTESEG------------------------------- 339
Cdd:TIGR00630 630 SIPLGLFTCITGVSGSGKSTLindtlypalanrlngAKTVPGRYTSIEGlehldkvihidqspigrtprsnpatytgvfd 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 340 --RIQFQGRP--RTENWTDYRLN----------CQ--------MVF-QDPYSSLDP-------RMTIEA----------- 378
Cdd:TIGR00630 710 eiRELFAETPeaKVRGYTPGRFSfnvkggrceaCQgdgvikieMHFlPDVYVPCEVckgkrynRETLEVkykgkniadvl 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 --LVEEALR---PVPGLdgkakrKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARR---PRFLIADEPVSAL 450
Cdd:TIGR00630 790 dmTVEEAYEffeAVPSI------SRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL 863
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1681691554 451 ---DVtvrAQVLDLFSDLQKRyGFSCLFISHDLGVVeQVADRVV 491
Cdd:TIGR00630 864 hfdDI---KKLLEVLQRLVDK-GNTVVVIEHNLDVI-KTADYII 902
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-245 |
2.75e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGK-TLAtraliSLLPPTIKVADGSVSYKGRDVLKMKENELRHlrgaEIGVVF 96
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKsTLA-----SLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ----GVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 97 QEPMT---SLNPSMTIGRQLEEGLI---LHTKASAQERRSLildmlkrvgirdPEG---ALSSYPHEFSGGMRQRIMLAS 167
Cdd:PRK10790 422 QDPVVladTFLANVTLGRDISEEQVwqaLETVQLAELARSL------------PDGlytPLGEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVMELMVELTraEGTAILLISHDLPMVARYTSrIVVMEKGAIVEKGRTEDLLKA 245
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVVIAHRLSTIVEADT-ILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
300-496 |
2.99e-10 |
|
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: 60.42 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR-PRTENWTDYRLNCQmvFQDPYSSLDPRMtIEA 378
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNR--YSVAYAAQKPWL-LNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 379 LVEEALRpvpgLDGKAKRKRTLETLEEVGLGVDY----------AGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVS 448
Cdd:cd03290 94 TVEENIT----FGSPFNKQRYKAVTDACSLQPDIdllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 449 ALDV-----TVRAQVLDLFSDlQKRygfSCLFISHDLGVVEQvADRVVVMQDG 496
Cdd:cd03290 170 ALDIhlsdhLMQEGILKFLQD-DKR---TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-479 |
4.86e-10 |
|
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: 61.87 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTlatraliSLLpptiKVADGsvsykgrdVLKMKENELRHLRGAEIGVVFQEP 99
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKS-------TLL----RIMAG--------VDKDFNGEARPQPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mtSLNPSMTIGRQLEEGLilHTKASAQER---------------RSLILDMLKRVGIRDPEG-------------ALSSY 151
Cdd:TIGR03719 78 --QLDPTKTVRENVEEGV--AEIKDALDRfneisakyaepdadfDKLAAEQAELQEIIDAADawdldsqleiamdALRCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 152 PHE-----FSGGMRQRIMLASVMLLKPALLIADEPTTALDAviqRDVMELMVELTRAEGTaILLISHD------------ 214
Cdd:TIGR03719 154 PWDadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPGT-VVAVTHDryfldnvagwil 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 215 -------LPMVARYTS-------RIVVMEKGaivEKGRTEDLL----------KAPQHPYTKKL-----LSSLPFRGRPR 265
Cdd:TIGR03719 230 eldrgrgIPWEGNYSSwleqkqkRLEQEEKE---ESARQKTLKrelewvrqspKGRQAKSKARLaryeeLLSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 266 QIDLTSVP-------MISARDIIVDYaGRKSLFRknkpkralhGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESE 338
Cdd:TIGR03719 307 TAEIYIPPgprlgdkVIEAENLTKAF-GDKLLID---------DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 339 GRIQF----------QGRprtenwtdyrlncqmvfqdpySSLDPRMTIEALVEEalrpvpGLDGKAKRKRTLETLEEVGL 408
Cdd:TIGR03719 377 GTIEIgetvklayvdQSR---------------------DALDPNKTVWEEISG------GLDIIKLGKREIPSRAYVGR 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 409 ----GVDYAGRYpHELSGGQRQRVAIARAIARRPRFLIADEPVSALDV-TVRA--QVLDLFSDlqkrygfSCLFISHD 479
Cdd:TIGR03719 430 fnfkGSDQQKKV-GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRAleEALLNFAG-------CAVVISHD 499
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
168-478 |
5.43e-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: 62.07 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRdvmELMVELTRAEGTAILLIsHDLPMVARYTSRIVVM------EKGAIVEKGRTED 241
Cdd:TIGR00954 350 FDKTHPAFLEMSEEELMQEFYNNG---RLLLKAADALGRLMLAG-RDMTRLAGFTARVDTLlqvlddVKSGNFKRPRVEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 242 LLKAPQHPYTKKLLsslPFRGRPRQID----LTSVPMISARDIIVdyagrkslfrknkpkraLHGVSIDIHEGEVVALVG 317
Cdd:TIGR00954 426 IESGREGGRNSNLV---PGRGIVEYQDngikFENIPLVTPNGDVL-----------------IESLSFEVPSGNNLLICG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 318 GSGSGKTTLGRTIAGLVTESEGRIQfqgRPRtenwtdyrlNCQMVF--QDPYssldprMTIEALVEEALRPVPGLDGKAK 395
Cdd:TIGR00954 486 PNGCGKSSLFRILGELWPVYGGRLT---KPA---------KGKLFYvpQRPY------MTLGTLRDQIIYPDSSEDMKRR 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 396 --RKRTLET-LEEVGL--------GVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRaqvlDLFSD 464
Cdd:TIGR00954 548 glSDKDLEQiLDNVQLthileregGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYR 623
|
330
....*....|....
