|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-532 |
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: 959.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlARHPSGTINYAGQDLL 80
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDP-AAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHELSG 160
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQA 240
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 241 DCETLFQSPQHPYTQELLAAEPSGGPA-TNVIGPPLLEVDDLKVWFPIKKGFLRTTVDYVKAVDGINFSLPQGQTLGIVG 319
Cdd:COG4172 240 PTAELFAAPQHPYTRKLLAAEPRGDPRpVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 320 ESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMG-TPA 398
Cdd:COG4172 320 ESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 399 EQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTY 478
Cdd:COG4172 400 ERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 479 LFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAAFLVP 532
Cdd:COG4172 480 LFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-528 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 710.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHELSGGQRQR 165
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 246 FQSPQHPYTQELLAAEPSGGP-ATNVIGPPLLEVDDLKVWFPIKKGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSG 324
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEPSGDPvPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 325 KSTLGLAILRLIGSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIH-KMGTPAEQEAA 403
Cdd:PRK15134 325 KSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 404 IIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISH 483
Cdd:PRK15134 405 VIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 799207702 484 DLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAA 528
Cdd:PRK15134 485 DLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-528 |
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: 630.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLarHPSGTINYAGQDLLTLK 83
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG--RISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EktirHIRGNRIAMIFQEPMTSLNPLhNIEKQINEVLGLHkGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQR 163
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENL-GLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCE 243
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 244 TLFQSPQHPYTQELLAAEPSGGPATNVIGPPLLEVDDLKVWFPIKKGflrttvDYVKAVDGINFSLPQGQTLGIVGESGS 323
Cdd:COG1123 229 EILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESGS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 324 GKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEA 402
Cdd:COG1123 303 GKSTLARLLLGLLRpTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 403 AIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFIS 482
Cdd:COG1123 383 RVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFIS 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 799207702 483 HDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAA 528
Cdd:COG1123 463 HDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-534 |
8.55e-160 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 468.95 E-value: 8.55e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTI-----NYA 75
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 76 GQDLLTLKEKTIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALP 155
Cdd:PRK10261 87 VIELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGC 235
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 236 IVEQADCETLFQSPQHPYTQELLAA---------------------------EPSGGPATNVIGPPLLEVDDLKVWFPIK 288
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAvpqlgamkgldyprrfplislehpakqEPPIEQDTVVDGEPILQVRNLVTRFPLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 289 KGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQVRPLRREMQVV 367
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGeIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 368 FQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:PRK10261 407 FQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEA 527
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
....*..
gi 799207702 528 aflVPAA 534
Cdd:PRK10261 567 ---VPVA 570
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-266 |
8.41e-134 |
|
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: 391.34 E-value: 8.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLarHPSGTINYAGQDLLTLKEK 85
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG--ITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHELSGGQRQR 165
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 799207702 246 FQSPQHPYTQELLAAEPSGGP 266
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
274-528 |
5.05e-131 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 384.47 E-value: 5.05e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRL 352
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEpTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 353 TQQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQR 432
Cdd:COG4608 86 SGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 433 IAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGI 512
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
250
....*....|....*.
gi 799207702 513 FAAPQHGYTRQLLEAA 528
Cdd:COG4608 246 YARPLHPYTQALLSAV 261
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-527 |
3.98e-117 |
|
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: 348.58 E-value: 3.98e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI----GSKGGIRFEGQQLD 350
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RLTQQQVRPLR-REMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGL-DPESR-HRYPHEFSG 427
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpDPERRlDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|
gi 799207702 508 DAAGIFAAPQHGYTRQLLEA 527
Cdd:COG0444 234 PVEELFENPRHPYTRALLSS 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-507 |
2.56e-104 |
|
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: 312.52 E-value: 2.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLT 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 354 QQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPA-EQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQR 432
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKeARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 433 IAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-240 |
1.69e-102 |
|
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: 307.51 E-value: 1.69e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplarHP-SGTINYAGQDLLTLKE 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL------KPtSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KtIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKvATQRTLELLELVGILEPHKRLKALPHELSGGQRQ 164
Cdd:cd03257 75 R-LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKK-EARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQA 240
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-529 |
5.43e-99 |
|
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: 299.41 E-value: 5.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQqldRLT 353
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGR---PVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 354 QQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGtpaEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRI 433
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 434 AIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIF 513
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 799207702 514 AAPQHGYTRQLLEAAF 529
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
272-528 |
6.02e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 281.85 E-value: 6.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 272 GPPLLEVDDLKVWFPIKKGFLRTTvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAiLRLIG--SKGGIRFEGQQL 349
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPE-RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARL-LTMIEtpTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DRLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQ 429
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 430 RQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDA 509
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250
....*....|....*....
gi 799207702 510 AGIFAAPQHGYTRQLLEAA 528
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSAT 258
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-267 |
1.59e-88 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 275.46 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEF-VTGDHHQRV------VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTI 72
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpVRGGLFGRTvgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE------PtSGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 73 NYAGQDLLTLKEKTIRHIRgNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRlk 152
Cdd:COG4608 76 LFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHAD-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 153 ALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQ 232
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260 270
....*....|....*....|....*....|....*
gi 799207702 233 KGCIVEQADCETLFQSPQHPYTQELLAAEPSGGPA 267
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSAVPVPDPE 267
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
274-532 |
9.52e-88 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 273.51 E-value: 9.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIK--KGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLD 350
Cdd:PRK15079 7 VLLEVADLKVHFDIKdgKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGLRIH--KMGTPAEQEAAIIAALKeVGLDPESRHRYPHEFSGG 428
Cdd:PRK15079 87 GMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLK-VGLLPNLINRYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 429 QRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGD 508
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 245
|
250 260
....*....|....*....|....
gi 799207702 509 AAGIFAAPQHGYTRQLLEAaflVP 532
Cdd:PRK15079 246 YDEVYHNPLHPYTKALMSA---VP 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-262 |
1.19e-84 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 265.43 E-value: 1.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplAR--HPSGTINYAGQDL 79
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL----AAngRIGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 LTLKEKTIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHELS 159
Cdd:PRK09473 84 LNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260
....*....|....*....|...
gi 799207702 240 ADCETLFQSPQHPYTQELLAAEP 262
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGLLNAVP 266
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-262 |
4.29e-83 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 261.60 E-value: 4.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlARHPSGTINYAGQDLLTLKEK 85
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHELSGGQRQR 165
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*..
gi 799207702 246 FQSPQHPYTQELLAAEP 262
Cdd:PRK11022 242 FRAPRHPYTQALLRALP 258
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-260 |
4.21e-81 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 253.57 E-value: 4.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLltlKEK 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKS----TLLRALA-GLERPWSGEVTFDGRPV---TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGnRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTgkvATQRTLELLELVGiLEPHKRLKaLPHELSGGQRQR 165
Cdd:COG1124 73 RRKAFRR-RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPD---REERIAELLEQVG-LPPSFLDR-YPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*
gi 799207702 246 FQSPQHPYTQELLAA 260
Cdd:COG1124 227 LAGPKHPYTRELLAA 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
274-529 |
8.57e-72 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 230.11 E-value: 8.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKGFLRTTvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLD-R 351
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQ--QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGeILINGHKLEyG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 352 LTQQQVRPLRreMqvVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQ 431
Cdd:COG4167 81 DYKYRCKHIR--M--IFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 432 RIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAG 511
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*...
gi 799207702 512 IFAAPQHGYTRQLLEAAF 529
Cdd:COG4167 237 VFANPQHEVTKRLIESHF 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
266-537 |
1.33e-69 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 226.53 E-value: 1.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 266 PATNVIGPPLLEVDDLKVWFPIKKGFlrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI--- 342
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 343 -RFEGQQLDRLTQQQVRPLRRE-MQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLdPESRHR 420
Cdd:PRK09473 76 aTFNGREILNLPEKELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 421 ---YPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMV 497
Cdd:PRK09473 155 mkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 799207702 498 VKHGQVVEQGDAAGIFAAPQHGYTRQLLEAaflVPaaRVD 537
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQPSHPYSIGLLNA---VP--RLD 269
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-263 |
7.14e-68 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 222.09 E-value: 7.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhPSGTIN-----YAGQDL 79
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK------DNWHVTadrfrWNGIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 LTLKEKTIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLgLHKGLTGKV------ATQRTLELLELVGILEPHKRLKA 153
Cdd:COG4170 76 LKLSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAI-PSWTFKGKWwqrfkwRKKRAIELLHRVGIKDHKDIMNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellkeLQ-----ARL----GMALLLISHDLNLVRRI 224
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQ---------AQifrllARLnqlqGTSILLISHDLESISQW 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 799207702 225 AHRVCVMQKGCIVEQADCETLFQSPQHPYTQELLAAEPS 263
Cdd:COG4170 226 ADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-267 |
3.20e-62 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 207.12 E-value: 3.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTAhsilRLLPypLARHP-SGTINYAGQDLLTlKEKTIRHIRGNRIAMIFQEP 102
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLA----RLLT--MIETPtGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 MTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPH-KRLkalPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:PRK11308 102 YGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHyDRY---PHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQELLAAE 261
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSAT 258
|
....*.
gi 799207702 262 PSGGPA 267
Cdd:PRK11308 259 PRLNPD 264
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-527 |
5.46e-62 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 206.52 E-value: 5.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKGFLRttvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI-----RFEGQQL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DRLTQQQVRPL-RREMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGL-DPESR-HRYPHEFS 426
Cdd:PRK11022 76 QRISEKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASRlDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 427 GGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQ 506
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260
....*....|....*....|.
gi 799207702 507 GDAAGIFAAPQHGYTRQLLEA 527
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRA 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
302-527 |
5.40e-60 |
|
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: 199.26 E-value: 5.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMC 380
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 461 RQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAApQHGYTRQLLEA 527
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSA 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-262 |
8.36e-60 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 200.70 E-value: 8.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDN--LIEIRDLSVEFVTGDHHQ---------RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPS 69
Cdd:PRK15079 1 VTEGKkvLLEVADLKVHFDIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 70 GTINYAGQDLLTLKEKTIRHIRgNRIAMIFQEPMTSLNPLHNIEKQINEVL-GLHKGLTGKVATQRTLELLELVGILEph 148
Cdd:PRK15079 76 GEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLP-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 149 KRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRV 228
Cdd:PRK15079 153 NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 232
|
250 260 270
....*....|....*....|....*....|....
gi 799207702 229 CVMQKGCIVEQADCETLFQSPQHPYTQELLAAEP 262
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
272-525 |
9.19e-57 |
|
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: 189.81 E-value: 9.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 272 GPPLLEVDDLKvwfpikKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEG 346
Cdd:COG1127 2 SEPMIEVRNLT------KSFGDRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVL----LKLIIgllrpDSGEILVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 347 QQLDRLTQQQVRPLRREMQVVFQDP--FGSLSprmcVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLdPESRHRYPHE 424
Cdd:COG1127 67 QDITGLSEKELYELRRRIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 425 FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250 260
....*....|....*....|.
gi 799207702 505 EQGDAAGIFAAPqHGYTRQLL 525
Cdd:COG1127 222 AEGTPEELLASD-DPWVRQFL 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-267 |
1.59e-56 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 199.70 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEF---------VTGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAG 76
Cdd:PRK10261 313 ILQVRNLVTRFplrsgllnrVTREVH--AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV-----ESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 77 QDLLTLKEKTIRHIRGNrIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRlkALPH 156
Cdd:PRK10261 386 QRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAW--RYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
250 260 270
....*....|....*....|....*....|.
gi 799207702 237 VEQADCETLFQSPQHPYTQELLAAEPSGGPA 267
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYTRKLMAAVPVADPS 573
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
274-527 |
1.28e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 195.31 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPiKKGFLRTTvdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS------KGGIRFEGQ 347
Cdd:PRK15134 4 PLLAIENLSVAFR-QQQTVRTV------VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QLDRLTQQQVRPLR-REMQVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESR--HRYPHE 424
Cdd:PRK15134 77 SLLHASEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKrlTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 425 FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260
....*....|....*....|...
gi 799207702 505 EQGDAAGIFAAPQHGYTRQLLEA 527
Cdd:PRK15134 237 EQNRAATLFSAPTHPYTQKLLNS 259
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-259 |
2.15e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 189.52 E-value: 2.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLLTLKEKT 86
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCINL-LERPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGnRIAMIFQEP--MTSLNPLHNIEkqinevLGL-HKGLTGKVATQRTLELLELVGiLEPHKrlKALPHELSGGQR 163
Cdd:COG1135 77 LRAARR-KIGMIFQHFnlLSSRTVAENVA------LPLeIAGVPKAEIRKRVAELLELVG-LSDKA--DAYPSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALD-------------VtvqlkilellkelQARLGMALLLISHDLNLVRRIAHRVCV 230
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDpettrsildllkdI-------------NRELGLTIVLITHEMDVVRRICDRVAV 213
|
250 260
....*....|....*....|....*....
gi 799207702 231 MQKGCIVEQADCETLFQSPQHPYTQELLA 259
Cdd:COG1135 214 LENGRIVEQGPVLDVFANPQSELTRRFLP 242
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-260 |
2.63e-55 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 186.44 E-value: 2.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEfvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhpSGTINYAGQDLLTLKEKT 86
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-------AGVRQTAGRVLLDGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLgLHKGLTGKVATqrTLELLELVGILEPHKRLKALPHELSGGQRQRV 166
Cdd:PRK10418 73 PCALRGRKIATIMQNPRSAFNPLHTMHTHARETC-LALGKPADDAT--LTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLF 246
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....
gi 799207702 247 QSPQHPYTQELLAA 260
Cdd:PRK10418 230 NAPKHAVTRSLVSA 243
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-259 |
3.55e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 185.58 E-value: 3.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLlTLKEK 85
Cdd:COG1126 1 MIEIENLHKSF--GDLE--VLKGISLDVEKGEVVVIIGPSGSGKS----TLLRCINL-LEEPDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGnRIAMIFQE----P-MTSLnplHNIekqineVLGL--HKGLTGKVATQRTLELLELVGILEphkRLKALPHEL 158
Cdd:COG1126 71 DINKLRR-KVGMVFQQfnlfPhLTVL---ENV------TLAPikVKKMSKAEAEERAMELLERVGLAD---KADAYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALD---------VTVQLkilellkelqARLGMALLLISHDLNLVRRIAHRVC 229
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevldVMRDL----------AKEGMTMVVVTHEMGFAREVADRVV 207
|
250 260 270
....*....|....*....|....*....|
gi 799207702 230 VMQKGCIVEQADCETLFQSPQHPYTQELLA 259
Cdd:COG1126 208 FMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-250 |
1.34e-54 |
|
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: 183.94 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLLTLKEK 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS----TLIRCING-LERPTSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQE--PMTSLNPLHNIEKQInEVLGLHKgltgKVATQRTLELLELVGiLEpHKRlKALPHELSGGQR 163
Cdd:cd03258 76 ELRKAR-RRIGMIFQHfnLLSSRTVFENVALPL-EIAGVPK----AEIEERVLELLELVG-LE-DKA-DAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCE 243
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 799207702 244 TLFQSPQ 250
Cdd:cd03258 227 EVFANPQ 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-267 |
1.70e-54 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 186.93 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLaRHPSGTINYAGQDLLTLKEK 85
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNW-RVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLglhKGLTGK--------VATQRTLELLELVGILEPHKRLKALPHE 157
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNI---PGWTYKgrwwqrfgWRKRRAIELLHRVGIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250 260 270
....*....|....*....|....*....|
gi 799207702 238 EQADCETLFQSPQHPYTQELLAAEPSGGPA 267
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQALIRAIPDFGSA 268
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-260 |
2.22e-54 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 184.27 E-value: 2.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFVTGD---HHQRV--VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQD 78
Cdd:COG4167 3 ALLEVRNLSKTFKYRTglfRRQQFeaVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIE------PtSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 79 LLTLKEKTirhiRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKalPHEL 158
Cdd:COG4167 77 LEYGDYKY----RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFY--PHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVE 238
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 799207702 239 QADCETLFQSPQHPYTQELLAA 260
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIES 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-514 |
2.75e-54 |
|
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: 191.55 E-value: 2.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHsILRLLP----------YPLARHPS----GTI 72
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMDqyeptsgriiYHVALCEKcgyvERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 73 NYAGQ--------------DLLTLKEKTIRHIRgNRIAMIFQEPMTslnpLHNIEKQINEVL-GLHK-GLTGKVATQRTL 136
Cdd:TIGR03269 76 SKVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTFA----LYGDDTVLDNVLeALEEiGYEGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 137 ELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISH 216
Cdd:TIGR03269 151 DLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 217 DLNLVRRIAHRVCVMQKGCIVEQADCETLFQSpqhpYTQELLAAEpsggPATNV-IGPPLLEVDDL-KVWFPIKKGFlrt 294
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV----FMEGVSEVE----KECEVeVGEPIIKVRNVsKRYISVDRGV--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 295 tvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFE-GQQLDRLTQQqvRPL-----RREMQVV 367
Cdd:TIGR03269 297 ----VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVRvGDEWVDMTKP--GPDgrgraKRYIGIL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 368 FQDPfgSLSPRMCVSEIVGE--GLRIHKmgtpAEQEAAIIAALKEVGLDPESR----HRYPHEFSGGQRQRIAIARALVL 441
Cdd:TIGR03269 371 HQEY--DLYPHRTVLDNLTEaiGLELPD----ELARMKAVITLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIK 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
287-517 |
7.28e-54 |
|
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: 182.01 E-value: 7.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFlRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLR 361
Cdd:cd03258 7 VSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINglerpTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDpFGSLSPRMcVSEIVGEGLRIHkmGTPAEQEAAIIAALKE-VGLDpESRHRYPHEFSGGQRQRIAIARALV 440
Cdd:cd03258 82 RRIGMIFQH-FNLLSSRT-VFENVALPLEIA--GVPKAEIEERVLELLElVGLE-DKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 441 LKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
303-523 |
7.59e-54 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 181.93 E-value: 7.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDP--FGSL 375
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTL----LRLIVgllrpDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGalFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SprmcVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:cd03261 93 T----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 456 DRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAApQHGYTRQ 523
Cdd:cd03261 168 DPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQ 234
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
6-260 |
9.78e-54 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 182.71 E-value: 9.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHpSGTINYAG-----QDLL 80
Cdd:COG4107 8 LLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPT-SGSVYYRDrdggpRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRGNRIAMIFQEPMTSLNPLH----NI-EKQIneVLGL-HKGltgkVATQRTLELLELVGIlePHKRLKAL 154
Cdd:COG4107 83 ALSEAERRRLRRTDWGMVYQNPRDGLRMDVsaggNIaERLM--AAGErHYG----DIRARALEWLERVEI--PLERIDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:COG4107 155 PRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNG 234
|
250 260
....*....|....*....|....*.