gi 1681691554 465 LQKRYGFSCLFISH 478
Cdd:TIGR00954 624 LCREFGITLFSVSH 637
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
298-499 |
6.01e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTENWTDYRLN--CQMVFQDPyssldpRMT 375
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEngISMVHQEL------NLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALVEEAL----RPVPGL--DGKAKRKRTLETLEEVGLGVDyagryPHE----LSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK10982 86 LQRSVMDNMwlgrYPTKGMfvDQDKMYRDTKAIFDELDIDID-----PRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 446 PVSALdvtVRAQVLDLFSDLQK--RYGFSCLFISHDLGVVEQVADRVVVMQDGRII 499
Cdd:PRK10982 161 PTSSL---TEKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
217-518 |
1.23e-09 |
|
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: 61.11 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 217 MVARYTSRIVVMEKgaIVEKGRTEDllKAPQHPYTKKLLSSLPFRGRprqidltsvpmISARDIIVDYagRKSLfrknkp 296
Cdd:TIGR00957 1242 MSSEMETNIVAVER--LKEYSETEK--EAPWQIQETAPPSGWPPRGR-----------VEFRNYCLRY--REDL------ 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDP-YSSLDPRM 374
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDLRFKITIIPQDPvLFSGSLRM 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEEALRPVPGLDGKAKRKRTLETLEEvglGVDYAGRYPHE-LSGGQRQRVAIARAIARRPRFLIADEPVSALDV- 452
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWWALELAHLKTFVSALPD---KLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVDLe 1455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 453 -------TVRAQvldlFSDLqkrygfSCLFISHDLGVVEQVAdRVVVMQDGRIIEegdrdtiFDSPKEAYTRR 518
Cdd:TIGR00957 1456 tdnliqsTIRTQ----FEDC------TVLTIAHRLNTIMDYT-RVIVLDKGEVAE-------FGAPSNLLQQR 1510
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
307-451 |
1.23e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 307 IHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTenwtdyrlNCQMVFQDPYSSLDPRMTIEALVEEALRP 386
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--------RGDRSRFMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 387 VPGLDGKAKRKRTLETLEEVGLgVDYAGRYPHELSGGQRQRVAIARA-IARRPRFLIaDEPVSALD 451
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLD 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-233 |
1.25e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLpptiKVADGSVSYKGRDVLKMKENElrhlRGaeIGVVFQEp 99
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE----RITSGEIWIGGRVVNELEPAD----RD--IAMVFQN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 mTSLNPSMTIGRQLEEGLILHtKASAQERRSLILDMLKRVGIrdpEGALSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK11650 85 -YALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILEL---EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 180 EPTTALDAVIqRDVMELMV-ELTRAEGTAILLISHDlpMVARYT--SRIVVMEKGAI 233
Cdd:PRK11650 160 EPLSNLDAKL-RVQMRLEIqRLHRRLKTTSLYVTHD--QVEAMTlaDRVVVMNGGVA 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
300-460 |
1.29e-09 |
|
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: 61.08 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGR----PRTENWTDYRLNCQMVFQDPYSSLDPRMT 375
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfsPQTSWIMPGTIKDNIIFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEAL-VEEALRPVPGLDGKakrkrtleTLEEVGLgvdyagryphELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTV 454
Cdd:TIGR01271 522 IKACqLEEDIALFPEKDKT--------VLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
....*.
gi 1681691554 455 RAQVLD 460
Cdd:TIGR01271 584 EKEIFE 589
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-217 |
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 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVLKMKENELRHLrgaeigvVFQEPM 100
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE----KGEILFERQSIKKDLCTYQKQL-------CFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 TSLNPSMTigrqLEEGLI--LHTKASAQERRSLILDMLKRVGIRDPEGALSSyphefsgGMRQRIMLASVMLLKPALLIA 178
Cdd:PRK13540 83 SGINPYLT----LRENCLydIHFSPGAVGITELCRLFSLEHLIDYPCGLLSS-------GQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1681691554 179 DEPTTALDaviQRDVMELM--VELTRAEGTAILLISH-DLPM 217
Cdd:PRK13540 152 DEPLVALD---ELSLLTIItkIQEHRAKGGAVLLTSHqDLPL 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-232 |
1.89e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 19 TGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRalisLLPPTIKVADGSVSYKGRDVLkmkenelrhlrgAEIGVVFQE 98
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFK----MLTGDTTVTSGDATVAGKSIL------------TNISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 ----PMTSLNPSMTIGRqleEGLILHTK---ASAQERRSLILDMLKRVGIRDPEGALSSyphEFSGGMRQRIMLASVMLL 171
Cdd:TIGR01257 2014 mgycPQFDAIDDLLTGR---EHLYLYARlrgVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 172 KPALLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKGA 232
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
414-495 |
2.37e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 414 GRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDLGVVEQvADRVVVM 493
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVF 1431
|
..
gi 1681691554 494 QD 495
Cdd:PTZ00265 1432 NN 1433
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
309-493 |
2.72e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 309 EGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQ-----------FQGrprTEnWTDYrlncqmvFQDPYS-----SLDP 372
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRG---TE-LQDY-------FKKLANgeikvAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 RMtiealVEEALRPVPG-----LDGKAKRKRTLETLEEVGLG--VDyagRYPHELSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:COG1245 167 QY-----VDLIPKVFKGtvrelLEKVDERGKLDELAEKLGLEniLD---RDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQVADRVVVM 493
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
278-496 |
3.00e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.03 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 278 RDIIVDYAGRKSLFRKNKPKRALHGVS--------IDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRT 349
Cdd:TIGR01257 1925 RQRIISGGNKTDILRLNELTKVYSGTSspavdrlcVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 350 ENWTDYRLNcqMVFQDPYSSLDPRMT-IEALVEEA-LRPVPGldgKAKRKRTLETLEEVGLGVdYAGRYPHELSGGQRQR 427
Cdd:TIGR01257 2005 TNISDVHQN--MGYCPQFDAIDDLLTgREHLYLYArLRGVPA---EEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRK 2078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 428 VAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLqKRYGFSCLFISHDLGVVEQVADRVVVMQDG 496
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-239 |
3.14e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 21 QQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVADGSVsyKGRDVLKMKEN------ELRHLRG-- 89
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKsagTITLHGKKI--NNHNANEAINHgfalvtEERRSTGiy 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 90 AEIGVVFQEPMTSLNPSMTigrqlEEGLILHTKASAqERRSLILDM-LKRVGIRDPEGALSsyphefsGGMRQRIMLASV 168
Cdd:PRK10982 339 AYLDIGFNSLISNIRNYKN-----KVGLLDNSRMKS-DTQWVIDSMrVKTPGHRTQIGSLS-------GGNQQKVIIGRW 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681691554 169 MLLKPALLIADEPTTALDAVIQRDVMELMVELTRaEGTAILLISHDLPMVARYTSRIVVMEKG---AIVEKGRT 239
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGlvaGIVDTKTT 478
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-187 |
3.43e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 32 APGEIFGIVGESGSGKT-----LATRALISLLPPTIKVADGSVSykgRDVLKmkenelrhlrgaEIGVVFQEPMtsLNPS 106
Cdd:PLN03211 92 SPGEILAVLGPSGSGKStllnaLAGRIQGNNFTGTILANNRKPT---KQILK------------RTGFVTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIGRQLE--EGLILHTKASAQERRSLILDMLKRVGIRDPEGAL--SSYPHEFSGGMRQRIMLASVMLLKPALLIADEPT 182
Cdd:PLN03211 155 LTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....*
gi 1681691554 183 TALDA 187
Cdd:PLN03211 235 SGLDA 239
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
234-273 |
4.45e-09 |
|
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: 52.79 E-value: 4.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1681691554 234 VEKGRTEDLLKAPQHPYTKKLLSSLPfRGRPRQIDLTSVP 273
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVP-RLDPPKRPLYTIP 39
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
296-451 |
6.75e-09 |
|
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: 58.41 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 296 PKRA-LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGriqfqgrprtENWTDYRLNCQMVFQDPYssLDPRM 374
Cdd:TIGR03719 16 PKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPGIKVGYLPQEPQ--LDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 TIEALVEEALRPVPGL------------------DGKAKRKRTLETLEEVGLGVDY---------AGRYP------HELS 421
Cdd:TIGR03719 84 TVRENVEEGVAEIKDAldrfneisakyaepdadfDKLAAEQAELQEIIDAADAWDLdsqleiamdALRCPpwdadvTKLS 163
|
170 180 190
....*....|....*....|....*....|
gi 1681691554 422 GGQRQRVAIARAIARRPRFLIADEPVSALD 451
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-209 |
6.86e-09 |
|
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: 55.73 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 18 RTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTIKVaDGSVSYKGRDVLKMKENELRHlrgaeigVVFQ 97
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV-EGDIHYNGIPYKEFAEKYPGE-------IIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMTSLNPSMTIGRQLEeglilhTKASAQERRSLildmlkRVgirdpegalssypheFSGGMRQRIMLASVMLLKPALLI 177
Cdd:cd03233 89 SEEDVHFPTLTVRETLD------FALRCKGNEFV------RG---------------ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190
....*....|....*....|....*....|..
gi 1681691554 178 ADEPTTALDAVIQRDVMELMVELTRAEGTAIL 209
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-237 |
1.08e-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: 58.49 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkENELRHLRGAeIGVVFQEP 99
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT----SGTVLVGGKDI----ETNLDAVRQS-LGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MtsLNPSMTIGRQLEegLILHTKASAQERRSLILD-MLKRVGI---RDPEGalssypHEFSGGMRQRIMLASVMLLKPAL 175
Cdd:TIGR01257 1013 I--LFHHLTVAEHIL--FYAQLKGRSWEEAQLEMEaMLEDTGLhhkRNEEA------QDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681691554 176 LIADEPTTALDAVIQRDVMELMveLTRAEGTAILLISHDLPMVARYTSRIVVMEKGAIVEKG 237
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
303-511 |
1.19e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 303 VSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGrprTENWTD-----YRLNCQMVFQDP----------- 366
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDinlkwWRSKIGVVSQDPllfsnsiknni 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 ------------------------YSSLDPRMTIEALVEEALRPV------PGLDGKAKRKRTLETLEEVGLGV-----D 411
Cdd:PTZ00265 481 kyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNDMsnttdsNELIEMRKNYQTIKDSEVVDVSKkvlihD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 412 YAGRYP-----------HELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDLQKRYGFSCLFISHDL 480
Cdd:PTZ00265 561 FVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
250 260 270
....*....|....*....|....*....|.
gi 1681691554 481 GVVeQVADRVVVMQDGRIIEEGDRDTIFDSP 511
Cdd:PTZ00265 641 STI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
306-494 |
1.53e-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: 54.50 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 306 DIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFqgrprtenwtdyrlncqmvfqdpyssldPRMTIEalveealr 385
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW----------------------------DGITPV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 386 pvpgldgkakrkrtletleevglgvdYAGRYPhELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSDL 465
Cdd:cd03222 65 --------------------------YKPQYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 1681691554 466 QKRYGFSCLFISHDLGVVEQVADRVVVMQ 494
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-251 |
1.89e-08 |
|
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: 55.69 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLlpptIKVADGSVSYKGRDVLKMKENELRhlrgAEIGVVFQEPMTS 102
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM----VDIFDGKIVIDGIDISKLPLHTLR----SRLSIILQDPILF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 103 lnpSMTIGRQLEEglilhTKASAQER--RSLILDMLKRVgIRDPEGALSSYPHE----FSGGMRQRIMLASVMLLKPALL 176
Cdd:cd03288 108 ---SGSIRFNLDP-----ECKCTDDRlwEALEIAQLKNM-VKSLPGGLDAVVTEggenFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681691554 177 IADEPTTALDA----VIQRDVMELMVELTraegtaILLISHDLPMVARyTSRIVVMEKGAIVEKGRTEDLLKAPQHPYT 251
Cdd:cd03288 179 IMDEATASIDMatenILQKVVMTAFADRT------VVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-229 |
2.31e-08 |
|
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: 55.11 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 1 MTMDKllTVCGLSLEVARTgqqvvksvsfDLAPGEIFGIVGESGSGKTLATRALISLLPPT---IKVADGSVSYKGRDVL 77
Cdd:cd03237 4 PTMKK--TLGEFTLEVEGG----------SISESEVIGILGPNGIGKTTFIKMLAGVLKPDegdIEIELDTVSYKPQYIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 78 KMKENELRHLrgaeigvvfqepMTSLNPSMTIGRQLeeglilhtkasaqerRSLILDMLKRVGIRDPEgalssyPHEFSG 157
Cdd:cd03237 72 ADYEGTVRDL------------LSSITKDFYTHPYF---------------KTEIAKPLQIEQILDRE------VPELSG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 158 GMRQRIMLASVmLLKPA-LLIADEPTTALDA--------VIQRDVMElmveltrAEGTAiLLISHDLPMVARYTSRIVVM 228
Cdd:cd03237 119 GELQRVAIAAC-LSKDAdIYLLDEPSAYLDVeqrlmaskVIRRFAEN-------NEKTA-FVVEHDIIMIDYLADRLIVF 189
|
.