gi 799207702 235 CIVEQADCETLFQSPQHPYTQELLAA 260
Cdd:COG4107 235 RVVESGLTDQVLEDPQHPYTQLLVSS 260
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
276-525 |
1.15e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.90 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPIKKGFlrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLD 350
Cdd:COG1135 2 IELENLSKTFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINllerpTSGSVLVDGVDLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RLTQQQVRPLRREMQVVFQDpFGSLSPRMcVSEIVGEGLRIhkMGTPAEQEAAIIAALKE-VGLDpESRHRYPHEFSGGQ 429
Cdd:COG1135 71 ALSERELRAARRKIGMIFQH-FNLLSSRT-VAENVALPLEI--AGVPKAEIRKRVAELLElVGLS-DKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 430 RQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDA 509
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250
....*....|....*.
gi 799207702 510 AGIFAAPQHGYTRQLL 525
Cdd:COG1135 226 LDVFANPQSELTRRFL 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-239 |
1.38e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 181.01 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLpyplaRHP-SGTINYAGQDLLTL 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGL-----DRPtSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 KEKTIRHIRGNRIAMIFQEP--MTSLNPLHNIEkqinevLGLH-KGLTGKVATQRTLELLELVGIlepHKRLKALPHELS 159
Cdd:COG1136 76 SERELARLRRRHIGFVFQFFnlLPELTALENVA------LPLLlAGVSRKERRERARELLERVGL---GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQ 239
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-258 |
8.07e-53 |
|
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: 179.40 E-value: 8.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 3 QDNLIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLT 81
Cdd:COG1127 2 SEPMIEVRNLTKSF--GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR------PdSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHIRgNRIAMIFQEP--MTSLNPLHNIEkqinevLGL--HKGLTGKVATQRTLELLELVGiLEPHKRLkaLPHE 157
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGalFDSLTVFENVA------FPLreHTDLSEAEIRELVLEKLELVG-LPGAADK--MPSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALD-----VTVQlkileLLKELQARLGMALLLISHDLNLVRRIAHRVCVMQ 232
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsaVIDE-----LIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250 260
....*....|....*....|....*.
gi 799207702 233 KGCIVEQADCETLFQSPqHPYTQELL 258
Cdd:COG1127 217 DGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
275-529 |
1.39e-51 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 176.90 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKGFLRTtvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLD--- 350
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 -RLTQQQVRplrremqVVFQDPFGSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQ 429
Cdd:PRK15112 82 ySYRSQRIR-------MIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 430 RQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDA 509
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250 260
....*....|....*....|
gi 799207702 510 AGIFAAPQHGYTRQLLEAAF 529
Cdd:PRK15112 235 ADVLASPLHELTKRLIAGHF 254
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-234 |
2.66e-51 |
|
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: 174.60 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLNIL-GGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQEP--MTSLNPLHNIEkqinevLGLH-KGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQR 163
Cdd:cd03255 76 LAAFRRRHIGFVFQSFnlLPDLTALENVE------LPLLlAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKG 234
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
302-505 |
5.58e-50 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 172.95 E-value: 5.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMC 380
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRiHKMG-TPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTV 459
Cdd:PRK10419 108 VREIIREPLR-HLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 799207702 460 QRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVE 505
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
273-517 |
8.76e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 174.90 E-value: 8.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFpikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQ 347
Cdd:COG3842 3 MPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMIAgfetpDSGRILLDGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QLDRltqqqVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFSG 427
Cdd:COG3842 68 DVTG-----LPPEKRNVGMVFQDY--ALFPHLTVAENVAFGLRMRGVP-KAEIRARVAELLELVGLE-GLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
|
250
....*....|
gi 799207702 508 DAAGIFAAPQ 517
Cdd:COG3842 219 TPEEIYERPA 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
299-529 |
1.76e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.14 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDpFG 373
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINllerpTSGRVLVDGQDLTALSEKELRKARRQIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMcVSEIVGEGLRIhkMGTPAEQEAAIIAALKE-VGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:PRK11153 93 LLSSRT-VFDNVALPLEL--AGTPKAEIKARVTELLElVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 453 SALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAAF 529
Cdd:PRK11153 169 SALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTL 245
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-506 |
2.79e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.76 E-value: 2.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQ 347
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTL----LNILGgldrpTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QLDRLTQQQVRPLRRE-MQVVFQDPFgsLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFS 426
Cdd:COG1136 71 DISSLSERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVS-RKERRERARELLERVGLG-DRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 427 GGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLmVVKHGQVVEQ 506
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVI-RLRDGRIVSD 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-526 |
1.86e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 165.17 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFpikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQL 349
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTL----LRCINlleepDSGTITVDGEDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DrLTQQQVRPLRREMQVVFQDpFgSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLdPESRHRYPHEFSGGQ 429
Cdd:COG1126 66 T-DSKKDINKLRRKVGMVFQQ-F-NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 430 RQRIAIARALVLKPRLILLDEPTSALD-RTVQrQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGD 508
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDpELVG-EVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250
....*....|....*...
gi 799207702 509 AAGIFAAPQHGYTRQLLE 526
Cdd:COG1126 220 PEEFFENPQHERTRAFLS 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-256 |
8.08e-47 |
|
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: 163.44 E-value: 8.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLLTLKEKT 86
Cdd:cd03261 1 IELRGLTKSF--GGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PD----SGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQEP--MTSLNPLHNIEKQINEvlglHKGLTGKVATQRTLELLELVGiLEPHKRLkaLPHELSGGQRQ 164
Cdd:cd03261 72 LYRLR-RRMGMLFQSGalFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVG-LRGAEDL--YPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCET 244
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
250
....*....|..
gi 799207702 245 LFQSpQHPYTQE 256
Cdd:cd03261 224 LRAS-DDPLVRQ 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-260 |
1.79e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 163.32 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 22 HQRVVNNVSFDIKRGETIALVGESGSGKSVTAhsilRLLpYPLARHPSGTINYAGQDLLTLKEKTIRHIRGNrIAMIFQE 101
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLA----RLL-VGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHkrLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:PRK10419 98 SISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSV--LDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCeTLFQSPQHPYTQELLAA 260
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV-GDKLTFSSPAGRVLQNA 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
274-532 |
2.31e-46 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 162.79 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKGFlrttvdyvkavDGINFSLPQGQTLGIVGESGSGKSTLGLAI-LRLIGSKGGIRF---EGQQL 349
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGC-----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYrmrDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 D--RLTQQQVRPL-RREMQVVFQDPFGSLspRMCVSE--IVGEGLrihkMGTPA----EQEAAIIAALKEVGLDPESRHR 420
Cdd:PRK11701 74 DlyALSEAERRRLlRTEWGFVHQHPRDGL--RMQVSAggNIGERL----MAVGArhygDIRATAGDWLERVEIDAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 421 YPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKH 500
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260 270
....*....|....*....|....*....|..
gi 799207702 501 GQVVEQGDAAGIFAAPQHGYTrQLLEAAFLVP 532
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYT-QLLVSSVLQV 258
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
299-517 |
3.16e-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: 161.35 E-value: 3.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTqqqVRPLRREMQVVFQDPFGSLsp 377
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDGKDITKKN---LRELRRKVGLVFQNPDDQL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 rmcVSEIVGE----GLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:COG1122 89 ---FAPTVEEdvafGPENLGL-PREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 454 ALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
299-507 |
4.96e-46 |
|
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: 160.38 E-value: 4.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTqqqvrPLRREMQVVFQDPfg 373
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVP-----PERRNIGMVFQDY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGLDPEsRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:cd03259 82 ALFPHLTVAENIAFGLKLRGVPKAEIRARVREL-LELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
299-489 |
1.36e-45 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 159.58 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLRRE-MQVVFQDPf 372
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGgldrpTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 gSLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:cd03255 92 -NLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 799207702 453 SALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVK 489
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-246 |
1.61e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.42 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLltlKEKT 86
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL-----KPTSGEVLVDGKDI---TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQEPmtslnplhniEKQI------NEV-LGL-HKGLTGKVATQRTLELLELVGILEphkRLKALPHEL 158
Cdd:COG1122 70 LRELR-RKVGLVFQNP----------DDQLfaptveEDVaFGPeNLGLPREEIRERVEEALELVGLEH---LADRPPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDvtvqlkilellKELQARL----------GMALLLISHDLNLVRRIAHRV 228
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD-----------PRGRRELlellkrlnkeGKTVIIVTHDLDLVAELADRV 204
|
250
....*....|....*...
gi 799207702 229 CVMQKGCIVEQADCETLF 246
Cdd:COG1122 205 IVLDDGRIVADGTPREVF 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
287-537 |
2.63e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.93 E-value: 2.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRltqqQVRPLR 361
Cdd:COG1118 8 ISKRFGSFT-----LLDDVSLEIASGELVALLGPSGSGKTTL----LRIIAgletpDSGRIVLNGRDLFT----NLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDPESrHRYPHEFSGGQRQRIAIARALVL 441
Cdd:COG1118 75 RRVGFVFQHY--ALFPHMTVAENIAFGLRVRPPS-KAEIRARVEELLELVQLEGLA-DRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYT 521
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
250
....*....|....*.
gi 799207702 522 RQLLEAAFLVPAARVD 537
Cdd:COG1118 231 ARFLGCVNVLRGRVIG 246
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
273-505 |
3.02e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.17 E-value: 3.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQ 347
Cdd:COG1116 5 APALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIAglekpTSGEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QldrltqqqVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFSG 427
Cdd:COG1116 74 P--------VTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVP-KAERRERARELLELVGLA-GFEDAYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSALD----RTVQrqvvELLRSLQAKYNLTYLFISHDL--AVvkALSHQLMVVKH- 500
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQ----DELLRLWQETGKTVLFVTHDVdeAV--FLADRVVVLSAr 215
|
....*.
gi 799207702 501 -GQVVE 505
Cdd:COG1116 216 pGRIVE 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
273-530 |
1.25e-43 |
|
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: 155.37 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFPIKKGFlrttvdyvkavDGINFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFE---GQQ 348
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGC-----------RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYImrsGAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LD--RLTQQQVRPL-RREMQVVFQDPFGSLspRMCVSEIVGEGLRIHKMGTPAEQEAAIIAA--LKEVGLDPESRHRYPH 423
Cdd:TIGR02323 70 LElyQLSEAERRRLmRTEWGFVHQNPRDGL--RMRVSAGANIGERLMAIGARHYGNIRATAQdwLEEVEIDPTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 424 EFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*..
gi 799207702 504 VEQGDAAGIFAAPQHGYTrQLLEAAFL 530
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYT-QLLVSSIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-504 |
2.67e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 160.95 E-value: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEF--VtgdhhqRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILrllpyplA---RHPSGTINYAGQD 78
Cdd:COG1129 2 EPLLEMRGISKSFggV------KALDGVSLELRPGEVHALLGENGAGKS-TLMKIL-------SgvyQPDSGEILLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 79 LltlKEKTIRHIRGNRIAMIFQEPM--TSLNPLHNIekqineVLGLHKGLTGKV----ATQRTLELLELVGI-LEPHKRL 151
Cdd:COG1129 68 V---RFRSPRDAQAAGIAIIHQELNlvPNLSVAENI------FLGREPRRGGLIdwraMRRRARELLARLGLdIDPDTPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 152 KalphELSGGQRQRVMIAMALANEPELLIADEPTTALDVT-VQlkilellkelqaRL----------GMALLLISHDLNL 220
Cdd:COG1129 139 G----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVE------------RLfriirrlkaqGVAIIYISHRLDE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 221 VRRIAHRVCVMQKGCIVEQADCETLfqspqhpyTQELLAAEPSG-------GPATNVIGPPLLEVDDLKVWfpikkgflr 293
Cdd:COG1129 203 VFEIADRVTVLRDGRLVGTGPVAEL--------TEDELVRLMVGreledlfPKRAAAPGEVVLEVEGLSVG--------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 294 ttvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQL------------------DRLTQ 354
Cdd:COG1129 266 ------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGeIRLDGKPVrirsprdairagiayvpeDRKGE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 355 Q--QVRPLRREMQVVFQD---PFGSLSPRM---CVSEIVGEgLRIhKMGTPAeqeaaiiaalKEVGldpesrhryphEFS 426
Cdd:COG1129 340 GlvLDLSIRENITLASLDrlsRGGLLDRRReraLAEEYIKR-LRI-KTPSPE----------QPVG-----------NLS 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 427 GGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
287-506 |
4.75e-43 |
|
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: 152.63 E-value: 4.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFlRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQldrltqqqVRPLR 361
Cdd:cd03293 6 VSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAglerpTSGEVLVDGEP--------VTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALVL 441
Cdd:cd03293 73 PDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEEL-LELVGLS-GFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDL--AVvkALSHQLMVV--KHGQVVEQ 506
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVLsaRPGRIVAE 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-253 |
7.22e-43 |
|
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: 153.95 E-value: 7.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLKEKTIRHIRGNRIAMIFQE--P 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE------PtSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSfaL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 MTSLNPLHNIEkqinevLGLH-KGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:cd03294 114 LPHRTVLENVA------FGLEvQGVPRAEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPY 253
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-512 |
7.25e-43 |
|
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: 152.33 E-value: 7.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFpikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQ-----QLD 350
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEvlldgKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RLTQQQVRPLRREMQVVFQ--DPFgslspRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPE-SRHRYPHEFSG 427
Cdd:cd03260 70 YDLDVDVLELRRRVGMVFQkpNPF-----PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEvKDRLHALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYnlTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
....*
gi 799207702 508 DAAGI 512
Cdd:cd03260 223 PTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
299-511 |
9.76e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 151.74 E-value: 9.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDpFG 373
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTL----LKLLYgeerpTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 sLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:COG2884 90 -LLPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 454 ALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAG 511
Cdd:COG2884 167 NLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
299-502 |
1.10e-42 |
|
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: 150.42 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQqVRPLRREMQVVFQDPfg 373
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAgleepDSGSILIDGEDLTDLEDE-LPPLRRRIGMVFQDF-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLrihkmgtpaeqeaaiiaalkevgldpesrhryphefSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:cd03229 86 ALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
300-502 |
1.42e-42 |
|
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: 151.08 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQqldRLTQQQVRPLRREMQVVFQDPFGSLspr 378
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGK---DLTKLSLKELRRKVGLVFQNPDDQF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 mcVSEIVGE----GLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:cd03225 89 --FGPTVEEevafGLENLGL-PEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 455 LDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:cd03225 165 LDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-238 |
1.62e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 151.36 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYpLARHP-SGTINYAGQDLLTLKEK 85
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLL-Y-GEERPtSGQVLVNGQDLSRLKRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQEP--MTSLNPLHNIEkqinevLGLH-KGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQ 162
Cdd:COG2884 73 EIPYLR-RRIGVVFQDFrlLPDRTVYENVA------LPLRvTGKSRKEIRRRVREVLDLVGLSD---KAKALPHELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDvtvqlkilellkELQA-----------RLGMALLLISHDLNLVRRIAHRVCVM 231
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLD------------PETSweimelleeinRRGTTVLIATHDLELVDRMPKRVLEL 210
|
....*..
gi 799207702 232 QKGCIVE 238
Cdd:COG2884 211 EDGRLVR 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-512 |
2.61e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.75 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQ 348
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTL----LRCLNglvepTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQQVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGlRIHKMGT--------PAEQEAAIIAALKEVGLDPESRHR 420
Cdd:COG3638 67 VTALRGRALRRLRRRIGMIFQQF--NLVPRLSVLTNVLAG-RLGRTSTwrsllglfPPEDRERALEALERVGLADKAYQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 421 yPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKH 500
Cdd:COG3638 144 -ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 799207702 501 GQVVEQGDAAGI 512
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-237 |
3.11e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.36 E-value: 3.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLKE 84
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE------PtSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KTIRHIRGnRIAMIFQEPmtSLNP----LHNiekqineVL-------GLHKGLTGKVAT---QRTLELLELVGILE-PHK 149
Cdd:COG3638 73 RALRRLRR-RIGMIFQQF--NLVPrlsvLTN-------VLagrlgrtSTWRSLLGLFPPedrERALEALERVGLADkAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 150 RlkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVC 229
Cdd:COG3638 143 R----ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
....*...
gi 799207702 230 VMQKGCIV 237
Cdd:COG3638 219 GLRDGRVV 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
292-528 |
3.47e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 153.91 E-value: 3.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 292 LRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI-----RFEGQQLDRLTQQQVRPL-RREMQ 365
Cdd:COG4170 13 IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrfRWNGIDLLKLSPRERRKIiGREIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 366 VVFQDPFGSLSPrmcvSEIVGEGL---------RIHKMGTPAEQEAAIIAALKEVGL-DPESRHR-YPHEFSGGQRQRIA 434
Cdd:COG4170 93 MIFQEPSSCLDP----SAKIGDQLieaipswtfKGKWWQRFKWRKKRAIELLHRVGIkDHKDIMNsYPHELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 435 IARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
250
....*....|....
gi 799207702 515 APQHGYTRQLLEAA 528
Cdd:COG4170 249 SPHHPYTKALLRSM 262
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-236 |
1.20e-41 |
|
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: 148.83 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLlTLKEKT 86
Cdd:cd03262 1 IEIKNLHKSF--GDFH--VLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRCINL-LEEPDSGTIIIDGLKL-TDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQ-----EPMTSLNplhNIEKQINEVLGLHKgltgKVATQRTLELLELVGILEphkRLKALPHELSGG 161
Cdd:cd03262 71 INELR-QKVGMVFQqfnlfPHLTVLE---NITLAPIKVKGMSK----AEAEERALELLEKVGLAD---KADAYPAQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALD---------VTVQLkilellkelqARLGMALLLISHDLNLVRRIAHRVCVMQ 232
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDpelvgevldVMKDL----------AEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
....