gi 1681691554 229 E 229
Cdd:cd03237 190 E 190
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
374-491 |
7.23e-08 |
|
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: 53.77 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTiealVEEALR---PVPGLdgkakrKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPR---FLIADEPV 447
Cdd:cd03271 131 MT----VEEALEffeNIPKI------ARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPT 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1681691554 448 SAL---DVTVRAQVLDLFSDLqkryGFSCLFISHDLGVVeQVADRVV 491
Cdd:cd03271 201 TGLhfhDVKKLLEVLQRLVDK----GNTVVVIEHNLDVI-KCADWII 242
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
310-482 |
7.55e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 310 GEVVALVGGSGSGKTTLGRTIAGLVTESEGRIqfqgrprtenwtdYRLNCQMVFQDPYSSLDprmtiealveealrpvpg 389
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-------------IYIDGEDILEEVLDQLL------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 390 ldgkakrkrtletleevglgVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVRAQVLDLFSD----- 464
Cdd:smart00382 51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllll 110
|
170
....*....|....*...
gi 1681691554 465 LQKRYGFSCLFISHDLGV 482
Cdd:smart00382 111 LKSEKNLTVILTTNDEKD 128
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-186 |
8.90e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 14 LEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGK-----TLATRAlisllppTIKVADGSVSYKGRDVLKMKENElrhlR 88
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKstlsaTLAGRE-------DYEVTGGTVEFKGKDLLELSPED----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 89 GAE-IGVVFQEPM------------TSLNPSMTIGRQleEGLILHTKASAQERRSLILDMlkrvgirdPEGALS-SYPHE 154
Cdd:PRK09580 76 AGEgIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLDRFDFQDLMEEKIALLKM--------PEDLLTrSVNVG 145
|
170 180 190
....*....|....*....|....*....|..
gi 1681691554 155 FSGGMRQRIMLASVMLLKPALLIADEPTTALD 186
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
297-503 |
1.02e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 297 KRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGL--VTESEGRIQFQGRPRTENWTDYRL--NCQMVFQDPYSSldP 372
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgeGIFMAFQYPVEI--P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 373 RMTIEALVEEALRPVPGLDGKAKRKR------TLETLEEVGLGVDYAGRYPHE-LSGGQRQRVAIARAIARRPRFLIADE 445
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRGQEPLDRfdfqdlMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQ--KRygfSCLFISHDLGVVEQVA-DRVVVMQDGRIIEEGD 503
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRdgKR---SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-252 |
2.27e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 151 YPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLISHDLPMVARyTSRIVVMEK 230
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
90 100
....*....|....*....|....*..
gi 1681691554 231 ----GAIVE-KGRTEDLLKAPQHPYTK 252
Cdd:PTZ00265 1434 pdrtGSFVQaHGTHEELLSVQDGVYKK 1460
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-215 |
3.30e-07 |
|
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: 51.60 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 32 APGEIFGIVGESGSGKTLATRALISLLPPTIKVADGSVSYkgRDVLK-MKENELRH----LRGAEIGVVFQEPMTSLNPS 106
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDW--DEILDeFRGSELQNyftkLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIGRQLEegliLHTKASAQERRSLILDMLKRVGIRDPEgalssyPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALD 186
Cdd:cd03236 102 AVKGKVGE----LLKKKDERGKLDELVDQLELRHVLDRN------IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|
gi 1681691554 187 aVIQR-DVMELMVELTRaEGTAILLISHDL 215
Cdd:cd03236 172 -IKQRlNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-234 |
3.45e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 4 DKLLTVCGLSlevartGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRDVlkmkenE 83
Cdd:PRK11288 255 EVRLRLDGLK------GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRT----AGQVYLDGKPI------D 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 84 LRHLRGA-EIGVVF------QE---PMTSLNPSMTI---GRQLEEGLILHTKASAQERRSLILDM-LKRVGIRDPEGALs 149
Cdd:PRK11288 319 IRSPRDAiRAGIMLcpedrkAEgiiPVHSVADNINIsarRHHLRAGCLINNRWEAENADRFIRSLnIKTPSREQLIMNL- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 150 syphefSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIVVME 229
Cdd:PRK11288 398 ------SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMR 470
|
....*
gi 1681691554 230 KGAIV 234
Cdd:PRK11288 471 EGRIA 475
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-247 |
3.56e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 25 KSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPT---IKVADGSVSykgrDVLKMKenelrhlRGaeIGVVFQEpmT 101
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITsgdLFIGEKRMN----DVPPAE-------RG--VGMVFQS--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 102 SLNPSMTIGRQLEEGLILH--TKASAQERRSLILDMLKRVGIrdpegaLSSYPHEFSGGMRQRIMLASVMLLKPALLIAD 179
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAgaKKEEINQRVNQVAEVLQLAHL------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 180 EPTTALDAVIQrdvMELMVELTRAE---GTAILLISHDLPMVARYTSRIVVMEKGAIVEKGRTEDLLKAPQ 247
Cdd:PRK11000 159 EPLSNLDAALR---VQMRIEISRLHkrlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-231 |
3.90e-07 |
|
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: 50.93 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 23 VVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVSYKGRdvlkmkenelrhlrgaeIGVVFQEP--M 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL----SGSVSVPGS-----------------IAYVSQEPwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 101 tslnpSMTI------GRQLEEGLILHT-KASAQERRsliLDMLK-----RVGirdpEGALSsypheFSGGMRQRIMLASV 168
Cdd:cd03250 79 -----NGTIrenilfGKPFDEERYEKViKACALEPD---LEILPdgdltEIG----EKGIN-----LSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 169 MLLKPALLIADEPTTALDAVIQRDVME--LMVELtrAEGTAILLISHDLPmVARYTSRIVVMEKG 231
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQ-LLPHADQIVVLDNG 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-234 |
6.84e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKT-LATralisllpptikvadgSV---SYkGRDV-----LKMKENELRHLRGA 90
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAM----------------SVfgrSY-GRNIsgtvfKDGKEVDVSTVSDA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 91 -------------EIGVVFQEPMTSlNPSMTIGRQLEEGLILH----TKASAQERRSLildMLKRVGIRDPEGALSsyph 153
Cdd:NF040905 335 idaglayvtedrkGYGLNLIDDIKR-NITLANLGKVSRRGVIDeneeIKVAEEYRKKM---NIKTPSVFQKVGNLS---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 efsGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTrAEGTAILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:NF040905 407 ---GGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
.
gi 1681691554 234 V 234
Cdd:NF040905 483 T 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
300-459 |
7.27e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTES--EGRIQFQGRPRTENwTDYRLNCQMVFQDPYSsldPRMTI- 376
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQE-TFARISGYCEQNDIHS---PQVTVr 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 377 EALVEEALRPVPGLDGKAKRKR---------TLETLEE--VGL-GVDyagryphELSGGQRQRVAIARAIARRPRFLIAD 444
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKEEKMMfvdevmelvELDNLKDaiVGLpGVT-------GLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170
....*....|....*
gi 1681691554 445 EPVSALDVTVRAQVL 459
Cdd:PLN03140 1045 EPTSGLDARAAAIVM 1059
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
293-451 |
9.89e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 293 KNKPKRALHGVSIDIHEGEVVALVGGSGSGKTTL-----GRTIAGLVTesEGRIQFQGRPRTENW---TDYrlnCQMvfQ 364
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGVIT--GGDRLVNGRPLDSSFqrsIGY---VQQ--Q 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 365 DPYSsldPRMTI-EALVEEALRPVPGLDGKAKRKR---------TLETLEEVGLGVDYAGrypheLSGGQRQRVAIARAI 434
Cdd:TIGR00956 845 DLHL---PTSTVrESLRFSAYLRQPKSVSKSEKMEyveevikllEMESYADAVVGVPGEG-----LNVEQRKRLTIGVEL 916
|
170
....*....|....*...
gi 1681691554 435 ARRPRFLI-ADEPVSALD 451
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLD 934
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
298-502 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLgrtiaglvtesegriqfqgrprtenwtdyrlncqmVFQDPYSSLDPRMtie 377
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------------VNEGLYASGKARL--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 378 alveEALRPVPGlDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPR--FLIADEPVSALDVTVR 455
Cdd:cd03238 51 ----ISFLPKFS-RNKLIFIDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 456 AQVLDLFSDLQKRyGFSCLFISHDLGVVEQvADRVVVM------QDGRIIEEG 502
Cdd:cd03238 126 NQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-188 |
2.65e-06 |
|
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: 50.68 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvADGSVSYKGrdvLKMKENELRH 86
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-----TEGEIQIDG---VSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGAeIGVVfqePMTSLNPSMTIGRQLEEglilHTKASAQErrslILDMLKRVGIRDpegALSSYPHE-----------F 155
Cdd:TIGR01271 1290 WRKA-FGVI---PQKVFIFSGTFRKNLDP----YEQWSDEE----IWKVAEEVGLKS---VIEQFPDKldfvlvdggyvL 1354
|
170 180 190
....*....|....*....|....*....|...
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALDAV 188
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
499-537 |
5.00e-06 |
|
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: 44.31 E-value: 5.00e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1681691554 499 IEEGDRDTIFDSPKEAYTRRLLSAIPALDQNEKGGVTLK 537
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIP 39
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-213 |
5.35e-06 |
|
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: 49.36 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvADGSVSYKGRDvlkmkenelrhlrgaeiGVVFQEP 99
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-----VYGGRLTKPAK-----------------GKLFYVP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MtslNPSMTIGrQLEEGLILHTKASAQERRSL-------ILDMLKRVGIRDPEGALSS---YPHEFSGGMRQRIMLASVM 169
Cdd:TIGR00954 522 Q---RPYMTLG-TLRDQIIYPDSSEDMKRRGLsdkdleqILDNVQLTHILEREGGWSAvqdWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1681691554 170 LLKPALLIADEPTTAldavIQRDVMELMVELTRAEGTAILLISH 213
Cdd:TIGR00954 598 YHKPQFAILDECTSA----VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-238 |
6.20e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 25 KSVSFDLAPGEIFGIVGESGSGKTlatraliSLLPPTIkVADG------SVSYKGRDVL-KMKENELRHLRGAEIGVVFQ 97
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKS-------SLAFDTI-YAEGqrryveSLSAYARQFLgQMDKPDVDSIEGLSPAIAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 98 EPMTSLNPSMTIGRQLE--EGL-ILHTKASAQERrsliLDMLKRVGIrdPEGALSSYPHEFSGGMRQRIMLASV--MLLK 172
Cdd:cd03270 84 QKTTSRNPRSTVGTVTEiyDYLrLLFARVGIRER----LGFLVDVGL--GYLTLSRSAPTLSGGEAQRIRLATQigSGLT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681691554 173 PALLIADEPTTALDaviQRDVMELMVELT--RAEGTAILLISHDLPMVaRYTSRIVVMEKGAIVEKGR 238
Cdd:cd03270 158 GVLYVLDEPSIGLH---PRDNDRLIETLKrlRDLGNTVLVVEHDEDTI-RAADHVIDIGPGAGVHGGE 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-244 |
1.05e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 20 GQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPPTikvaDGSVsykgrdvlKMKENelrhlrgAEIGVV---- 95
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD----SGTV--------KWSEN-------ANIGYYaqdh 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 96 ---FQEPMTsLNPSMTIGRQLEEGlilhtkasAQERRSLILDML-------KRVGIrdpegalssypheFSGGMRQRIML 165
Cdd:PRK15064 392 aydFENDLT-LFDWMSQWRQEGDD--------EQAVRGTLGRLLfsqddikKSVKV-------------LSGGEKGRMLF 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 166 ASVMLLKPALLIADEPTTALDaviqrdvME----LMVELTRAEGTAIlLISHDLPMVARYTSRIV-VMEKGAIVEKGRTE 240
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMD-------MEsiesLNMALEKYEGTLI-FVSHDREFVSSLATRIIeITPDGVVDFSGTYE 521
|
....