gi 799207702 233 KGCI 236
Cdd:cd03262 210 DGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-261 |
1.29e-41 |
|
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: 149.76 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-----EPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHirgnRIAMIFQEpmTSLNPLHNIEKQINEVLGLHKGLTGKVAtQRTLELLELVGiLEPHKRLKALPHELSGGQRQRV 166
Cdd:cd03295 73 LRR----KIGYVIQQ--IGLFPHMTVEENIALVPKLLKWPKEKIR-ERADELLALVG-LDPAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLF 246
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|....*
gi 799207702 247 QSPQHPYTQELLAAE 261
Cdd:cd03295 225 RSPANDFVAEFVGAD 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
1.39e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.85 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQ-DNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDL 79
Cdd:COG1116 1 MSAaAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLI-AGLEKPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 ltlkektirHIRGNRIAMIFQEPmtSLNP----LHNIEkqinevLGL-HKGLTGKVATQRTLELLELVGiLEPHkrLKAL 154
Cdd:COG1116 76 ---------TGPGPDRGVVFQEP--ALLPwltvLDNVA------LGLeLRGVPKAERRERARELLELVG-LAGF--EDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDV----TVQlkilELLKELQARLGMALLLISHDlnlVR---RIAHR 227
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHD---VDeavFLADR 208
|
....*..
gi 799207702 228 VCVMQKG 234
Cdd:COG1116 209 VVVLSAR 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-245 |
5.44e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.52 E-value: 5.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLKEK 85
Cdd:COG1131 1 IEVRGLTKRY--GDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR------PtSGEVRVLGEDVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgnRIAMIFQEP--MTSLNPLHNIEkqineVLGLHKGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQR 163
Cdd:COG1131 71 VRR-----RIGYVPQEPalYPDLTVRENLR-----FFARLYGLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVtVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCE 243
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDP-EARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
..
gi 799207702 244 TL 245
Cdd:COG1131 217 EL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-260 |
8.54e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 150.34 E-value: 8.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLLTLKEKT 86
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS----TLIRCINL-LERPTSGRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQE---------------PMTslnpLHNIEK-QINevlglhkgltgkvatQRTLELLELVGILEPHKR 150
Cdd:PRK11153 77 LRKAR-RQIGMIFQHfnllssrtvfdnvalPLE----LAGTPKaEIK---------------ARVTELLELVGLSDKADR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 151 LkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCV 230
Cdd:PRK11153 137 Y---PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAV 213
|
250 260 270
....*....|....*....|....*....|
gi 799207702 231 MQKGCIVEQADCETLFQSPQHPYTQELLAA 260
Cdd:PRK11153 214 IDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
299-530 |
1.14e-40 |
|
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: 146.93 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGQQLDRltqqQVRPLRREMQVVFQDPFg 373
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLagllkPDSGSILIDGEDVRK----EPREARRQIGVLPDERG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 sLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:COG4555 85 -LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 454 ALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAapqhGYTRQLLEAAFL 530
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE----EIGEENLEDAFV 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
292-503 |
2.30e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.96 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 292 LRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQD 370
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDpPTSGEIYLDGKPLSAMPPPE---WRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 P--FGslsprmcvsEIVGEGL-RIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:COG4619 83 PalWG---------GTVRDNLpFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-240 |
2.31e-40 |
|
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: 145.35 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKekt 86
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIA-GLERPDSGEILIDGRDVTGVP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irhIRGNRIAMIFQEPmtSLNPLHNIEKQIneVLGL-HKGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGGQRQR 165
Cdd:cd03259 69 ---PERRNIGMVFQDY--ALFPHLTVAENI--AFGLkLRGVPKAEIRARVRELLELVGLEGLLNRY---PHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQA 240
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
302-537 |
2.41e-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: 146.34 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPfgSLSPRMC 380
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGeVLLDGRDLASLSRRE---LARRIAYVPQEP--PAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHK--MGTPAEQ-EAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:COG1120 92 VRELVALGRYPHLglFGRPSAEdREAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFaapqhgyTRQLLEAAFLVPAARVD 537
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-------TPELLEEVYGVEARVIE 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
301-536 |
2.65e-40 |
|
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: 147.02 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRPLRRE-MQVVFQDpFGsLSPR 378
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQS-FA-LLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:cd03294 117 RTVLENVAFGLEVQGVP-RAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 459 VQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAaflVPAARV 536
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG---VDRAKV 269
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-245 |
3.54e-40 |
|
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: 145.02 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03260 1 IELRDLNVYY--GDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgnRIAMIFQEPmtslNPLH-NIEKQINEVLGLHKGLTGKVATQRTLELLELVGIL-EPHKRLKALphELSGGQRQ 164
Cdd:cd03260 77 LELRR--RVGMVFQKP----NPFPgSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRLHAL--GLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDVTvqLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCET 244
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPI--STAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 799207702 245 L 245
Cdd:cd03260 227 I 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-234 |
6.38e-40 |
|
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: 143.76 E-value: 6.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 8 EIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYAGQDLltl 82
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKS----TLLRLLngllgPT------SGEVLVDGKDL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 KEKTIRHIRGnRIAMIFQEPMTSL-NPlhNIEKQIneVLGL-HKGLTGKVATQRTLELLELVGILEphkRLKALPHELSG 160
Cdd:cd03225 66 TKLSLKELRR-KVGLVFQNPDDQFfGP--TVEEEV--AFGLeNLGLPEEEIEERVEEALELVGLEG---LRDRSPFTLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-510 |
6.68e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 151.33 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFvtGDhhqrVV--NNVSFDIKRGETIALVGESGSGKSvTAHSILrllpYPLARHPSGTINYAGQDL 79
Cdd:COG3845 1 MMPPALELRGITKRF--GG----VVanDDVSLTVRPGEIHALLGENGAGKS-TLMKIL----YGLYQPDSGEILIDGKPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 ltlkektirHIRGNR------IAMIFQEPM--TSLNPLHNIekqineVLGLHKGLTG----KVATQRTLELLELVGI-LE 146
Cdd:COG3845 70 ---------RIRSPRdaialgIGMVHQHFMlvPNLTVAENI------VLGLEPTKGGrldrKAARARIRELSERYGLdVD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 147 PHkrlkALPHELSGGQRQRVMIAMALANEPELLIADEPTTALdvTVQLKILELLKELQ-ARLGMALLLISHDLNLVRRIA 225
Cdd:COG3845 135 PD----AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQEADELFEILRRlAAEGKSIIFITHKLREVMAIA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 226 HRVCVMQKGCIVEQADCETLfqspqhpyTQELLAA-------EPSGGPATNVIGPPLLEVDDLKVwfPIKKGflrttvdy 298
Cdd:COG3845 209 DRVTVLRRGKVVGTVDTAET--------SEEELAElmvgrevLLRVEKAPAEPGEVVLEVENLSV--RDDRG-------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI--LRLIgSKGGIRFEGQQLDRLTQQQvrplRREMQVVF--QDPFGS 374
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLRPP-ASGSIRLDGEDITGLSPRE----RRRLGVAYipEDRLGR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 -LSPRMCVSE-IVgeglrihkmgtpaeqeaaiiaaLKEVGLDPESRH---------------------RYPHE------F 425
Cdd:COG3845 346 gLVPDMSVAEnLI----------------------LGRYRRPPFSRGgfldrkairafaeelieefdvRTPGPdtparsL 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALD----RTVQRQVVELLRSlqakyNLTYLFISHDLAVVKALSHQLMVVKHG 501
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRDA-----GAAVLLISEDLDEILALSDRIAVMYEG 478
|
....*....
gi 799207702 502 QVVEQGDAA 510
Cdd:COG3845 479 RIVGEVPAA 487
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
299-530 |
8.67e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.44 E-value: 8.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-G----SKGGIRFEGQQLDRLTQQqvrpLRREMQVVFQDPfg 373
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRMLlGllrpTSGEVRVLGEDVARDPAE----VRRRIGYVPQEP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:COG1131 83 ALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 454 ALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIfaapqhgyTRQLLEAAFL 530
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KARLLEDVFL 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
300-525 |
2.80e-39 |
|
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: 143.21 E-value: 2.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLdrlTQQQVRPLRREMQVVFQDPfgSLSPR 378
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDI---REQDPVELRRKIGYVIQQI--GLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGLDPES-RHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:cd03295 90 MTVEENIALVPKLLKWPKEKIRERADEL-LALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLL 525
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
301-517 |
4.15e-39 |
|
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: 142.38 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLdrltqQQVRPLRREMQVVFQDPfgSL 375
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGKDI-----TNLPPHKRPVNTVFQNY--AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:cd03300 84 FPHLTVFENIAFGLRLKKLP-KAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 456 DRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:cd03300 162 DLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-260 |
4.67e-39 |
|
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: 142.88 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLLTLKEK 85
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-PS----SGEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TirhiRGNRIAMIFQE-----PMTSLnplhniekqinEVLGL----HKGLTGKVAT---QRTLELLELVGILepHKRLKA 153
Cdd:COG1120 72 E----LARRIAYVPQEppapfGLTVR-----------ELVALgrypHLGLFGRPSAedrEAVEEALERTGLE--HLADRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 LpHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQK 233
Cdd:COG1120 135 V-DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
250 260
....*....|....*....|....*..
gi 799207702 234 GCIVEQADCETLFqspqhpyTQELLAA 260
Cdd:COG1120 214 GRIVAQGPPEEVL-------TPELLEE 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-253 |
1.95e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.09 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtGDhhQRVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLpYPLARHPSGTINYAGQDLLTLK-E 84
Cdd:COG3842 5 ALELENVSKRY--GD--VTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMI-AGFETPDSGRILLDGRDVTGLPpE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KtirhiRGnrIAMIFQE----PMtsLNPLHNIEKqinevlGL-HKGLTGKVATQRTLELLELVGiLEPHkrLKALPHELS 159
Cdd:COG3842 76 K-----RN--VGMVFQDyalfPH--LTVAENVAF------GLrMRGVPKAEIRARVAELLELVG-LEGL--ADRYPHQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLN--LVrrIAHRVCVMQKGCIV 237
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA--LADRIAVMNDGRIE 215
|
250
....*....|....*.
gi 799207702 238 EQADCETLFQSPQHPY 253
Cdd:COG3842 216 QVGTPEEIYERPATRF 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-231 |
2.97e-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: 139.53 E-value: 2.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLltlkekt 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIIA-GLERPTSGEVLVDGEPV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irHIRGNRIAMIFQEPmtSLNPLHNIEKqiNEVLGL-HKGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQRQR 165
Cdd:cd03293 69 --TGPGPDRGYVFQQD--ALLPWLTVLD--NVALGLeLQGVPKAEARERAEELLELVGLSG---FENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVM 231
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
288-505 |
3.32e-38 |
|
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: 139.79 E-value: 3.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 288 KKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLR- 361
Cdd:TIGR02211 12 QEGKLDTRV-----LKGVSLSIGKGEIVAIVGSSGSGKSTL----LHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQdpFGSLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDPESRHRyPHEFSGGQRQRIAIARALVL 441
Cdd:TIGR02211 83 KKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-SVKEAKERAYEMLEKVGLEHRINHR-PSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALShQLMVVKHGQVVE 505
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEMKDGQLFN 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-186 |
4.96e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 136.62 E-value: 4.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLtlkeKTIRHIRGNRIAMIFQEPmtS 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLT----DDERKSLRKEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 LNPLHNIEKQINEVLGLhKGLTGKVATQRTLELLELVGILE-PHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 799207702 185 TT 186
Cdd:pfam00005 149 TA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-514 |
1.11e-37 |
|
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: 139.49 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGqqLDRLTQQQVRPLRREMQVVFQDP-- 371
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLakllnGL----LLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVFQNPdn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 -FgslsprmcVSEIVGE----GL------------RIHKmgtpaeqeaaiiaALKEVGLDpESRHRYPHEFSGGQRQRIA 434
Cdd:TIGR04520 89 qF--------VGATVEDdvafGLenlgvpreemrkRVDE-------------ALKLVGME-DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 435 IARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVkALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-240 |
1.34e-37 |
|
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: 138.34 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 3 QDNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTL 82
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLA-GLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 KEKTIRHIRGNRIAMIFQE----P-MTSL-N---PLhniekqinEVLGLhkgltgKVATQRTLELLELVGILEphkRLKA 153
Cdd:COG4181 80 DEDARARLRARHVGFVFQSfqllPtLTALeNvmlPL--------ELAGR------RDARARARALLERVGLGH---RLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQK 233
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRA 221
|
....*..
gi 799207702 234 GCIVEQA 240
Cdd:COG4181 222 GRLVEDT 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
299-502 |
1.78e-37 |
|
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: 135.97 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GS 374
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPFlfsGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LsprmcvseivgeglrihkmgtpaeqeaaiiaalKEVGLdpesrhryphefSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:cd03228 92 I---------------------------------RENIL------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 455 LDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKaLSHQLMVVKHGQ 502
Cdd:cd03228 127 LDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-234 |
1.85e-37 |
|
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: 136.16 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgnRIAMIFQEP--MTSLNPLHNIekqinevlglhkgltgkvatqrtlellelvgilephkrlkALPheLSGGQRQ 164
Cdd:cd03229 72 PPLRR--RIGMVFQDFalFPHLTVLENI----------------------------------------ALG--LSGGQQQ 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
302-519 |
1.87e-37 |
|
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: 138.24 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTqqqvrPLRREMQVVFQDPfgSLSPRMC 380
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkILLNGKDITNLP-----PEKRDISYVPQNY--ALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHKMGTPAEQEAAIIAAlKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIA-EMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 461 RQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHG 519
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
276-503 |
3.10e-37 |
|
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: 136.89 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPIKKgflrttvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLD 350
Cdd:cd03262 1 IEIKNLHKSFGDFH-----------VLKGIDLTVKKGEVVVIIGPSGSGKSTL----LRCINlleepDSGTIIIDGLKLT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 rLTQQQVRPLRREMQVVFQDpFgSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQR 430
Cdd:cd03262 66 -DDKKNINELRQKVGMVFQQ-F-NLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 431 QRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-237 |
5.44e-37 |
|
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: 136.93 E-value: 5.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHhqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLKEK 85
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE------PtSGSVLIDGTDINKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGnRIAMIFQ-----EPMTSL-NPLHNIEKQINEVLGLHKGLTgKVATQRTLELLELVGILEPH-KRLKalphEL 158
Cdd:cd03256 72 ALRQLRR-QIGMIFQqfnliERLSVLeNVLSGRLGRRSTWRSLFGLFP-KEEKQRALAALERVGLLDKAyQRAD----QL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-260 |
6.02e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 6.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLl 80
Cdd:COG1121 1 MMMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PT----SGTVRLFGKPP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 tlkektirHIRGNRIAMIFQE-------PMTSLnplhniekqinEVLGL----HKGLT---GKVATQRTLELLELVGILE 146
Cdd:COG1121 71 --------RRARRRIGYVPQRaevdwdfPITVR-----------DVVLMgrygRRGLFrrpSRADREAVDEALERVGLED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 147 -PHKRLkalpHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIA 225
Cdd:COG1121 132 lADRPI----GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYF 206
|
250 260 270
....*....|....*....|....*....|....*
gi 799207702 226 HRVCVMQKGCIVeqadcetlFQSPQHPYTQELLAA 260
Cdd:COG1121 207 DRVLLLNRGLVA--------HGPPEEVLTPENLSR 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
302-453 |
6.52e-37 |
|
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: 133.54 E-value: 6.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLdrlTQQQVRPLRREMQVVFQDPFgsLSPRMC 380
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 381 VSEIVGEGLRIHKMGTpAEQEAAIIAALKEVGLDPESR---HRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:pfam00005 76 VRENLRLGLLLKGLSK-REKDARAEEALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-239 |
6.88e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 134.49 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 8 EIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLLTLKEKTI 87
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PS----SGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 88 RhirgNRIAMIFQepmtslnplhniekqinevlglhkgltgkvatqrtleLLELVGILepHKRLKALpHELSGGQRQRVM 167
Cdd:cd03214 72 A----RKIAYVPQ-------------------------------------ALELLGLA--HLADRPF-NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 168 IAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
300-517 |
8.41e-37 |
|
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: 137.58 E-value: 8.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDP--- 371
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLiqhlnGL----LKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPehq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 -----------FGslsPR-MCVSEivGEGLRIHKMgtpaeqeaaiiaALKEVGLDPESRHRYPHEFSGGQRQRIAIARAL 439
Cdd:TIGR04521 95 lfeetvykdiaFG---PKnLGLSE--EEAEERVKE------------ALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 440 VLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-250 |
1.29e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 137.20 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVV-NNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYAGQDLL 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKAlDDVSLTIEDGEFVAIIGHTGSGKS----TLIQHLngllkPT------SGTVTIDGRDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRgNRIAMIFQEPmtslnplhniEKQINE--VL-----GLHK-GLTGKVATQRTLELLELVGIlePHKRLK 152
Cdd:TIGR04521 71 AKKKKKLKDLR-KKVGLVFQFP----------EHQLFEetVYkdiafGPKNlGLSEEEAEERVKEALELVGL--DEEYLE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 153 ALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQ 232
Cdd:TIGR04521 138 RSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMH 217
|
250
....*....|....*...