gi 1681691554 241 DLLK 244
Cdd:PRK15064 522 EYLR 525
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
315-451 |
1.20e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 315 LVGGSGSGKTTLGRTIAGLVTESEGriqfqgrprtENWTDYRLNCQMVFQDPYssLDPRMTIEALVEEALRPVpgldgKA 394
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG----------EARPAPGIKVGYLPQEPQ--LDPEKTVRENVEEGVAEV-----KA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 395 KRKRTLETLEEVGLGVDY--------------------------------AGRYPH------ELSGGQRQRVAIARAIAR 436
Cdd:PRK11819 101 ALDRFNEIYAAYAEPDADfdalaaeqgelqeiidaadawdldsqleiamdALRCPPwdakvtKLSGGERRRVALCRLLLE 180
|
170
....*....|....*
gi 1681691554 437 RPRFLIADEPVSALD 451
Cdd:PRK11819 181 KPDMLLLDEPTNHLD 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
156-221 |
1.37e-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: 1.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVM---LLKPA-LLIADEPTTALDAVIQRDVMELMVELtRAEGTAILLISHDLPMVARY 221
Cdd:cd03227 79 SGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELA 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-245 |
1.39e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 17 ARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPP---TIKVADGSVSYKGRDV----LKMKENELrhlrg 89
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetSSVVIRGSVAYVPQVSwifnATVRENIL----- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 90 aeIGVVFQepmtslnpSMTIGRQLEEGLILHTkasaqerrsliLDM-----LKRVGIRDPEgalssypheFSGGMRQRIM 164
Cdd:PLN03232 701 --FGSDFE--------SERYWRAIDVTALQHD-----------LDLlpgrdLTEIGERGVN---------ISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 165 LASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTAILLIS--HDLPMVarytSRIVVMEKGAIVEKGRTEDL 242
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNqlHFLPLM----DRIILVSEGMIKEEGTFAEL 826
|
...
gi 1681691554 243 LKA 245
Cdd:PLN03232 827 SKS 829
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
100-326 |
1.59e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 100 MTSLNPSMTIGRQLEEGLilhtkasaQERRSLILDMlkRVGIRDPEGALSSypheFSGGMRQRIMLASVM--LLKPALLI 177
Cdd:PRK00635 436 LSQLPSKSLSIEEVLQGL--------KSRLSILIDL--GLPYLTPERALAT----LSGGEQERTALAKHLgaELIGITYI 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 178 ADEPTTALDAviqRDVMELM--VELTRAEGTAILLISHDLPMVArYTSRIVVMEKGA------IVEKGRTEDLLkAPQHP 249
Cdd:PRK00635 502 LDEPSIGLHP---QDTHKLInvIKKLRDQGNTVLLVEHDEQMIS-LADRIIDIGPGAgifggeVLFNGSPREFL-AKSDS 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 250 YTKKLLsslpfrgrpRQIDLTSVPMISARDIivdyaGRKSLFRKNKpkRALHGVSIDIHEGEVVALVGGSGSGKTTL 326
Cdd:PRK00635 577 LTAKYL---------RQELTIPIPEKRTNSL-----GTLTLSKATK--HNLKDLTISLPLGRLTVVTGVSGSGKSSL 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-248 |
3.08e-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: 46.00 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISLLPptikvADGSVSYKGRDVLKMKeneLRH 86
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-----TEGDIQIDGVSWNSVP---LQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 LRGAeIGVVFQEPMTSLNPsmtigrqLEEGLILHTKASAQErrslILDMLKRVGIRDpegALSSYPHE-----------F 155
Cdd:cd03289 75 WRKA-FGVIPQKVFIFSGT-------FRKNLDPYGKWSDEE----IWKVAEEVGLKS---VIEQFPGQldfvlvdggcvL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALD----AVIQRDVMELMVELTraegtaILLISHDL-PMVAryTSRIVVMEK 230
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDpityQVIRKTLKQAFADCT------VILSEHRIeAMLE--CQRFLVIEE 211
|
250
....*....|....*...
gi 1681691554 231 GAIVEKGRTEDLLKAPQH 248
Cdd:cd03289 212 NKVRQYDSIQKLLNEKSH 229
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
374-446 |
3.15e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTiealVEEAL---RPVPGLdgkakrKRTLETLEEVGLGvdyagrYPH------ELSGGQRQRVAIARAIARRPR---FL 441
Cdd:COG0178 788 MT----VEEALeffENIPKI------ARKLQTLQDVGLG------YIKlgqpatTLSGGEAQRVKLASELSKRSTgktLY 851
|
....*
gi 1681691554 442 IADEP 446
Cdd:COG0178 852 ILDEP 856
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-243 |
3.29e-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: 46.86 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQQVVKSVSFDLAPGEIFGIVGESGSGKTlatrALISLLPPTIKVADGSVSYKGrdvlkmkenelrh 86
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKS----SLLSALLAEMDKVEGHVHMKG------------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 87 lrgaEIGVVFQEPMT---SLNPSMTIGRQLEEglilHTKASAQERRSLI--LDMLkrvgirdPEGALSSYPHE---FSGG 158
Cdd:TIGR00957 700 ----SVAYVPQQAWIqndSLRENILFGKALNE----KYYQQVLEACALLpdLEIL-------PSGDRTEIGEKgvnLSGG 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 159 MRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMV-ELTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIVEKG 237
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMG 843
|
....*.
gi 1681691554 238 RTEDLL 243
Cdd:TIGR00957 844 SYQELL 849
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
294-500 |
4.27e-05 |
|
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: 45.28 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 294 NKPKRALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGRPRTE-NWTDYRLNCQMVFQDP--YS-- 368
Cdd:cd03288 31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQDPilFSgs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 369 ---SLDP-RMTIEALVEEALRpvpgldgKAKRKRTLETLEEvglGVDYAGRYPHE-LSGGQRQRVAIARAIARRPRFLIA 443
Cdd:cd03288 111 irfNLDPeCKCTDDRLWEALE-------IAQLKNMVKSLPG---GLDAVVTEGGEnFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681691554 444 DEPVSALDVT----VRAQVLDLFSDLqkrygfSCLFISHDLGVVEQvADRVVVMQDGRIIE 500
Cdd:cd03288 181 DEATASIDMAteniLQKVVMTAFADR------TVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-244 |
4.54e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 27 VSFDLAPGEIFGIVGESGSGKTLATRALISLLPPtikVADGSVSYKGRdvlkmkenelrhlrgaeigvVFQEPMTSLNPS 106
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP---RSDASVVIRGT--------------------VAYVPQVSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 107 MTIgrqleEGLILHTKASAQER--RSLILDMLKRVGIRDPEGALSSYPHE---FSGGMRQRIMLASVMLLKPALLIADEP 181
Cdd:PLN03130 693 ATV-----RDNILFGSPFDPERyeRAIDVTALQHDLDLLPGGDLTEIGERgvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681691554 182 TTALDAVIQRDVMELMVELTRAEGTAILLIS--HDLPMVarytSRIVVMEKGAIVEKGRTEDLLK 244
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEEGTYEELSN 828
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-230 |
5.31e-05 |
|
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: 43.52 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 33 PGEIFGIVGESGSGKTLATRALISLLPPTikvadgsvsykgrdvlkmkenelrhlrgaEIGVVFqepmtsLNPSMTIGRQ 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-----------------------------GGGVIY------IDGEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 113 LEEGLILHTKasaqerrslildmlkrvgirdpegalsSYPHEFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRD 192
Cdd:smart00382 46 LDQLLLIIVG---------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1681691554 193 VMELMV-----ELTRAEGTAILLISHD----LPMVARYTSRIVVMEK 230
Cdd:smart00382 99 LLLLEElrlllLLKSEKNLTVILTTNDekdlGPALLRRRFDRRIVLL 145
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
497-524 |
8.27e-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: 41.19 E-value: 8.27e-05
10 20
....*....|....*....|....*...
gi 1681691554 497 RIIEEGDRDTIFDSPKEAYTRRLLSAIP 524
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIP 28
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
156-232 |
8.35e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.47 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVML--LKPALLIADEPTTALDaviQRDVMELMVELTR--AEGTAILLISHDLPMVaRYTSRIVVMEKG 231
Cdd:cd03238 89 SGGELQRVKLASELFsePPGTLFILDEPSTGLH---QQDINQLLEVIKGliDLGNTVILIEHNLDVL-SSADWIIDFGPG 164
|
.
gi 1681691554 232 A 232
Cdd:cd03238 165 S 165
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
374-502 |
1.23e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 374 MTiealVEEAL---RPVPgldgKAKRKrtLETLEEVGLGvdyagrYPH------ELSGGQRQRVAIARAIARRP--RFL- 441
Cdd:PRK00349 792 MT----VEEALeffEAIP----KIARK--LQTLVDVGLG------YIKlgqpatTLSGGEAQRVKLAKELSKRStgKTLy 855
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 442 IADEPVSAL---DVTVRAQVLDLFSDLqkryGFSCLFISHDLGVVEQvADRVVVM------QDGRIIEEG 502
Cdd:PRK00349 856 ILDEPTTGLhfeDIRKLLEVLHRLVDK----GNTVVVIEHNLDVIKT-ADWIIDLgpeggdGGGEIVATG 920
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
156-221 |
6.09e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALDAviqRDVMELMVELTRAEGTaILLISHDlpmvaRY 221
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPGT-VVAVTHD-----RY 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
154-244 |
6.86e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLASVMLLKPALLIADEPTTALDAVIQRDVMELMVELTRAEGTaILLISHDLPMVARYTSRIVVMEKGAI 233
Cdd:PRK13546 143 KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKT-IFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
90
....*....|.
gi 1681691554 234 VEKGRTEDLLK 244
Cdd:PRK13546 222 KDYGELDDVLP 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
298-502 |
7.61e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 298 RALHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQG------RPRtenwtdyRLNCQMVFQDP----- 366
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadaRHR-------RAVCPRIAYMPqglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 367 --YSSLDprmtiealVEEAL----RpVPGLDGKAKRKRTLETLEEVGLGvDYAGRYPHELSGGQRQRVAIARAIARRPRF 440
Cdd:NF033858 88 nlYPTLS--------VFENLdffgR-LFGQDAAERRRRIDELLRATGLA-PFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 441 LIADEPVSALDVTVRAQVLDLFSDL-QKRYGFSCLfishdlgvveqVA----------DRVVVMQDGRIIEEG 502
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVL-----------VAtaymeeaerfDWLVAMDAGRVLATG 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
154-229 |
8.95e-04 |
|
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: 42.08 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLAsVMLLKPA-LLIADEPTTALDA--------VIQRdvmelmveLTRAEGTAILLISHDLPMVARYTSR 224
Cdd:COG1245 455 DLSGGELQRVAIA-ACLSRDAdLYLLDEPSAHLDVeqrlavakAIRR--------FAENRGKTAMVVDHDIYLIDYISDR 525
|
....*
gi 1681691554 225 IVVME 229
Cdd:COG1245 526 LMVFE 530
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
301-326 |
1.22e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 1.22e-03
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
300-502 |
1.28e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLG----------RTIAGLVTESEGRIQFQGRPRTENWTDyrLNCQMVFQDPYSS 369
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAYARQFLGQMDKPDVDSIEG--LSPAIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 370 LDPRMTIEALVE--EALRPVPGLDGKAKRkrtLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFL--IADE 445
Cdd:cd03270 89 RNPRSTVGTVTEiyDYLRLLFARVGIRER---LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVlyVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 446 PVSALDVTVRAQVLDLFSDLQKRyGFSCLFISHDLGVVEQvADRVVVM------QDGRIIEEG 502
Cdd:cd03270 166 PSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-214 |
1.47e-03 |
|
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: 39.90 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 36 IFGIVGESGSGKT---LATR-ALISLLPPTIKVADGSvsykgRDVLKMKENelrhlrGAEIGVVFQEPMTSLnpsMTIGR 111
Cdd:cd03240 24 LTLIVGQNGAGKTtiiEALKyALTGELPPNSKGGAHD-----PKLIREGEV------RAQVKLAFENANGKK---YTITR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 112 ---QLEEGLILHtkasaQ-ERRSLILDMLKRVgirdpegalssyphefSGGMRQ------RIMLASVMLLKPALLIADEP 181
Cdd:cd03240 90 slaILENVIFCH-----QgESNWPLLDMRGRC----------------SGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190
....*....|....*....|....*....|....