gi 799207702 233 KGCIVEQADCETLFQSPQ 250
Cdd:TIGR04521 218 KGKIVLDGTPREVFSDVD 235
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
287-516 |
2.68e-36 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 134.93 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQqvrplR 361
Cdd:TIGR00968 6 ISKRFGSFQ-----ALDDVNLEVPTGSLVALLGPSGSGKSTL----LRIIAgleqpDSGRIRLNGQDATRVHAR-----D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVL 441
Cdd:TIGR00968 72 RKIGFVFQHY--ALFKHLTVRDNIAFGLEIRKH-PKAKIKARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:TIGR00968 148 EPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHP 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-258 |
2.84e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.97 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLltlkeKT 86
Cdd:COG1118 3 IEVRNISKRF--GSFT--LLDDVSLEIASGELVALLGPSGSGKT----TLLRII-AGLETPDSGRIVLNGRDL-----FT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQEP-----MTSLNplhNIEKqinevlGL-HKGLTGKVATQRTLELLELVGILEPHKRLkalPHELSG 160
Cdd:COG1118 69 NLPPRERRVGFVFQHYalfphMTVAE---NIAF------GLrVRPPSKAEIRARVEELLELVQLEGLADRY---PSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQA 240
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....*...
gi 799207702 241 DCETLFQSPQHPYTQELL 258
Cdd:COG1118 217 TPDEVYDRPATPFVARFL 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
304-526 |
3.46e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 135.26 E-value: 3.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLD---RLTQQQ--VRPLRREMQVVFQDpFg 373
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTL----LRCINlleqpEAGTIRVGDITIDtarSLSQQKglIRQLRQHVGFVFQN-F- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPEsRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 454 ALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLE 526
Cdd:PRK11264 174 ALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
272-517 |
3.89e-36 |
|
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: 135.17 E-value: 3.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 272 GPPLLEVDDLKVWFpikKGflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEG 346
Cdd:COG0411 1 SDPLLEVRGLTKRF---GG--------LVAVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLITgfyrpTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 347 QQLDRLTQQQV--RPLRRemqvVFQDP--FGSLSP----RMCVSEIVGEGLRIHKMGTPAEQEAAIIAA------LKEVG 412
Cdd:COG0411 66 RDITGLPPHRIarLGIAR----TFQNPrlFPELTVlenvLVAAHARLGRGLLAALLRLPRARREEREAReraeelLERVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 413 LDPEsRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALS 492
Cdd:COG0411 142 LADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
250 260
....*....|....*....|....*
gi 799207702 493 HQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:COG0411 221 DRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
305-517 |
4.72e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.37 E-value: 4.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLgLAILRL--IGSKGGIRFEGQQLD---RLTQQQVRPLRREMQVVFQDPfgSLSPRM 379
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSL-LRVLNLleTPDSGQLNIAGHQFDfsqKPSEKAIRLLRQKVGMVFQQY--NLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 CVSEIVGEG-LRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:COG4161 98 TVMENLIEApCKVLGL-SKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 459 VQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAgIFAAPQ 517
Cdd:COG4161 176 ITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQ 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
301-526 |
5.13e-36 |
|
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: 142.67 E-value: 5.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GSLS 376
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDVFlfsGTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 prmcvseivgEGLRihkMGTPAEQEAAIIAALKEVGLDPESRHRyPH-----------EFSGGQRQRIAIARALVLKPRL 445
Cdd:COG2274 567 ----------ENIT---LGDPDATDEEIIEAARLAGLHDFIEAL-PMgydtvvgeggsNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 446 ILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKaLSHQLMVVKHGQVVEQGDAAGIFAapQHGYTRQLL 525
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLA--RKGLYAELV 707
|
.
gi 799207702 526 E 526
Cdd:COG2274 708 Q 708
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-238 |
5.94e-36 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 133.63 E-value: 5.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHsILRLLPYPlarhPSGTINYAGQDLLTLKEK 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLH-LLGGLDNP----TSGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQ--EPMTSLNPLHNIEKQInevlgLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQR 163
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKSVKEAKERAYEMLEKVGL---EHRINHRPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAhRVCVMQKGCIVE 238
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEMKDGQLFN 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
255-510 |
7.41e-36 |
|
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: 141.05 E-value: 7.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 255 QELLAAE----PSGGPATNVIGPPLLEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGL 330
Cdd:COG4988 312 FALLDAPepaaPAGTAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 331 AILRLIG-SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GSLSprmcvseivgEGLRihkMGTPAEQEAAIIA 406
Cdd:COG4988 382 LLLGFLPpYSGSILINGVDLSDLDPAS---WRRQIAWVPQNPYlfaGTIR----------ENLR---LGRPDASDEELEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 407 ALKEVGLDPESRhRYPHEF-----------SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyN 475
Cdd:COG4988 446 ALEAAGLDEFVA-ALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--G 522
|
250 260 270
....*....|....*....|....*....|....*
gi 799207702 476 LTYLFISHDLAVVKALSHQLmVVKHGQVVEQGDAA 510
Cdd:COG4988 523 RTVILITHRLALLAQADRIL-VLDDGRIVEQGTHE 556
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
276-510 |
1.01e-35 |
|
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: 133.46 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTQ 354
Cdd:cd03256 1 IEVENLSKTYP----------NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 355 QQVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGlRIHKMGT--------PAEQEAAIIAALKEVGLDPESRHRyPHEFS 426
Cdd:cd03256 71 KALRQLRRQIGMIFQQF--NLIERLSVLENVLSG-RLGRRSTwrslfglfPKEEKQRALAALERVGLLDKAYQR-ADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 427 GGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQ 506
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
....
gi 799207702 507 GDAA 510
Cdd:cd03256 227 GPPA 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-260 |
1.41e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 133.76 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFV--TG---DHHQRVVNNVSFDIKRGETIALVGESGSGKSVtahsilrllpypLARHPSGTINYAGQD 78
Cdd:PRK15112 2 ETLLEVRNLSKTFRyrTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKST------------LAKMLAGMIEPTSGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 79 LLTLKEKTI---RHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPHKRLkaLP 155
Cdd:PRK15112 70 LLIDDHPLHfgdYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY--YP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGC 235
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
250 260
....*....|....*....|....*
gi 799207702 236 IVEQADCETLFQSPQHPYTQELLAA 260
Cdd:PRK15112 228 VVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
302-507 |
2.02e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.63 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQdpfgslsprmc 380
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeILLDGKDLASLSPKE---LARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 vseivgeglrihkmgtpaeqeaaiiaALKEVGLDPEsRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:cd03214 81 --------------------------ALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 461 RQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
300-517 |
2.38e-35 |
|
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: 132.46 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQqldRLTQQQVRplRREMQVVFQDPfgS 374
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAglerpDSGTILFGGE---DATDVPVQ--ERNVGFVFQHY--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSPRMCVSEIVGEGLRIHKMGTP---AEQEAAIIAALKEVGLDPESRhRYPHEFSGGQRQRIAIARALVLKPRLILLDEP 451
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 452 TSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-510 |
3.99e-35 |
|
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: 132.04 E-value: 3.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKgflrttvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLT 353
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----------QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 354 QQQVRPLRREMQVVFQDpfGSLSPRMCVSEIVGEGlRIHKMGT--------PAEQEAAIIAALKEVGLDpESRHRYPHEF 425
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQH--YNLIERLTVLENVLHG-RLGYKPTwrsllgrfSEEDKERALSALERVGLA-DKAYQRADQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVE 505
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
....*
gi 799207702 506 QGDAA 510
Cdd:TIGR02315 227 DGAPS 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-236 |
4.47e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKT 86
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHirgnRIAMIFQEP----MTslnplhnIEKQINEVLGLHKGltgKVATQRTLELLELVGIlePHKRLKALPHELSGGQ 162
Cdd:COG4619 72 WRR----QVAYVPQEPalwgGT-------VRDNLPFPFQLRER---KFDRERALELLERLGL--PPDILDKPVERLSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
297-525 |
4.77e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 133.68 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQqldRLTQQQVRPLRREMQVVFQDp 371
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT----LRMINrliepTSGRILIDGE---DIRDLDPVELRRRIGYVIQQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 fGSLSPRMCVSE---IVGEGL---------RIHKMgtpaeqeaaiiaaLKEVGLDPES-RHRYPHEFSGGQRQRIAIARA 438
Cdd:COG1125 85 -IGLFPHMTVAEniaTVPRLLgwdkeriraRVDEL-------------LELVGLDPEEyRDRYPHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 439 LVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDL--AVvkALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:COG1125 151 LAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTPEEILANP 228
|
....*....
gi 799207702 517 QHGYTRQLL 525
Cdd:COG1125 229 ANDFVADFV 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
287-516 |
9.82e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.98 E-value: 9.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLdRLTQQQVRPLR 361
Cdd:PRK09493 7 VSKHFGPTQV-----LHNIDLNIDQGEVVVIIGPSGSGKSTL----LRCINkleeiTSGDLIVDGLKV-NDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDpFgSLSPRMCVSEIVGEG-LRIHKMGTpAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALV 440
Cdd:PRK09493 77 QEAGMVFQQ-F-YLFPHLTALENVMFGpLRVRGASK-EEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 441 LKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-529 |
1.13e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLkvwfpikkgflrtTVDY--VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQL 349
Cdd:COG1121 4 MPAIELENL-------------TVSYggRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DRLTQQ-----QVRPLRREMqvvfqdpfgslsPrMCVSEIVGEGlRIHKMGTPAEQEAAIIAA----LKEVGLDpESRHR 420
Cdd:COG1121 71 RRARRRigyvpQRAEVDWDF------------P-ITVRDVVLMG-RYGRRGLFRRPSRADREAvdeaLERVGLE-DLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 421 YPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKH 500
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNR 214
|
250 260
....*....|....*....|....*....
gi 799207702 501 GqVVEQGDAAGIFaapqhgyTRQLLEAAF 529
Cdd:COG1121 215 G-LVAHGPPEEVL-------TPENLSRAY 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-517 |
1.83e-34 |
|
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: 129.86 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFpikKGFlrttvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLD 350
Cdd:cd03219 1 LEVRGLTKRF---GGL--------VALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISgflrpTSGSVLFDGEDIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RLTQQQVRplRREMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAA---------LKEVGLDPEsRHRY 421
Cdd:cd03219 66 GLPPHEIA--RLGIGRTFQIP--RLFPELTVLENVMVAAQARTGSGLLLARARREEReareraeelLERVGLADL-ADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 422 PHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHG 501
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
250
....*....|....*.
gi 799207702 502 QVVEQGDAAGIFAAPQ 517
Cdd:cd03219 220 RVIAEGTPDEVRNNPR 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-237 |
2.66e-34 |
|
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: 129.73 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHhqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEK 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV-----EPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQEpMTSLNPLHNIEKQINEVLGLHKGLTG------KVATQRTLELLELVGILE-PHKRLKalphEL 158
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQH-YNLIERLTVLENVLHGRLGYKPTWRSllgrfsEEDKERALSALERVGLADkAYQRAD----QL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
300-526 |
3.59e-34 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 132.67 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRPLRR-EMQVVFQDpFGsLSP 377
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEpTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQ-FA-LFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:TIGR01186 85 HMTILQNTSLGPELLGW-PEQERKEKALELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLE 526
Cdd:TIGR01186 163 LIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
299-518 |
4.16e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.12 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-G----SKGGIRFEGQQLDRLtqqqvRPLRREMQVVFQDPfg 373
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIaGledpTSGEILIGGRDVTDL-----PPKDRNIAMVFQSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDPEsRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:COG3839 85 ALYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLEDL-LDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQH 518
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-527 |
4.29e-34 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 131.46 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-------LRLIGSKggIRFEG 346
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDG-------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnWRVTADR--MRFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 347 QQLDRLTQQQVRPL-RREMQVVFQDPFGSLSP-----RMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGL-DPES-R 418
Cdd:PRK15093 73 IDLLRLSPRERRKLvGHNVSMIFQEPQSCLDPservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIkDHKDaM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 419 HRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260
....*....|....*....|....*....
gi 799207702 499 KHGQVVEQGDAAGIFAAPQHGYTRQLLEA 527
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRA 261
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-236 |
5.26e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 126.36 E-value: 5.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL-PYplarhpSGTINYAGQDLLTLKEK 85
Cdd:cd03230 1 IEVRNLSKRY--GKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPD------SGEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgnRIAMIFQEPMtslnplhniekqinevlgLHKGLTGKvatqrtlELLelvgilephkrlkalphELSGGQRQR 165
Cdd:cd03230 71 VKR-----RIGYLPEEPS------------------LYENLTVR-------ENL-----------------KLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-260 |
8.11e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 128.89 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLArhPS-GTINYAGQ-----DLLTLKEKTIRHIRGNRIAMIFQE 101
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLA--PDaGEVHYRMRdgqlrDLYALSEAERRRLLRTEWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMTSLNPL----HNIEKQINEVLGLHKGLTGKVATQrtleLLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPE 177
Cdd:PRK11701 98 PRDGLRMQvsagGNIGERLMAVGARHYGDIRATAGD----WLERVEI--DAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 178 LLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQEL 257
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLL 251
|
...
gi 799207702 258 LAA 260
Cdd:PRK11701 252 VSS 254
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-250 |
8.78e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.21 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPypLARHP-SGTINYAGQDL---LTLKEKTIRHIRGNrIAMI 98
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKS----SLLRVLN--LLETPdSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 99 FQE----P-MTSLNPLhnIEKQINeVLGLHKgltgKVATQRTLELLELVGILEphkRLKALPHELSGGQRQRVMIAMALA 173
Cdd:COG4161 88 FQQynlwPhLTVMENL--IEAPCK-VLGLSK----EQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 174 NEPELLIADEPTTALD--VTVQLKILELLKelqARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCEtLFQSPQ 250
Cdd:COG4161 158 MEPQVLLFDEPTAALDpeITAQVVEIIREL---SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQ 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
287-516 |
1.10e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.99 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGQQL-DRLTQQqvrpl 360
Cdd:PRK11432 12 ITKRFGSNTV-----IDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDGEDVtHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 361 rREMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALV 440
Cdd:PRK11432 78 -RDICMVFQSY--ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEA-LELVDLA-GFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 441 LKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
276-503 |
1.70e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 125.20 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPIKKgflrttvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLD 350
Cdd:cd03230 1 IEVRNLSKRYGKKT-----------ALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIILgllkpDSGEIKVLGKDIK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RltqqQVRPLRREMQVVFQDPfgSLSPRMCVSEIVgeglrihkmgtpaeqeaaiiaalkevgldpesrhryphEFSGGQR 430
Cdd:cd03230 66 K----EPEEVKRRIGYLPEEP--SLYENLTVRENL--------------------------------------KLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 431 QRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-256 |
1.79e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.85 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYPLARHpSGTINYAG 76
Cdd:COG1117 7 TLEPKIEVRNLNVYY--GDKQ--ALKDINLDIPENKVTALIGPSGCGKS----TLLRCLnrmndLIPGARV-EGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 77 QDLLTLKEKTIRHIRgnRIAMIFQEPmtslNPL-HNIEKqiNEVLGL--HKGLTGKVATQRTLELLELVGILEPHK-RLK 152
Cdd:COG1117 78 EDIYDPDVDVVELRR--RVGMVFQKP----NPFpKSIYD--NVAYGLrlHGIKSKSELDEIVEESLRKAALWDEVKdRLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 153 ALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-----------------VTVqlkilellkelqarlgmalLLIS 215
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakieelilelkkdYTI-------------------VIVT 210
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 799207702 216 HDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQE 256
Cdd:COG1117 211 HNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
305-507 |
1.85e-33 |
|
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: 126.64 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPqGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRlTQQQVR--PLRREMQVVFQDpfGSLSP 377
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTL----LRCIAglekpDGGTIVLNGTVLFD-SRKKINlpPQQRKIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIVGEGLRIHKmgtPAEQEAAIIAALKEVGLDPESRhRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:cd03297 89 HLNVRENLAFGLKRKR---NREDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-234 |
2.02e-33 |
|
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: 124.80 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL-PYplarhpSGTINYAGQDLLTLKEK 85
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPT------SGEILIDGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgNRIAMIFQEPM---TSLnpLHNIekqinevlglhkgltgkvatqrtlellelvgilephkrlkalpheLSGGQ 162
Cdd:cd03228 73 SLR----KNIAYVPQDPFlfsGTI--RENI---------------------------------------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKG 234
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETE--ALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-239 |
2.35e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 127.93 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvTahsilrllpypLARH------P-SGTINYAGQDl 79
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKS-T-----------LAKLlnglllPtSGKVTVDGLD- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 lTLKEKTIRHIRgNRIAMIFQepmtslNPlhniEKQI------NEV-LGL-HKGLTGKVATQRTLELLELVGILEphkRL 151
Cdd:TIGR04520 66 -TLDEENLWEIR-KKVGMVFQ------NP----DNQFvgatveDDVaFGLeNLGVPREEMRKRVDEALKLVGMED---FR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 152 KALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVM 231
Cdd:TIGR04520 131 DREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVM 209
|
....*...