gi 1681691554 182 TTALDAV-IQRDVMELMVELTRAEGTAILLISHD 214
Cdd:cd03240 149 TTNLDEEnIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-229 |
1.54e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 154 EFSGGMRQRIMLAsVMLLKPA-LLIADEPTTALDaVIQRdvmeLMV-----ELTRAEGTAILLISHDLPMVARYTSRIVV 227
Cdd:PRK13409 453 DLSGGELQRVAIA-ACLSRDAdLYLLDEPSAHLD-VEQR----LAVakairRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
..
gi 1681691554 228 ME 229
Cdd:PRK13409 527 FE 528
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
156-219 |
2.01e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASvMLLKPA----LLIADEPTTALDAviqRDVMELMVELTR--AEGTAILLISHDLPMVA 219
Cdd:cd03271 171 SGGEAQRIKLAK-ELSKRStgktLYILDEPTTGLHF---HDVKKLLEVLQRlvDKGNTVVVIEHNLDVIK 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
376-531 |
2.09e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 376 IEALVEEALRPVPGLDGKAKRKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRFLIADEPVSALDVTVr 455
Cdd:PLN03073 301 VSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA- 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681691554 456 aqVLDLFSDLQKrYGFSCLFISHDLGVVEQVADRVVVMQDGRIIE-EGDRDTiFDSPKEaytRRLLSAIPALDQNEK 531
Cdd:PLN03073 380 --VLWLETYLLK-WPKTFIVVSHAREFLNTVVTDILHLHGQKLVTyKGDYDT-FERTRE---EQLKNQQKAFESNER 449
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-209 |
2.09e-03 |
|
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: 39.53 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 7 LTVCGLSLEVARTGQ--QVVKSVSFDLAPGEIFGIVGESGSGKT-----LATRAlisllppTIKVADGSVSYKGRdvlKM 79
Cdd:cd03232 4 LTWKNLNYTVPVKGGkrQLLNNISGYVKPGTLTALMGESGAGKTtlldvLAGRK-------TAGVITGEILINGR---PL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 80 KENELRhlrgaEIGVVFQEPMtsLNPSMTIgrqlEEGLILHTKAsaqerRSLILDMLKRVGIrdpegalssyphefsggm 159
Cdd:cd03232 74 DKNFQR-----STGYVEQQDV--HSPNLTV----REALRFSALL-----RGLSVEQRKRLTI------------------ 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1681691554 160 rqRIMLASvmllKPALLIADEPTTALDAVIQRDVMELMVELTRAeGTAIL 209
Cdd:cd03232 120 --GVELAA----KPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAIL 162
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-232 |
4.13e-03 |
|
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: 38.85 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 19 TGQQVVKSVSFDLAPGEIFGIVGESGSGKTLATRALISllppTIKVADGSVSYKGRDVLKMKENELRHLRGAEIGVVFQE 98
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG----EMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 99 PMTsLNPSmtigrqLEEGLILHTKASAQERRSLI--------LDMLkrvgirdPEGALSSYPHE---FSGGMRQRIMLAS 167
Cdd:cd03290 88 PWL-LNAT------VEENITFGSPFNKQRYKAVTdacslqpdIDLL-------PFGDQTEIGERginLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681691554 168 VMLLKPALLIADEPTTALDAVIQRDVM-ELMVELTRAEGTAILLISHDLPMVArYTSRIVVMEKGA 232
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDGS 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
304-484 |
4.81e-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: 38.11 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 304 SIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTeseGRIQFQGRPRTENWTDYRlncqmvfqdPYSSLDPRMTIealveea 383
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIGLALG---GAQSATRRRSGVKAGCIV---------AAVSAELIFTR------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 384 lrpvpgldgkakrkrtletleevglgvdyagrypHELSGGQRQRVAIA-----RAIARRPrFLIADEPVSALDVTVRAQV 458
Cdd:cd03227 76 ----------------------------------LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|....*.
gi 1681691554 459 LDLFSDLQKRyGFSCLFISHDLGVVE 484
Cdd:cd03227 121 AEAILEHLVK-GAQVIVITHLPELAE 145
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
156-246 |
5.62e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 156 SGGMRQRIMLASVMLLKPALLIADEPTTALDA-VIQRDVMELMveLTRAEGTAILLISHDLPMVARyTSRIVVMEKGAIV 234
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVE 860
|
90
....*....|..
gi 1681691554 235 EKGRTEDLLKAP 246
Cdd:PTZ00243 861 FSGSSADFMRTS 872
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
300-500 |
8.45e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 300 LHGVSIDIHEGEVVALVGGSGSGKTTLGRTIAGLVTESEGRIQFQGrprteNWTDYRLNcQMVFQDPYSSLDPRM----- 374
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----NWQLAWVN-QETPALPQPALEYVIdgdre 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681691554 375 --TIEALVEEALRPVPG-----LDGKAK-------RKRTLETLEEVGLGVDYAGRYPHELSGGQRQRVAIARAIARRPRF 440
Cdd:PRK10636 91 yrQLEAQLHDANERNDGhaiatIHGKLDaidawtiRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681691554 441 LIADEPVSALDvtvraqvLDLFSDLQ---KRYGFSCLFISHDLGVVEQVADRVVVMQDGRIIE 500
Cdd:PRK10636 171 LLLDEPTNHLD-------LDAVIWLEkwlKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| |