gi 799207702 232 QKGCIVEQ 239
Cdd:TIGR04520 210 NKGKIVAE 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
305-525 |
3.39e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.41 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLtqqqvRPLRREMQVVFQDpfGSLSPRM 379
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTL----LNLIAgflppDSGRILWNGQDLTAL-----PPAERPVSMLFQE--NNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 CVSEIVGEGLR------------IHKMgtpaeqeaaiiaaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:COG3840 87 TVAQNIGLGLRpglkltaeqraqVEQA-------------LERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLL 525
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
300-502 |
4.50e-33 |
|
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: 123.51 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQqldRLTQQQVRPLRREMQVVFQdpfgslspr 378
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGeILIDGK---DIAKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 mcvseivgeglrihkmgtpaeqeaaiiaalkevgldpesrhrypheFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 799207702 459 VQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
299-503 |
6.01e-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: 125.21 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDpfGSLSP 377
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLdpESRHR-YPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:cd03292 92 DRNVYENVAFALEVTGVP-PREIRKRVPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 457 RTVQRQVVELLRSLQaKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:cd03292 169 PDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
302-533 |
7.47e-33 |
|
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: 128.96 E-value: 7.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI---GSKGGIRFEGQQLDRLTqqqvrPLRREMQVVFQDPfgSLSPR 378
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVkaaGLTGRIAIADRDLTHAP-----PHKRGLALLFQNY--ALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:TIGR03258 94 LKVEDNVAFGLRAQKM-PKADIAERVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDAN 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 459 VQRQVVELLRSLQAKY-NLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAAFLVPA 533
Cdd:TIGR03258 172 IRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
299-507 |
7.72e-33 |
|
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: 124.67 E-value: 7.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDrltqqQVRPLRREMQVVFQDPfg 373
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGGRDVT-----DLPPKDRDIAMVFQNY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVP-KDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
274-495 |
1.01e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.93 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFpiKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQ 348
Cdd:PRK11629 4 ILLQCDNLCKRY--QEGSVQTDV-----LHNVSFSIGEGEMMAIVGSSGSGKSTL----LHLLGgldtpTSGDVIFNGQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQQVRPLR-REMQVVFQdpFGSLSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDPESRHRyPHEFSG 427
Cdd:PRK11629 73 MSKLSSAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKK-KPAEINSRALEMLAAVGLEHRANHR-PSELSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQL 495
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
302-527 |
1.09e-32 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 125.58 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIgsKGGIRFEGQQLdRLTQQQVRP--LR-REMQVVFQDPFGSLSPR 378
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL--PAGVRQTAGRV-LLDGKPVAPcaLRgRKIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRihKMGTPAEQEAAIIAaLKEVGLDPESR--HRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:PRK10418 96 HTMHTHARETCL--ALGKPADDATLTAA-LEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 457 RTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEA 527
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
274-510 |
1.13e-32 |
|
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: 124.85 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKGFLrttvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQ 348
Cdd:COG4181 7 PIIELRGLTKTVGTGAGEL-------TILKGISLEVEAGESVAIVGASGSGKSTL----LGLLAgldrpTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQQVRPLRRE-MQVVFQDpFgSLSPRMCVSEIVG---EgLRIHKmgtpaEQEAAIIAALKEVGLDPESRHrYPHE 424
Cdd:COG4181 76 LFALDEDARARLRARhVGFVFQS-F-QLLPTLTALENVMlplE-LAGRR-----DARARARALLERVGLGHRLDH-YPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 425 FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVkALSHQLMVVKHGQVV 504
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLV 225
|
....*.
gi 799207702 505 EQGDAA 510
Cdd:COG4181 226 EDTAAT 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-528 |
1.58e-32 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 130.43 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLpYPLARHpSGTINYAGQdllTLKEKTIRHIRGNRIAMIFQEPM 103
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKS-TLMKVLSGV-YPHGTY-EGEIIFEGE---ELQASNIRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 --TSLNPLHNIekqineVLG---LHKGLTGKVA-TQRTLELLELVGI-LEPHKRLKalphELSGGQRQRVMIAMALANEP 176
Cdd:PRK13549 93 lvKELSVLENI------FLGneiTPGGIMDYDAmYLRAQKLLAQLKLdINPATPVG----NLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 177 ELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLfqspqhpyTQE 256
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM--------TED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 257 LLAAEPSGGPATNV-------IGPPLLEVDDLKVWFPIKKGflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLG 329
Cdd:PRK13549 234 DIITMMVGRELTALyprephtIGEVILEVRNLTAWDPVNPH--------IKRVDDVSFSLRRGEILGIAGLVGAGRTELV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 330 LAILrliG-----SKGGIRFEGQQLDRLTQQQVrpLRREMQVVFQD--PFGsLSPRMCVSE-IVGEGLRIHKMGTPAEQE 401
Cdd:PRK13549 306 QCLF---GaypgrWEGEIFIDGKPVKIRNPQQA--IAQGIAMVPEDrkRDG-IVPVMGVGKnITLAALDRFTGGSRIDDA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 402 AAIIAALKEVGldpESRHRYPHEF------SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYN 475
Cdd:PRK13549 380 AELKTILESIQ---RLKVKTASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQG 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 476 LTYLFISHDLAVVKALSHQLMVVKHGQVveQGDaagifaAPQHGYTR-QLLEAA 528
Cdd:PRK13549 456 VAIIVISSELPEVLGLSDRVLVMHEGKL--KGD------LINHNLTQeQVMEAA 501
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
305-517 |
2.22e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 124.36 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLgLAILRL--IGSKGGIRFEGQQLD---RLTQQQVRPLRREMQVVFQDPfgSLSPRM 379
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSL-LRVLNLleMPRSGTLNIAGNHFDfskTPSDKAIRELRRNVGMVFQQY--NLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 CVSEIVGEG-LRIHKMGTPAEQEAAIIAaLKEVGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:PRK11124 98 TVQQNLIEApCRVLGLSKDQALARAEKL-LERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 459 VQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGiFAAPQ 517
Cdd:PRK11124 176 ITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-516 |
3.40e-32 |
|
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: 126.07 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 317 IVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLdrltqQQVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGLRI 391
Cdd:TIGR01187 1 LLGPSGCGKTTL----LRLLAgfeqpDSGSIMLDGEDV-----TNVPPHLRHINMVFQSY--ALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 392 HKMG----TPAEQEAAIIAALKEVGldpesrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELL 467
Cdd:TIGR01187 70 RKVPraeiKPRVLEALRLVQLEEFA------DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207702 468 RSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
295-500 |
3.60e-32 |
|
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: 123.03 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 295 TVDY--VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLdrlTQQQVR----PLRREMQVV 367
Cdd:cd03235 6 TVSYggHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKPL---EKERKRigyvPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 368 FqdpfgslspRMCVSEIVGEGLRIHK---MGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPR 444
Cdd:cd03235 83 F---------PISVRDVVLMGLYGHKglfRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 445 LILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDL-AVVKALSHQLMVVKH 500
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLgLVLEYFDRVLLLNRT 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-234 |
4.43e-32 |
|
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: 122.74 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHhqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA---ALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLL-YGALTPSRGQVRIAGEDVNRLRGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQEpmTSLNPLHNIEKQIN---EVLGLHKGLTGKvatqRTLELLELVGILEphkRLKALPHELSGGQ 162
Cdd:TIGR02673 73 QLPLLR-RRIGVVFQD--FRLLPDRTVYENVAlplEVRGKKEREIQR----RVGAALRQVGLEH---KADAFPEQLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:TIGR02673 143 QQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
304-525 |
4.91e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 123.76 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLdRLTQ-----------QQVRPLRREMQVV 367
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTF----LRCINlletpDSGEIRVGGEEI-RLKPdrdgelvpadrRQLQRIRTRLGMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 368 FQDpFgSLSPRMCVSEIVGEGlRIHKMGTPAEQEAAI-IAALKEVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLI 446
Cdd:COG4598 101 FQS-F-NLWSHMTVLENVIEA-PVHVLGRPKAEAIERaEALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVM 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 447 LLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLL 525
Cdd:COG4598 177 LFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
287-516 |
5.25e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.60 E-value: 5.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGQQLDrltqqQVRPLR 361
Cdd:PRK09452 20 ISKSFDGKEV-----ISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIMLDGQDIT-----HVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKmgTPAEQEAAIIA-ALKEVGLDPESRHRyPHEFSGGQRQRIAIARALV 440
Cdd:PRK09452 86 RHVNTVFQSY--ALFPHMTVFENVAFGLRMQK--TPAAEITPRVMeALRMVQLEEFAQRK-PHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 441 LKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
27-260 |
6.67e-32 |
|
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: 123.40 E-value: 6.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 27 NNVSFDIKRGETIALVGESGSGKSVTAHSIL-RLLPyplarhPSGTINYAGQD-----LLTLKEKTIRHIRGNRIAMIFQ 100
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAP------DHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPMTSL----NPLHNIEKQINEVLGLHKGLTgKVATQRTLELLELvgilePHKRLKALPHELSGGQRQRVMIAMALANEP 176
Cdd:TIGR02323 94 NPRDGLrmrvSAGANIGERLMAIGARHYGNI-RATAQDWLEEVEI-----DPTRIDDLPRAFSGGMQQRLQIARNLVTRP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 177 ELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQE 256
Cdd:TIGR02323 168 RLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQL 247
|
....
gi 799207702 257 LLAA 260
Cdd:TIGR02323 248 LVSS 251
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
300-507 |
7.09e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.51 E-value: 7.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GSl 375
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTFlfsGT- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 sprmcvseiVGEGLRihkMGTPAEQEAAIIAALKEVGLdpesrhrypHEF-------------------SGGQRQRIAIA 436
Cdd:COG1132 430 ---------IRENIR---YGRPDATDEEVEEAAKAAQA---------HEFiealpdgydtvvgergvnlSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 437 RALVLKPRLILLDEPTSALD----RTVQRQVVELLRslqakyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:COG1132 489 RALLKDPPILILDEATSALDteteALIQEALERLMK------GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
255-526 |
8.48e-32 |
|
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: 129.12 E-value: 8.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 255 QELLAAEPS-GGPATNVIGP--PLLEVDDLkvwfpikkgflrtTVDY----VKAVDGINFSLPQGQTLGIVGESGSGKST 327
Cdd:COG4987 310 NELLDAPPAvTEPAEPAPAPggPSLELEDV-------------SFRYpgagRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 328 LGLAILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GSLsprmcvseivGEGLRIhkmGTPAEQEAA 403
Cdd:COG4987 377 LLALLLRFLDPQSGsITLGGVDLRDLDEDD---LRRRIAVVPQRPHlfdTTL----------RENLRL---ARPDATDEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 404 IIAALKEVGLD------PESRHRYPHE----FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAk 473
Cdd:COG4987 441 LWAALERVGLGdwlaalPDGLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA- 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 799207702 474 yNLTYLFISHDLAVVkALSHQLMVVKHGQVVEQGDAAGIFAapQHGYTRQLLE 526
Cdd:COG4987 520 -GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-239 |
1.75e-31 |
|
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: 129.18 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYAGQDLLT 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRhirgNRIAMIFQEPM---TSLnpLHNIekqineVLGlHKGLTgkvaTQRTLELLELVGIlepHKRLKALPH-- 156
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFlfsGTI--RENI------TLG-DPDAT----DEEIIEAARLAGL---HDFIEALPMgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ---------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVRRiAHR 227
Cdd:COG2274 602 dtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE--AIILENLRRLLKGRTVIIIAHRLSTIRL-ADR 678
|
250
....*....|..
gi 799207702 228 VCVMQKGCIVEQ 239
Cdd:COG2274 679 IIVLDKGRIVED 690
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-250 |
2.23e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 121.66 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 9 IRDLSVEFVTGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQ--DL-LTLKEK 85
Cdd:PRK11124 3 IQLNGINCFYGAH--QALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMP----RSGTLNIAGNhfDFsKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNrIAMIFQE----P-MTSLNPLhnIEKQINeVLGLHKgltgKVATQRTLELLELVGiLEPHKrlKALPHELSG 160
Cdd:PRK11124 76 AIRELRRN-VGMVFQQynlwPhLTVQQNL--IEAPCR-VLGLSK----DQALARAEKLLERLR-LKPYA--DRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALD--VTVQLKILELLKelqARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVE 238
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDpeITAQIVSIIREL---AETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
250
....*....|..
gi 799207702 239 QADcETLFQSPQ 250
Cdd:PRK11124 222 QGD-ASCFTQPQ 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-528 |
2.33e-31 |
|
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: 127.25 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyplARHPSGT----INYAGQDLltlKEKTIRHIRGNRIAMIF 99
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKS----TLMKILS---GVYPHGTwdgeIYWSGSPL---KASNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 100 QEPM--TSLNPLHNIEKQiNEVLglHKG--LTGKVATQRTLELLELVgilephkRLKALPH-----ELSGGQRQRVMIAM 170
Cdd:TIGR02633 85 QELTlvPELSVAENIFLG-NEIT--LPGgrMAYNAMYLRAKNLLREL-------QLDADNVtrpvgDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 171 ALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLfqspq 250
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 251 hpyTQELLAAEPSGGPATNV-------IGPPLLEVDDLKVWFPIKKgflrttvdYVKAVDGINFSLPQGQTLGIVGESGS 323
Cdd:TIGR02633 229 ---SEDDIITMMVGREITSLyphepheIGDVILEARNLTCWDVINP--------HRKRVDDVSFSLRRGEILGVAGLVGA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 324 GKSTLglaILRLIGS-----KGGIRFEGQQLDRLTQQQVrpLRREMQVVFQDpfgslSPRMCVSEIVGEGLRIHKMGTPA 398
Cdd:TIGR02633 298 GRTEL---VQALFGAypgkfEGNVFINGKPVDIRNPAQA--IRAGIAMVPED-----RKRHGIVPILGVGKNITLSVLKS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 399 EQEAAIIAALKEVGLDPESRHRYP----HEF------SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLR 468
Cdd:TIGR02633 368 FCFKMRIDAAAELQIIGSAIQRLKvktaSPFlpigrlSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 469 SLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVveQGDAAgifaapQHGYTR-QLLEAA 528
Cdd:TIGR02633 448 QL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL--KGDFV------NHALTQeQVLAAA 499
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-258 |
3.10e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.40 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlRLLPYPLA-RHPSGTINYAGQDLLTLK 83
Cdd:PRK11264 2 SAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAgTIRVGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRHIRgNRIAMIFQEpmTSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQR 163
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVT-VQLKILELLKELQARLGMalLLISHDLNLVRRIAHRVCVMQKGCIVEQADC 242
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPElVGEVLNTIRQLAQEKRTM--VIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
250
....*....|....*.
gi 799207702 243 ETLFQSPQHPYTQELL 258
Cdd:PRK11264 229 KALFADPQQPRTRQFL 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-234 |
4.83e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.31 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHsILRLLPYPlarhPSGTINYAGQDLLTLKEK 85
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTP----TSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQ--EPMTSLNPLHNIEKQInevlgLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQR 163
Cdd:PRK11629 80 AKAELRNQKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGER 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIaHRVCVMQKG 234
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-234 |
4.86e-31 |
|
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: 119.56 E-value: 4.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 8 EIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLltlkekti 87
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-PT----SGSIRVFGKPL-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 88 rHIRGNRIAMIFQepmtslnpLHNIEKQ----INEVLGL----HKGLTGKVAT---QRTLELLELVGILEPHKRLKAlph 156
Cdd:cd03235 64 -EKERKRIGYVPQ--------RRSIDRDfpisVRDVVLMglygHKGLFRRLSKadkAKVDEALERVGLSELADRQIG--- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
305-533 |
9.68e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 122.90 E-value: 9.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQL-DRLTQQQVRPLRREMQVVFQDPfgSLSPR 378
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTL----LRAIAglerpDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQEA--RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRihkmgtpAEQEAAIIAALKEV----GLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:COG4148 92 LSVRGNLLYGRK-------RAPRAERRISFDEVvellGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 455 LDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAAFLVPA 533
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
273-502 |
1.85e-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: 118.69 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKvwfpikKGFLRTTVDYVK--AVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRF- 344
Cdd:COG4778 2 TTLLEVENLS------KTFTLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTL----LKCIygnylPDSGSILVr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 345 -EGQQLD--RLTQQQVRPLRR-EMQVVFQdpFGSLSPRMCVSEIVGEGLRihKMGTPAEQ-EAAIIAALKEVGLDPESRH 419
Cdd:COG4778 72 hDGGWVDlaQASPREILALRRrTIGYVSQ--FLRVIPRVSALDVVAEPLL--ERGVDREEaRARARELLARLNLPERLWD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 420 RYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVK 499
Cdd:COG4778 148 LPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 799207702 500 HGQ 502
Cdd:COG4778 227 PFS 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
274-514 |
1.92e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.12 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPikkgflrTTVDYvkAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLdrl 352
Cdd:PRK13635 4 EIIRVEHISFRYP-------DAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 353 TQQQVRPLRREMQVVFQDP----FGSlsprmCVSEIVGEGLRIHkmGTPAEQEAA-IIAALKEVGLDpESRHRYPHEFSG 427
Cdd:PRK13635 72 SEETVWDVRRQVGMVFQNPdnqfVGA-----TVQDDVAFGLENI--GVPREEMVErVDQALRQVGME-DFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVkALSHQLMVVKHGQVVEQG 507
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEG 222
|
....*..
gi 799207702 508 DAAGIFA 514
Cdd:PRK13635 223 TPEEIFK 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-248 |
2.08e-30 |
|
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: 124.87 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVefvTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL-PYplarhpSGTINYAGQDLLTLKEK 85
Cdd:COG4988 337 IELEDVSF---SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPY------SGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgNRIAMIFQEPM---TSLnpLHNIekqinevlglhkGLTGKVATQRTL-ELLELVGILEphkRLKALPHE---- 157
Cdd:COG4988 408 SWR----RQIAWVPQNPYlfaGTI--RENL------------RLGRPDASDEELeAALEAAGLDE---FVAALPDGldtp 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 -------LSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCV 230
Cdd:COG4988 467 lgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD--AETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILV 543
|
250
....*....|....*...
gi 799207702 231 MQKGCIVEQADCETLFQS 248
Cdd:COG4988 544 LDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-260 |
3.30e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFvtGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQdllT 81
Cdd:PRK13635 1 MKEEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL-----LPEAGTITVGGM---V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHIRgNRIAMIFQEPMtslNPLHNIEKQINEVLGL-HKGLTGKVATQRTLELLELVGILEphkRLKALPHELSG 160
Cdd:PRK13635 71 LSEETVWDVR-RQVGMVFQNPD---NQFVGATVQDDVAFGLeNIGVPREEMVERVDQALRQVGMED---FLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQA 240
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
250 260
....*....|....*....|....*...
gi 799207702 241 DCETLFQSPQH--------PYTQELLAA 260
Cdd:PRK13635 223 TPEEIFKSGHMlqeigldvPFSVKLKEL 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
300-504 |
4.13e-30 |
|
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: 116.97 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRltqqqvRPLRREMQVVFQDPFGSLspr 378
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLNGKPIKA------KERRKSIGYVMQDVDYQL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 mcVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGL-DPESRHryPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:cd03226 85 --FTDSVREELLLGLKELDAGNEQAETV-LKDLDLyALKERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 458 TVQRQVVELLRSLQAKYNlTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:cd03226 160 KNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
300-507 |
5.41e-30 |
|
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: 117.33 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLI-----GSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDP--- 371
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLfrfydVSSGSILIDGQDIREVTLDS---LRRAIGVVPQDTvlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 ---------FGSLSprmcVSEI----VGEGLRIHK--MGTPAEQEAAiiaaLKEVGLdpesrhryphEFSGGQRQRIAIA 436
Cdd:cd03253 88 ndtigynirYGRPD----ATDEevieAAKAAQIHDkiMRFPDGYDTI----VGERGL----------KLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 437 RALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-524 |
6.22e-30 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 117.33 E-value: 6.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPFgsl 375
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLAS---LRRQIGLVSQDVF--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 sprmCVSEIVGEGLRIhkmGTPAEQEAAIIAALKEVGLdpesrhrypHEF-------------------SGGQRQRIAIA 436
Cdd:cd03251 87 ----LFNDTVAENIAY---GRPGATREEVEEAARAANA---------HEFimelpegydtvigergvklSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 437 RALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFAap 516
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA-- 225
|
....*...
gi 799207702 517 QHGYTRQL 524
Cdd:cd03251 226 QGGVYAKL 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
305-516 |
7.57e-30 |
|
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: 120.22 E-value: 7.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQ-QVRPLRREMQVVFQDpfGSLSPRMCVS 382
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRTLFDSRKGiFLPPEKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGLrihKMGTPAEQEAAIIAALKEVGLDPESRhRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ 462
Cdd:TIGR02142 94 GNLRYGM---KRARPSERRISFERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 463 VVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
299-528 |
1.12e-29 |
|
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: 116.87 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLtqqQVRPLRREMQVVFQDP---FGS 374
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeILLDGVDIRDL---NLRWLRSQIGLVSQEPvlfDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 lsprmcvseiVGEGLRihkMGTPAEQEAAIIAALKEVGLdpesrhrypHEF-------------------SGGQRQRIAI 435
Cdd:cd03249 93 ----------IAENIR---YGKPDATDEEVEEAAKKANI---------HDFimslpdgydtlvgergsqlSGGQKQRIAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 436 ARALVLKPRLILLDEPTSALDRTVQRQVVELLRslQAKYNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFAa 515
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA- 226
|
250
....*....|...
gi 799207702 516 pQHGYTRQLLEAA 528
Cdd:cd03249 227 -QKGVYAKLVKAQ 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-518 |
1.13e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFpikKGFlrttvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLR-------LIGS---KGGI 342
Cdd:COG1117 9 EPKIEVRNLNVYY---GDK--------QALKDINLDIPENKVTALIGPSGCGKSTL----LRclnrmndLIPGarvEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 343 RFEGQQ-LDRltqqQVRP--LRREMQVVFQ--DPFgslsPrMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPES 417
Cdd:COG1117 74 LLDGEDiYDP----DVDVveLRRRVGMVFQkpNPF----P-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 418 RHR---YPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYnlTYLFISHDLAVVKALSHQ 494
Cdd:COG1117 145 KDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|....
gi 799207702 495 LMVVKHGQVVEQGDAAGIFAAPQH 518
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPKD 246
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-260 |
1.14e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 117.21 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILR---LLPYPlarhPSGTINYAGQDLLTLK 83
Cdd:COG4598 9 LEVRDLHKSF--GDLE--VLKGVSLTARKGDVISIIGSSGSGKS----TFLRcinLLETP----DSGEIRVGGEEIRLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 ----------EKTIRHIRGnRIAMIFQE-----PMTSLN-----PLHniekqineVLGLHKgltgKVATQRTLELLELVG 143
Cdd:COG4598 77 drdgelvpadRRQLQRIRT-RLGMVFQSfnlwsHMTVLEnvieaPVH--------VLGRPK----AEAIERAEALLAKVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 144 ILEphkRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-------VTVQLKIlellkelqARLGMALLLISH 216
Cdd:COG4598 144 LAD---KRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelvgevLKVMRDL--------AEEGRTMLVVTH 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 799207702 217 DLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQELLAA 260
Cdd:COG4598 213 EMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
301-513 |
1.16e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLG-LAILRLIGSKGGIRFEGQqldRLTQQQVRPLRREMQVVFQDP----FGSL 375
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAkLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRKHIGIVFQNPdnqfVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 sprmcVSEIVGEGLRIHKMGTpAEQEAAIIAALKEVGLDPESRHRyPHEFSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:PRK13648 101 -----VKYDVAFGLENHAVPY-DEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 456 DRTVQRQVVELLRSLQAKYNLTYLFISHDLAvvKAL-SHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-237 |
1.48e-29 |
|
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: 116.38 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLKEk 85
Cdd:cd03219 1 LEVRGLTKRF--GGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR------PtSGSVLFDGEDITGLPP- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 tirHIRGNR-IAMIFQ--EPMTSLNPLHNIEkqinevLGLHKGLTG-----------KVATQRTLELLELVGIlepHKRL 151
Cdd:cd03219 70 ---HEIARLgIGRTFQipRLFPELTVLENVM------VAAQARTGSglllararreeREARERAEELLERVGL---ADLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 152 KALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVM 231
Cdd:cd03219 138 DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE-ETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVL 216
|
....*.
gi 799207702 232 QKGCIV 237
Cdd:cd03219 217 DQGRVI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-234 |
1.66e-29 |
|
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: 113.49 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 8 EIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKTI 87
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 88 RhirgNRIAMIFQepmtslnplhniekqinevlglhkgltgkvatqrtlellelvgilephkrlkalpheLSGGQRQRVM 167
Cdd:cd00267 72 R----RRIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 168 IAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
27-234 |
1.99e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 115.20 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 27 NNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEKTIRHIRgNRIAMIFQEP--MT 104
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKS----TLLKLI-YKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFrlLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLNPLHNIEKQInEVLGLhkglTGKVATQRTLELLELVGIlePHKRlKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:cd03292 92 DRNVYENVAFAL-EVTGV----PPREIRKRVPAALELVGL--SHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 799207702 185 TTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-250 |
2.23e-29 |
|
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: 115.80 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEkt 86
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIA-GFETPTSGEILLDGKDITNLPP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irHIRGnrIAMIFQEpmTSLNPLHNIEKQIneVLGLH-KGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGGQRQR 165
Cdd:cd03300 70 --HKRP--VNTVFQN--YALFPHLTVFENI--AFGLRlKKLPKAEIKERVAEALDLVQLEGYANRK---PSQLSGGQQQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
....*
gi 799207702 246 FQSPQ 250
Cdd:cd03300 219 YEEPA 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-239 |
2.91e-29 |
|
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: 115.73 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLpYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRML-AGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIrgnriAMIFQEpmtslNPLH---NIEKQINEVLGLHkGLTGKVATQRTLELLELVGILEP-HKRLkalpHELSGG 161
Cdd:COG4555 72 ARRQI-----GVLPDE-----RGLYdrlTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFlDRRV----GELSTG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-258 |
4.93e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.80 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEK 85
Cdd:PRK09493 1 MIEFKNVSKHF--GPT--QVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCIN-KLEEITSGDLIVDGLKVNDPKVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 tIRHIRgNRIAMIFQE----P-MTSLN-----PLHNiekqinevlglhKGLTGKVATQRTLELLELVGILEphkRLKALP 155
Cdd:PRK09493 72 -ERLIR-QEAGMVFQQfylfPhLTALEnvmfgPLRV------------RGASKEEAEKQARELLAKVGLAE---RAHHYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVCVMQKGC 235
Cdd:PRK09493 135 SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
250 260
....*....|....*....|...
gi 799207702 236 IVEQADCETLFQSPQHPYTQELL 258
Cdd:PRK09493 214 IAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-234 |
5.41e-29 |
|
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: 113.93 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFDIKrGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKTIRHIRGNRIAMIFQEpmTSLN 107
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKS----TLLRCIA-GLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 108 PLHNIEKQIneVLGLhKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTA 187
Cdd:cd03297 88 PHLNVRENL--AFGL-KRKRNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 188 LDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
302-529 |
5.73e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGQQLDRLTQQQvRPLRREM-----QVVFqdP 371
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTL----LRALsgelsPDSGEVRLNGRPLADWSPAE-LARRRAVlpqhsSLSF--P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 FGslsprmcVSEIVGEGLRIHKmGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALV------LKPRL 445
Cdd:PRK13548 91 FT-------VEEVVAMGRAPHG-LSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 446 ILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGdaagifaAPQHGYTRQLL 525
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG-------TPAEVLTPETL 234
|
....
gi 799207702 526 EAAF 529
Cdd:PRK13548 235 RRVY 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
283-507 |
7.19e-29 |
|
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: 114.24 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 283 VWFPIKKGflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQvrpLR 361
Cdd:cd03254 8 VNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDISRKS---LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQVVFQDPFgsLSPRMCVSEIvgeglrihKMGTPAEQEAAIIAALKEVGLDPESRHR---YPHE-------FSGGQRQ 431
Cdd:cd03254 77 SMIGVVLQDTF--LFSGTIMENI--------RLGRPNATDEEVIEAAKEAGAHDFIMKLpngYDTVlgenggnLSQGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 432 RIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
304-529 |
7.39e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 7.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQ----------QLDRLTQQQVRPLRREMQVVF 368
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTF----LRCINflekpSEGSIVVNGQtinlvrdkdgQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 369 QDpfGSLSPRMCVSEIVGEGlRIHKMG-TPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:PRK10619 99 QH--FNLWSHMTVLENVMEA-PIQVLGlSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEA 527
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
..
gi 799207702 528 AF 529
Cdd:PRK10619 255 SL 256
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-237 |
1.22e-28 |
|
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: 113.23 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLtlkeKTIRHIRgNRIAMIFQEP 102
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK------PtSGRATVAGHDVV----REPREVR-RRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 MT--SLNPLHNIEKQinevlGLHKGLTGKVATQRTLELLELVGILE-PHKRLKALphelSGGQRQRVMIAMALANEPELL 179
Cdd:cd03265 83 SVddELTGWENLYIH-----ARLYGVPGAERRERIDELLDFVGLLEaADRLVKTY----SGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 180 IADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
274-529 |
1.43e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.10 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKgflrttvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL------IGSKGGIRFEGQ 347
Cdd:PRK14239 4 PILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QLDRLTQQQVRpLRREMQVVFQDPfgslSP-RMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYpHE-- 424
Cdd:PRK14239 73 NIYSPRTDTVD-LRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-HDsa 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 425 --FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYnlTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:PRK14239 147 lgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGD 224
|
250 260
....*....|....*....|....*..
gi 799207702 503 VVEQGDAAGIFAAPQHGYTRQLLEAAF 529
Cdd:PRK14239 225 LIEYNDTKQMFMNPKHKETEDYISGKF 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-228 |
2.16e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.95 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRllpyPLARHPSGTINYAGQDLL 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILA----GLDDGSSGEVSLVGQPLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRGNRIAMIFQEPM--TSLNPLHNIEkqineVLGLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHEL 158
Cdd:PRK10584 76 QMDEEARAKLRAKHVGFVFQSFMliPTLNALENVE-----LPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRV 228
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
301-513 |
2.28e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLG---LAILRliGSKGGIRFEGQQLDRLTqqqVRPLRREMQVVFQDP---FGS 374
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISkilTGLLK--PQSGEIKIDGITISKEN---LKEIRKKIGIIFQNPdnqFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSprmcVSEIVGEGLRiHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:PRK13632 99 AT----VEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 455 LDRTVQRQVVELLRSLQAKYNLTYLFISHDL-AVVKAlsHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAILA--DKVIVFSEGKLIAQGKPKEIL 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-260 |
2.74e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.09 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLltlkek 85
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLA-GFEQPTAGQIMLDGVDL------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 tiRHIRGNR--IAMIFQEpmTSLNPLHNIEKQINEVLGLHKGLTGKVaTQRTLELLELVGILEPHKRLkalPHELSGGQR 163
Cdd:PRK11607 84 --SHVPPYQrpINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEI-ASRVNEMLGLVHMQEFAKRK---PHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCE 243
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
250
....*....|....*..
gi 799207702 244 TLFQSPQHPYTQELLAA 260
Cdd:PRK11607 236 EIYEHPTTRYSAEFIGS 252
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-241 |
3.19e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 115.57 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLkekt 86
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIA-GLEHQTSGHIRFHGTDVSRL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irHIRGNRIAMIFQ-----EPMTSLNplhNIEKQINeVLGLHKGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGG 161
Cdd:PRK10851 70 --HARDRKVGFVFQhyalfRHMTVFD---NIAFGLT-VLPRRERPNAAAIKAKVTQLLEMVQLAHLADRY---PAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIvEQAD 241
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI-EQAG 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-259 |
3.97e-28 |
|
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: 118.33 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKT 86
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEP---MTSLnpLHNIekqinevlglhkgLTGKV-ATQRTL-ELLELVGIlepHKRLKALPH----- 156
Cdd:COG4987 407 LR----RRIAVVPQRPhlfDTTL--RENL-------------RLARPdATDEELwAALERVGL---GDWLAALPDgldtw 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ------ELSGGQRQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQARlgmALLLISHDLNLVRRiAHRVC 229
Cdd:COG4987 465 lgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGR---TVLLITHRLAGLER-MDRIL 540
|
250 260 270
....*....|....*....|....*....|
gi 799207702 230 VMQKGCIVEQADCETLFQspQHPYTQELLA 259
Cdd:COG4987 541 VLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-259 |
4.22e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 112.75 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLLT 81
Cdd:PRK10619 1 MSENKLNVIDLHKRY--GEHE--VLKGVSLQANAGDVISIIGSSGSGKS----TFLRCINF-LEKPSEGSIVVNGQTINL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKE----------KTIRHIRgNRIAMIFQE--PMTSLNPLHNIEKQINEVLGLHKgltgKVATQRTLELLELVGILEPHK 149
Cdd:PRK10619 72 VRDkdgqlkvadkNQLRLLR-TRLTMVFQHfnLWSHMTVLENVMEAPIQVLGLSK----QEARERAVKYLAKVGIDERAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 150 rlKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVqLKILELLKELQARLGMALLLISHDLNLVRRIAHRVC 229
Cdd:PRK10619 147 --GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
250 260 270
....*....|....*....|....*....|
gi 799207702 230 VMQKGCIVEQADCETLFQSPQHPYTQELLA 259
Cdd:PRK10619 224 FLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
301-510 |
5.85e-28 |
|
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: 111.37 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQVrpLRREMQVVFQDP--FGSLSp 377
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGRDITGLPPHER--ARAGIGYVPEGRriFPELT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 rmcvseiVGEGLRihkMGTPAEQEAAIIAALKEV-GLDP---ESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:cd03224 92 -------VEENLL---LGAYARRRAKRKARLERVyELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 454 ALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAA 510
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAA 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-228 |
6.06e-28 |
|
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: 110.78 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 9 IRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQDLLTLKEKTIR 88
Cdd:TIGR03608 1 LKNISKKF--GDKV--ILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKF----DSGQVYLNGQETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 89 HIRGNRIAMIFQE--PMTSLNPLHNIEkqinevLGL-HKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQR 165
Cdd:TIGR03608 72 KFRREKLGYLFQNfaLIENETVEENLD------LGLkYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 166 VMIAMALANEPELLIADEPTTALDvTVQLKILELLKELQARLGMALLLISHDLnLVRRIAHRV 228
Cdd:TIGR03608 143 VALARAILKPPPLILADEPTGSLD-PKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-506 |
6.51e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQ 348
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTTL----LNLIAgflapSSGEITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 L-----DRltqqqvrplrremQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPH 423
Cdd:COG4525 71 VtgpgaDR-------------GVVFQKD--ALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGLA-DFARRRIW 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 424 EFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDL--AVVKALSHQLMVVKHG 501
Cdd:COG4525 134 QLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALFLATRLVVMSPGPG 213
|
....*
gi 799207702 502 QVVEQ 506
Cdd:COG4525 214 RIVER 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-256 |
7.08e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.93 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFvtGDhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLP-YPLARhPSGTINYAGQDLLTLK 83
Cdd:PRK14247 2 NKIEIRDLKVSF--GQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElYPEAR-VSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRHirgnRIAMIFQEPmtslNPLHNIEKQINEVLGLHKGLTGKVAT---QRTLELLELVGILEPHK-RLKALPHELS 159
Cdd:PRK14247 77 VIELRR----RVQMVFQIP----NPIPNLSIFENVALGLKLNRLVKSKKelqERVRWALEKAQLWDEVKdRLDAPAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLD--PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
250
....*....|....*..
gi 799207702 240 ADCETLFQSPQHPYTQE 256
Cdd:PRK14247 227 GPTREVFTNPRHELTEK 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
300-532 |
8.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGQQLdrlTQQQV--RPLRREMQVVFQDP- 371
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLiqhlnGL----LKPTSGKIIIDGVDI---TDKKVklSDIRKKVGLVFQYPe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 -------------FGSLSPRMCVSEI---VGEGLRIhkmgtpaeqeaaiiaalkeVGLDPES-RHRYPHEFSGGQRQRIA 434
Cdd:PRK13637 94 yqlfeetiekdiaFGPINLGLSEEEIenrVKRAMNI-------------------VGLDYEDyKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 435 IARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIF- 513
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFk 234
|
250 260 270
....*....|....*....|....*....|
gi 799207702 514 ----------AAPQHGY-TRQLLEAAFLVP 532
Cdd:PRK13637 235 evetlesiglAVPQVTYlVRKLRKKGFNIP 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
302-528 |
1.01e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.86 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQL---DRLTQQQVRPL--RREMQVVFQ--DPFgs 374
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRlfgRNIYSPDVDPIevRREVGMVFQypNPF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 lsPRMCVSEIVGEGLRIHKMGTPAEQEAAIIA-ALKEVGLDPESRHR---YPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:PRK14267 98 --PHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 451 PTSALDRTVQRQVVELLRSLQAKYnlTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLLEAA 528
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-239 |
1.07e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFvTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLArhpSGTINYAGQDLLTLKE 84
Cdd:COG1132 340 IEFENVS--F-SYPGDRPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLrfYDPT---SGRILIDGVDIRDLTL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KTIRhirgNRIAMIFQEPM---TSLnpLHNI--------EKQINEVLglhkgltgkvatqrtlellELVGIlepHKRLKA 153
Cdd:COG1132 410 ESLR----RQIGVVPQDTFlfsGTI--RENIrygrpdatDEEVEEAA-------------------KAAQA---HEFIEA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 LPH-----------ELSGGQRQRVMIAMALANEPELLIADEPTTALDV----TVQlkilellkelQA--RL--GMALLLI 214
Cdd:COG1132 462 LPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTeteaLIQ----------EAleRLmkGRTTIVI 531
|
250 260
....*....|....*....|....*
gi 799207702 215 SHDLNLVRRiAHRVCVMQKGCIVEQ 239
Cdd:COG1132 532 AHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-239 |
1.14e-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: 111.09 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLlpY-PLarhpSGTINYAGQDLLTLkek 85
Cdd:cd03249 1 IEFKNVSFRYPSRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF--YdPT----SGEILLDGVDIRDL--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQEPMtslnpLHNIEKQINEVLGLHKgltgkvATQRTLEllELVGILEPHKRLKALPH--------- 156
Cdd:cd03249 71 NLRWLR-SQIGLVSQEPV-----LFDGTIAENIRYGKPD------ATDEEVE--EAAKKANIHDFIMSLPDgydtlvger 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 --ELSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKG 234
Cdd:cd03249 137 gsQLSGGQKQRIAIARALLRNPKILLLDEATSALD--AESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNG 213
|
....*
gi 799207702 235 CIVEQ 239
Cdd:cd03249 214 QVVEQ 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-505 |
1.64e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.93 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 9 IRDLSVEFvtGDhhQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpyplarhpsgtinyAGQDLLTlkEKTIR 88
Cdd:COG0488 1 LENLSKSF--GG--RPLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKIL--------------AGELEPD--SGEVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 89 HIRGNRIAMIFQEP------------MTSLNPLHNIEKQINEVLGLHKG----------LTGKVAT-------QRTLELL 139
Cdd:COG0488 57 IPKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEpdedlerlaeLQEEFEAlggweaeARAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 140 ELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDV-TVqlkilellkelQ------ARLGMALL 212
Cdd:COG0488 137 SGLGF--PEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSI-----------EwleeflKNYPGTVL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 213 LISHDLNLVRRIAHRVCVMQKGCI-------------------VEQADCETL-------------FQSPQHPYTQ----- 255
Cdd:COG0488 204 VVSHDRYFLDRVATRILELDRGKLtlypgnysayleqraerleQEAAAYAKQqkkiakeeefirrFRAKARKAKQaqsri 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 256 ------ELLAAEPSGG------PATNVIGPPLLEVDDLkvwfpiKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGS 323
Cdd:COG0488 284 kaleklEREEPPRRDKtveirfPPPERLGKKVLELEGL------SKSYGDKTL-----LDDLSLRIDRGDRIGLIGPNGA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 324 GKSTLglaiLRLIGSK----GGIRFEGQQLDR--LTQQQvrplrREMqvvfqDPfgSLSPRMCVSEIVGEGLRIHKMGTp 397
Cdd:COG0488 353 GKSTL----LKLLAGElepdSGTVKLGETVKIgyFDQHQ-----EEL-----DP--DKTVLDELRDGAPGGTEQEVRGY- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 398 aeqeaaiiaaLKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDrtvqrqvVELLRSLQ---AKY 474
Cdd:COG0488 416 ----------LGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-------IETLEALEealDDF 478
|
570 580 590
....*....|....*....|....*....|.
gi 799207702 475 NLTYLFISHDLAVVKALSHQLMVVKHGQVVE 505
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
303-524 |
1.68e-27 |
|
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: 116.98 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLR-LIG----SKGGIRFEGQQLDRLTQQQVRplrREMQVVFQDpfGSLSP 377
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTL----LRlLLGfetpESGSVFYDGQDLAGLDVQAVR---RQLGVVLQN--GRLMS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIVGeglrihkmGTPAEQEAAIIAaLKEVGLD------PESRHRYPHE----FSGGQRQRIAIARALVLKPRLIL 447
Cdd:TIGR03797 541 GSIFENIAG--------GAPLTLDEAWEA-ARMAGLAediramPMGMHTVISEgggtLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAkynlTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGD------AAGIFAAPQHgyt 521
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLERLKV----TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTydelmaREGLFAQLAR--- 683
|
...
gi 799207702 522 RQL 524
Cdd:TIGR03797 684 RQL 686
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-245 |
1.71e-27 |
|
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: 110.22 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplARhpSGTINYAGQDLLTLK-EK 85
Cdd:cd03224 1 LEVENLNAGY--GKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PR--SGSIRFDGRDITGLPpHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhiRGnrIAMIFQEPM--TSLNPLHNIEkqinevLGLHKGltGKVATQRTLE-LLELVGILEphKRLKALPHELSGGQ 162
Cdd:cd03224 72 RAR--AG--IGYVPEGRRifPELTVEENLL------LGAYAR--RRAKRKARLErVYELFPRLK--ERRKQLAGTLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKElqARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQAD 241
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLApKIVEEIFEAIREL--RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
....
gi 799207702 242 CETL 245
Cdd:cd03224 216 AAEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-260 |
1.75e-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: 110.51 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLltlkekT 86
Cdd:cd03296 3 IEVRNVSKRF--GDF--VALDDVSLDIPSGELVALLGPSGSGKT----TLLRLIA-GLERPDSGTILFGGEDA------T 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQ-----EPMTSLNplhniekqiNEVLGL---HKGLTGKVAT--QRTLELLELVGILEPHKRLkalPH 156
Cdd:cd03296 68 DVPVQERNVGFVFQhyalfRHMTVFD---------NVAFGLrvkPRSERPPEAEirAKVHELLKLVQLDWLADRY---PA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
250 260
....*....|....*....|....
gi 799207702 237 VEQADCETLFQSPQHPYTQELLAA 260
Cdd:cd03296 216 EQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
299-517 |
2.84e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS-KGGIRFEGQqldRLTQQQVRPLRREMQVVFQDPFGSLSP 377
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGE---LLTAENVWNLRRKIGMVFQNPDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 rMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHryPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:PRK13642 97 -ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVkALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
302-503 |
2.90e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.98 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGqqlDRLTQQQVRPLRREMQVVFQDP----F 372
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKST----TVRLIDglleaESGQIIIDG---DLLTEENVWDIRHKIGMVFQNPdnqfV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 GSlsprmCVSEIVGEGLRihKMGTPAEQEAA-IIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEP 451
Cdd:PRK13650 96 GA-----TVEDDVAFGLE--NKGIPHEEMKErVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 799207702 452 TSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVkALSHQLMVVKHGQV 503
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-246 |
4.72e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.59 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGqDLLTlk 83
Cdd:PRK13650 2 SNIIEVKNLTFKYKE-DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL-----EAESGQIIIDG-DLLT-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRHIRgNRIAMIFQEPMtslNPLHNIEKQINEVLGL-HKGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGGQ 162
Cdd:PRK13650 73 EENVWDIR-HKIGMVFQNPD---NQFVGATVEDDVAFGLeNKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVrRIAHRVCVMQKGCIVEQADC 242
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTP 224
|
....
gi 799207702 243 ETLF 246
Cdd:PRK13650 225 RELF 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
300-517 |
5.41e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.49 E-value: 5.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGQQLDRLT-QQQVRPLRREMQVVFQDP-- 371
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlnGL----LQPTSGTVTIGERVITAGKkNKKLKPLRKKVGIVFQFPeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 ------------FGSLSprMCVSEIVGEgLRIHKMgtpaeqeaaiiaaLKEVGLDPESRHRYPHEFSGGQRQRIAIARAL 439
Cdd:PRK13634 97 qlfeetvekdicFGPMN--FGVSEEDAK-QKAREM-------------IELVGLPEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 440 VLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
301-507 |
5.55e-27 |
|
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: 108.73 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLtqqQVRPLRREMQVVFQDPF---GSLS 376
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKI---GLHDLRSRISIIPQDPVlfsGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRMCVSEIVGEGlRIHKmgtpaeqeaaiiaALKEVGLD-----PESRHRYPHE-----FSGGQRQRIAIARALVLKPRLI 446
Cdd:cd03244 96 SNLDPFGEYSDE-ELWQ-------------ALERVGLKefvesLPGGLDTVVEeggenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 447 LLDEPTSALDRTVQRQVVELLRSlqAKYNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-261 |
5.95e-27 |
|
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: 108.96 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHQRvvnNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLK-E 84
Cdd:cd03299 1 LKVENLSKDW--KEFKLK---NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK------PdSGKILLNGKDITNLPpE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KtirhirgNRIAMIFQEpmTSLNPLHNIEKQIneVLGLHKGLTGKVATQR-TLELLELVGILEphkRLKALPHELSGGQR 163
Cdd:cd03299 70 K-------RDISYVPQN--YALFPHMTVYKNI--AYGLKKRKVDKKEIERkVLEIAEMLGIDH---LLNRKPETLSGGEQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCE 243
Cdd:cd03299 136 QRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
250
....*....|....*...
gi 799207702 244 TLFQSPQHPYTQELLAAE 261
Cdd:cd03299 216 EVFKKPKNEFVAEFLGFN 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
300-514 |
7.78e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.87 E-value: 7.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQ-QQVRPLRREMQVVFQDP------ 371
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKTKdKYIRPVRKRIGMVFQFPesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 --------FGSLSPRMCVSEIVGEGLRIhkmgtpaeqeaaiiaaLKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKP 443
Cdd:PRK13646 101 dtvereiiFGPKNFKMNLDEVKNYAHRL----------------LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 444 RLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
290-521 |
8.36e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.80 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 290 GFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQL----DRLTQQQVRPLRREMQ 365
Cdd:PRK14271 30 GFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 366 VVFQDPfgslSP-RMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRY---PHEFSGGQRQRIAIARALVL 441
Cdd:PRK14271 105 MLFQRP----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKynLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYT 521
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
287-523 |
1.02e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.97 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQqLDRLTQQ------QVRPL 360
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGR-VEFFNQNiyerrvNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 361 RREMQVVFQDPfgSLSPrMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESR---HRYPHEFSGGQRQRIAIAR 437
Cdd:PRK14258 87 RRQVSMVHPKP--NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKhkiHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 438 ALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKH-----GQVVEQGDAAGI 512
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|.
gi 799207702 513 FAAPQHGYTRQ 523
Cdd:PRK14258 244 FNSPHDSRTRE 254
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
287-526 |
1.05e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.33 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQqqvrplr 361
Cdd:PRK10851 8 IKKSFGRTQV-----LNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAglehqTSGHIRFHGTDVSRLHA------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQV--VFQDPfgSLSPRMCVSEIVGEGLRI---HKMGTPAEQEAAIIAALKEVGLDpesrH---RYPHEFSGGQRQRI 433
Cdd:PRK10851 72 RDRKVgfVFQHY--ALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLA----HladRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 434 AIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
250
....*....|...
gi 799207702 514 AAPQhgyTRQLLE 526
Cdd:PRK10851 226 REPA---TRFVLE 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
301-525 |
1.30e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRPLRRE-MQVVFQDpfGSLSPR 378
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIhkMGTPAEQEAAIIA-ALKEVGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:PRK10070 121 MTVLDNTAFGMEL--AGINAEERREKALdALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQLL 525
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
301-513 |
1.32e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-LRLIGSKGGIRFEGqqLDRLTQQQVRPLRREMQVVFQDPFGSLsprm 379
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 cVSEIVGEGLRI--HKMGT-PAEQEAAIIAALKEVGLDPESRHRyPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:PRK13633 99 -VATIVEEDVAFgpENLGIpPEEIRERVDESLKKVGMYEYRRHA-PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 457 RTVQRQVVELLRSLQAKYNLTYLFISHDL-AVVKAlsHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-237 |
2.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.60 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRV-VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLlTLKEK 85
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL-----KPTSGKIIIDGVDI-TDKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQEPMTSLNPlHNIEKQIneVLGLHK-GLTGKVATQRTLELLELVGiLEPHKRLKALPHELSGGQRQ 164
Cdd:PRK13637 77 KLSDIR-KKVGLVFQYPEYQLFE-ETIEKDI--AFGPINlGLSEEEIENRVKRAMNIVG-LDYEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
276-508 |
2.50e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaILRLIG----SKGGIRFEGQQLDR 351
Cdd:PRK13647 5 IEVEDLHFRYK----------DGTKALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLNGiylpQRGRVKVMGREVNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 352 LTQQQVRplrREMQVVFQDP--------------FGSLSPRMCVSEI---VGEGLRIHKMgtpaeqeaaiiaalkevgld 414
Cdd:PRK13647 72 ENEKWVR---SKVGLVFQDPddqvfsstvwddvaFGPVNMGLDKDEVerrVEEALKAVRM-------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 415 PESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQ 494
Cdd:PRK13647 129 WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQ 207
|
250
....*....|....
gi 799207702 495 LMVVKHGQVVEQGD 508
Cdd:PRK13647 208 VIVLKEGRVLAEGD 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-237 |
4.01e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.27 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDlltLKEKT 86
Cdd:COG4152 2 LELKGLTKRF--GDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL-----APDSGEVLWDGEP---LDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHI------RGnriamifqepmtsLNPLHNIEKQInEVLGLHKGLTGKVATQRTLELLELVGILE-PHKRLKalphELS 159
Cdd:COG4152 70 RRRIgylpeeRG-------------LYPKMKVGEQL-VYLARLKGLSKAEAKRRADEWLERLGLGDrANKKVE----ELS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALD-VTVQlkILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVE--LLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
297-514 |
4.10e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGL---AILRliGSKGGIRFEGQQLDrLTQQQVRPLRREMQVVFQDPFG 373
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQnlnGILK--PSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSpRMCVSEIVGEGlrIHKMGTPA-EQEAAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:PRK13636 94 QLF-SASVYQDVSFG--AVNLKLPEdEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 453 SALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
274-473 |
4.23e-26 |
|
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: 105.64 E-value: 4.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFpikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQ 348
Cdd:COG4133 1 MMLEAENLSCRR-----------GERLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILAgllppSAGEVLWNGEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDrltqQQVRPLRREMQVVFQDP--FGSLSPRmcvseivgEGLRIH-KMGTPAEQEAAIIAALKEVGLDPeSRHRYPHEF 425
Cdd:COG4133 66 IR----DAREDYRRRLAYLGHADglKPELTVR--------ENLRFWaALYGLRADREAIDEALEAVGLAG-LADLPVRQL 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAK 473
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR 180
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-505 |
4.73e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.41 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQDLLTLKEKTIRHirgNRIAMIFQEpM 103
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEP----TKGTITINNINYNKLDHKLAAQ---LGIGIIYQE-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 TSLNPLHNIEkqiNEVLGLHkgLTGKV----------ATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALA 173
Cdd:PRK09700 90 SVIDELTVLE---NLYIGRH--LTKKVcgvniidwreMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 174 NEPELLIADEPTTALdvTVQLKILELLKELQARL-GMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLfqSPQHP 252
Cdd:PRK09700 162 LDAKVIIMDEPTSSL--TNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV--SNDDI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 253 YT----QELLAAEPSGGPAT-NVIGPPLLEVDDLkvwfpikkgflrTTVDYvKAVDGINFSLPQGQTLGIVGESGSGKST 327
Cdd:PRK09700 238 VRlmvgRELQNRFNAMKENVsNLAHETVFEVRNV------------TSRDR-KKVRDISFSVCRGEILGFAGLVGSGRTE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 328 LGLAILRLIGSKGG-IRFEGQQLDrlTQQQVRPLRREMQVVFQD-------PFGSLSPRMCVSEIVGEGLRIHKMG--TP 397
Cdd:PRK09700 305 LMNCLFGVDKRAGGeIRLNGKDIS--PRSPLDAVKKGMAYITESrrdngffPNFSIAQNMAISRSLKDGGYKGAMGlfHE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 398 AEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLT 477
Cdd:PRK09700 383 VDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKV 461
|
490 500
....*....|....*....|....*...
gi 799207702 478 YLFISHDLAVVKALSHQLMVVKHGQVVE 505
Cdd:PRK09700 462 ILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-241 |
7.56e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPLarhpSGTINYAGqdlLT 81
Cdd:PRK13632 3 NKSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKS-TISKILTGLLKPQ----SGEIKIDG---IT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHIRGNrIAMIFQEPmtslnplHN------IEKQIneVLGL-HKGLTGKVATQRTLELLELVGILephKRLKAL 154
Cdd:PRK13632 73 ISKENLKEIRKK-IGIIFQNP-------DNqfigatVEDDI--AFGLeNKKVPPKKMKDIIDDLAKKVGME---DYLDKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVrRIAHRVCVMQKG 234
Cdd:PRK13632 140 PQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEG 218
|
....*..
gi 799207702 235 CIVEQAD 241
Cdd:PRK13632 219 KLIAQGK 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-503 |
9.01e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.53 E-value: 9.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTgdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQDLLTLKeK 85
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP-----PDSGTLEIGGNPCARLT-P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGnrIAMIFQEPMtsLNPlhNIEKQINEVLGLHKGltgKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQR 165
Cdd:PRK15439 81 AKAHQLG--IYLVPQEPL--LFP--NLSVKENILFGLPKR---QASMQKMKQLLAALGC---QLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArLGMALLLISHDLNLVRRIAHRVCVMQKGCIV-----EQA 240
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIAlsgktADL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 241 DCETLFQ--SP-----QHPYTQELLAAEPsGGPATNVIGPPLLEVDDLKvwfpiKKGFLRttvdyvkavdgINFSLPQGQ 313
Cdd:PRK15439 228 STDDIIQaiTPaarekSLSASQKLWLELP-GNRRQQAAGAPVLTVEDLT-----GEGFRN-----------ISLEVRAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 314 TLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQL------DRLTQQQVR-PLRREMQVVFQDpfGSLSPRMCvseiv 385
Cdd:PRK15439 291 ILGLAGVVGAGRTELAETLYGLRPARGGrIMLNGKEInalstaQRLARGLVYlPEDRQSSGLYLD--APLAWNVC----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 386 geGLRIHKMG---TPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ 462
Cdd:PRK15439 364 --ALTHNRRGfwiKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARND 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 799207702 463 VVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK15439 442 IYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
299-504 |
1.05e-25 |
|
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: 103.28 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGSKGGIRFEGQQLDRLTQQQVRplRREMQVVFQdpfgsls 376
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTL-MKILsgLYKPDSGEILVDGKEVSFASPRDAR--RAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 prmcvseivgeglrihkmgtpaeqeaaiiaalkevgldpesrhrypheFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 457 RTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:cd03216 115 PAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-271 |
1.06e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.24 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLpYPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:COG3839 4 LELENVSKSY--GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMI-AGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irhiRGnrIAMIFQEP-----MTSLNplhNIEkqinevLGLH-KGLTGKVATQRTLELLELVGIlEPHkrLKALPHELSG 160
Cdd:COG3839 75 ----RN--IAMVFQSYalyphMTVYE---NIA------FPLKlRKVPKAEIDRRVREAAELLGL-EDL--LDRKPKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQA 240
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
250 260 270
....*....|....*....|....*....|.
gi 799207702 241 DCETLFQSPQHPYTQELLaaepsGGPATNVI 271
Cdd:COG3839 217 TPEELYDRPANLFVAGFI-----GSPPMNLL 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
302-529 |
1.20e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQD-----P 371
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTL----LKLLtgeltPSSGEVRLNGRPLAAWSPWE---LARRRAVLPQHsslafP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 FGslsprmcVSEIVGEGLRIHKmGTPAEQEAAIIAALKEVGLDP-ESRHrYPhEFSGGQRQRIAIARALV-------LKP 443
Cdd:COG4559 90 FT-------VEEVVALGRAPHG-SSAAQDRQIVREALALVGLAHlAGRS-YQ-TLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 444 RLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGdaagifaAPQHGYTRQ 523
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG-------TPEEVLTDE 231
|
....*.
gi 799207702 524 LLEAAF 529
Cdd:COG4559 232 LLERVY 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
276-517 |
1.45e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPIKKgflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG--------SKGGIRFEGQ 347
Cdd:PRK13640 6 VEFKHVSFTYPDSK---------KPALNDISFSIPRGSWTALIGHNGSGKST----ISKLINglllpddnPNSKITVDGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QLdrlTQQQVRPLRREMQVVFQDP----FGSlsprmCVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGL----DPEsrh 419
Cdd:PRK13640 73 TL---TAKTVWDIREKVGIVFQNPdnqfVGA-----TVGDDVAFGLENRAVPRPEMIKIVRDV-LADVGMldyiDSE--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 420 ryPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVkALSHQLMVVK 499
Cdd:PRK13640 141 --PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLD 217
|
250
....*....|....*...
gi 799207702 500 HGQVVEQGDAAGIFAAPQ 517
Cdd:PRK13640 218 DGKLLAQGSPVEIFSKVE 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
274-525 |
1.80e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKvwfpikKGFlrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQ 348
Cdd:PRK11607 18 PLLEIRNLT------KSF-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LdrltqQQVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMgtPAEQEAAIIAALKEVGLDPESRHRYPHEFSGG 428
Cdd:PRK11607 83 L-----SHVPPYQRPINMMFQSY--ALFPHMTVEQNIAFGLKQDKL--PKAEIASRVNEMLGLVHMQEFAKRKPHQLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 429 QRQRIAIARALVLKPRLILLDEPTSALDRTV----QRQVVELLRSLQAkynlTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERVGV----TCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
250 260
....*....|....*....|.
gi 799207702 505 EQGDAAGIFAAPQHGYTRQLL 525
Cdd:PRK11607 230 QIGEPEEIYEHPTTRYSAEFI 250
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-237 |
2.07e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHQR--VVNNVSFDIKRGETIALVGESGSGKSVTA-HSILRLLPyplarhPSGTINYAGQDll 80
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAkHMNALLIP------SEGKVYVDGLD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRgNRIAMIFQepmtslNPLHNIEKQINE---VLGLHK-GLTGKVATQRTLELLELVGILEpHKRLKalPH 156
Cdd:PRK13633 74 TSDEENLWDIR-NKAGMVFQ------NPDNQIVATIVEedvAFGPENlGIPPEEIRERVDESLKKVGMYE-YRRHA--PH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCI 236
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
.
gi 799207702 237 V 237
Cdd:PRK13633 223 V 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-512 |
2.23e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFPikkGflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQ 347
Cdd:COG1129 2 EPLLEMRGISKSFG---G--------VKALDGVSLELRPGEVHALLGENGAGKSTL----MKILSgvyqpDSGEILLDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 348 QLDRLTQQQVRplRREMQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGT--PAEQEAAIIAALKEVGL--DPESRHRyph 423
Cdd:COG1129 67 PVRFRSPRDAQ--AAGIAIIHQEL--NLVPNLSVAENIFLGREPRRGGLidWRAMRRRARELLARLGLdiDPDTPVG--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 424 EFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 799207702 504 VEQGDAAGI 512
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-237 |
2.55e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 103.49 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 8 EIRDLSVEFvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLltlKEKTi 87
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKT----TLAKILA-GLIKESSGSILLNGKPI---KAKE- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 88 rhiRGNRIAMIFQEPMTSLnplhnIEKQINEVLGLHKGLTGKVAtQRTLELLELVGILEPHKRLkalPHELSGGQRQRVM 167
Cdd:cd03226 69 ---RRKSIGYVMQDVDYQL-----FTDSVREELLLGLKELDAGN-EQAETVLKDLDLYALKERH---PLSLSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 168 IAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
302-507 |
2.81e-25 |
|
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: 110.22 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGQQLdrltqQQVRP--LRREMQVVFQDPFgslspr 378
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQHGQVLVDGVDL-----AIADPawLRRQMGVVLQENV------ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 mCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHE-------FSGGQRQRIAIARALVLKPRLILLDEP 451
Cdd:TIGR01846 542 -LFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 452 TSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-258 |
3.40e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.68 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 30 SFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYAGQDLLTLKEktirhirGNR-IAMIFQEpm 103
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIagflpPD------SGRILWNGQDLTALPP-------AERpVSMLFQE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 tslnplHN------IEKQINevLGLHKGLT-GKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEP 176
Cdd:COG3840 80 ------NNlfphltVAQNIG--LGLRPGLKlTAEQRAQVEQALERVGL---AGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 177 ELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQE 256
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
..
gi 799207702 257 LL 258
Cdd:COG3840 229 YL 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-250 |
5.84e-25 |
|
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: 103.14 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplARhpSGTINYAGQDLLTLK 83
Cdd:COG0410 1 MPMLEVENLHAGY--GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---PR--SGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 -EKTIRhiRGnrIAM------IFqepmTSLNPLHNIEkqinevLGLHkGLTGKVATQRTLE-LLELVGILEphKRLKALP 155
Cdd:COG0410 72 pHRIAR--LG--IGYvpegrrIF----PSLTVEENLL------LGAY-ARRDRAEVRADLErVYELFPRLK--ERRRQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 HELSGGQRQRVMIAMALANEPELLIADEPTTAL---------DVTVQLkilellkelqARLGMALLLISHDLNLVRRIAH 226
Cdd:COG0410 135 GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLapliveeifEIIRRL----------NREGVTILLVEQNARFALEIAD 204
|
250 260
....*....|....*....|....
gi 799207702 227 RVCVMQKGCIVEQADCETLFQSPQ 250
Cdd:COG0410 205 RAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
293-524 |
6.63e-25 |
|
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: 103.33 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 293 RTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQ-- 369
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAW---LRRQVGVVLQen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 370 --------DPFGSLSPRMCVSEIVgEGLRI---HKMGTPAEQEAAIIAALKEVGLdpesrhryphefSGGQRQRIAIARA 438
Cdd:cd03252 86 vlfnrsirDNIALADPGMSMERVI-EAAKLagaHDFISELPEGYDTIVGEQGAGL------------SGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 439 LVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFAApqH 518
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE--N 227
|
....*.
gi 799207702 519 GYTRQL 524
Cdd:cd03252 228 GLYAYL 233
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
275-499 |
7.04e-25 |
|
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: 102.85 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKvwfpikKGFLRTTVDYVK--AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILR--LIGS-KGGIRFEGQQL 349
Cdd:TIGR02324 1 LLEVEDLS------KTFTLHQQGGVRlpVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnyLPDSgRILVRHEGAWV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 D--RLTQQQVRPLRR-EMQVVFQdpFGSLSPRMCVSEIVGEGLRihKMGTPAEQ-EAAIIAALKEVGLDPESRHRYPHEF 425
Cdd:TIGR02324 75 DlaQASPREVLEVRRkTIGYVSQ--FLRVIPRVSALEVVAEPLL--ERGVPREAaRARARELLARLNIPERLWHLPPATF 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVK 499
Cdd:TIGR02324 151 SGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDVT 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-517 |
8.63e-25 |
|
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: 102.75 E-value: 8.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWfpikkgflrttvdY--VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQL 349
Cdd:COG0410 1 MPMLEVENLHAG-------------YggIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDGEDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DRL-TQQQVR------PLRREMqvvfqdpFGSLSprmcvseiVGEGLRihkMGT-PAEQEAAIIAALKEV-GLDP---ES 417
Cdd:COG0410 68 TGLpPHRIARlgigyvPEGRRI-------FPSLT--------VEENLL---LGAyARRDRAEVRADLERVyELFPrlkER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 418 RHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMV 497
Cdd:COG0410 130 RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYV 208
|
250 260
....*....|....*....|
gi 799207702 498 VKHGQVVEQGDAAGIFAAPQ 517
Cdd:COG0410 209 LERGRIVLEGTAAELLADPE 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-268 |
8.98e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 108.27 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQDLLTLKEK 85
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKP----TSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRGNRIAMIFQE--PMTSLNPLHNIEkqineVLGLHKGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQR 163
Cdd:PRK10535 79 ALAQLRREHFGFIFQRyhLLSHLTAAQNVE-----VPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDlNLVRRIAHRvcvmqkgcIVEQADCE 243
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAER--------VIEIRDGE 220
|
250 260
....*....|....*....|....*
gi 799207702 244 TLFQSPQHPYTQELLAAEPSGGPAT 268
Cdd:PRK10535 221 IVRNPPAQEKVNVAGGTEPVVNTAS 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-523 |
1.12e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 292 LRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQL---DRLTQQQVRPLRREMQVVF 368
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYldgQDIFKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 369 QDPfgSLSPRMCVSEIVGEGLRIHKM-GTPAEQEAAIIAALKEVGLDPESRHRY---PHEFSGGQRQRIAIARALVLKPR 444
Cdd:PRK14247 89 QIP--NPIPNLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 445 LILLDEPTSALDRTVQRQVVELLrsLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQ 523
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
302-490 |
1.22e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.79 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAIL----RLIGSKGGIRFEGQQLDRLTqqqvrPLRREMQVVFQDP--FGSL 375
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgtlsPAFSASGEVLLNGRRLTALP-----AEQRRIGILFQDDllFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SprmcvseiVGEGLRihkMGTPAEQE-----AAIIAALKEVGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:COG4136 92 S--------VGENLA---FALPPTIGraqrrARVEQALEEAGLAGFA-DRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 799207702 451 PTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKA 490
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-256 |
1.54e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhIRgNRIAMIFQEPmtslNPL-HNIEKqiNEVLGLH-KGLTGKVATQRTLEL-LELVGILEPHK-RLKALPHELSGG 161
Cdd:PRK14239 81 TVD-LR-KEIGMVFQQP----NPFpMSIYE--NVVYGLRlKGIKDKQVLDEAVEKsLKGASIWDEVKdRLHDSALGLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMalLLISHDLNLVRRIAHRVCVMQKGCIVEQAD 241
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
250
....*....|....*
gi 799207702 242 CETLFQSPQHPYTQE 256
Cdd:PRK14239 231 TKQMFMNPKHKETED 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
301-505 |
1.59e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQldrltqqqVRPLRREMQVVFQDPfgSL 375
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTL----LNLIAgfvpyQHGSITLDGKP--------VEGPGAERGVVFQNE--GL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQM-LKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 799207702 456 DRTVQRQVVELLRSLQAKYNLTYLFISHDL--AVVKALSHQLMVVKHGQVVE 505
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIeeAVFMATELVLLSPGPGRVVE 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
299-507 |
1.62e-24 |
|
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: 101.51 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEG---QQLDRLTqqqvrpLRREMQVVFQDP--- 371
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGtdiRQLDPAD------LRRNIGYVPQDVtlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 FGSLSPRMCvseivgeglrihkMGTPAEQEAAIIAALKEVGLDPESRhRYPHEF-----------SGGQRQRIAIARALV 440
Cdd:cd03245 91 YGTLRDNIT-------------LGAPLADDERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 441 LKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVkALSHQLMVVKHGQVVEQG 507
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
297-507 |
1.83e-24 |
|
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: 107.11 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTqqqVRPLRREMQVVFQDPF--- 372
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEpDSGQILLDGHDLADYT---LASLRRQVALVSQDVVlfn 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 GSlsprmcVSEIVGEGlRIHKMGTPAEQEAAIIAALKEV------GLDPE-----SRhrypheFSGGQRQRIAIARALVL 441
Cdd:TIGR02203 420 DT------IANNIAYG-RTEQADRAEIERALAAAYAQDFvdklplGLDTPigengVL------LSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
303-526 |
2.17e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.54 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDpfGSLSP 377
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTL----LRLIGgqiapDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 458 TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHgYTRQLLE 526
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQFLD 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-250 |
2.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARH--PSGTINYAGqdlLT 81
Cdd:PRK13640 3 DNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKS----TISKLINGLLLPDdnPNSKITVDG---IT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHIRgNRIAMIFQEPMtslNPLHNIEKQINEVLGLHKGLTGKVATQRTL-ELLELVGILEphkRLKALPHELSG 160
Cdd:PRK13640 74 LTAKTVWDIR-EKVGIVFQNPD---NQFVGATVGDDVAFGLENRAVPRPEMIKIVrDVLADVGMLD---YIDSEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVrRIAHRVCVMQKGCIVEQA 240
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
250
....*....|
gi 799207702 241 DCETLFQSPQ 250
Cdd:PRK13640 226 SPVEIFSKVE 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-243 |
2.79e-24 |
|
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: 106.43 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHQ-RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPlarhPSGTINY-AGQDLLT 81
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE-P----TSGEVNVrVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHiRGNR---IAMIFQEpmTSLNPLHNIEKQINEVLGLHkgLTGKVATQRTLELLELVGILEPHKR--LKALPH 156
Cdd:TIGR03269 352 MTKPGPDG-RGRAkryIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEEKAEeiLDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*..
gi 799207702 237 VEQADCE 243
Cdd:TIGR03269 507 VKIGDPE 513
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
287-508 |
3.08e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.86 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL--GLAILrLIGSKGGIR--FEGQQLDRLTQ-------- 354
Cdd:PRK13651 8 IVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFieHLNAL-LLPDTGTIEwiFKDEKNKKKTKekekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 355 -----------QQVRPLRREMQVVFQDP--------------FGSLSprmcvseivgeglrihkMGTPAEQEAAIIAA-L 408
Cdd:PRK13651 87 lviqktrfkkiKKIKEIRRRVGVVFQFAeyqlfeqtiekdiiFGPVS-----------------MGVSKEEAKKRAAKyI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 409 KEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQaKYNLTYLFISHDLAVV 488
Cdd:PRK13651 150 ELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNV 228
|
250 260
....*....|....*....|
gi 799207702 489 KALSHQLMVVKHGQVVEQGD 508
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGD 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-234 |
3.10e-24 |
|
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: 100.97 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTgdHHQ-----RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQ--- 77
Cdd:COG4778 4 LLEVENLSKTFTL--HLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCI-YGNYLPDSGSILVRHDggw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 78 -DLLTLKEKTIRHIRGNRIAMIFQ---------------EPMtslnplhniekqinevlgLHKGLTGKVATQRTLELLEL 141
Cdd:COG4778 77 vDLAQASPREILALRRRTIGYVSQflrviprvsaldvvaEPL------------------LERGVDREEARARARELLAR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 142 VGILEphkRLKAL-PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNL 220
Cdd:COG4778 139 LNLPE---RLWDLpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEV 214
|
250
....*....|....
gi 799207702 221 VRRIAHRVCVMQKG 234
Cdd:COG4778 215 REAVADRVVDVTPF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
305-523 |
3.86e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQL---DRLTQQQVRPLRREMQVVFQDPfgSLSPRMC 380
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQP--NPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRY---PHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:PRK14246 107 IYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 458 TVQRQVVELLRSLqaKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQHGYTRQ 523
Cdd:PRK14246 187 VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
301-507 |
5.34e-24 |
|
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: 100.14 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTL--GLAILrLIGSKGGIRFEGQQLDRltqqQVRPLRREMQVVFQDPfgSLSPr 378
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTL-LKPTSGRATVAGHDVVR----EPREVRRRIGIVFQDL--SVDD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 mcvsEIVG-EGLRIHK--MGTPAEQEAA-IIAALKEVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:cd03265 87 ----ELTGwENLYIHArlYGVPGAERRErIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 799207702 455 LDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
303-503 |
5.60e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.29 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGSkggirfegqqLDRLTQQQVR----PL---RREMQVVFQDpfGSL 375
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTL----LRLLAG----------LETPSAGELLagtaPLaeaREDTRLMFQD--ARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SPRMCVSEIVGEGLRIHkmgtpaeQEAAIIAALKEVGLdpESR-HRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQ-------WRDAALQALAAVGL--ADRaNEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207702 455 LDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-239 |
6.26e-24 |
|
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: 99.66 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL-PYplarhpSGTINYAGQDLLTLKEK 85
Cdd:cd03269 1 LEVENVTKRF--GRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPD------SGEVLFDGKPLDIAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHI---RGNRIAMIFQEPMTSLNPLhniekqinevlglhKGLTGKVATQRTLELLELVGILEphKRLKALpHELSGGQ 162
Cdd:cd03269 71 RIGYLpeeRGLYPKMKVIDQLVYLAQL--------------KGLKKEEARRRIDEWLERLELSE--YANKRV-EELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDVtVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
266-513 |
7.72e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 266 PATNVIGPPLLEVDDLKVWFPIKkgflrtTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG---- 341
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEK------QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 342 --------IRFEGQQLDRLTQQ--QVRPLRREMQVVFQDPFGSLSPRMCVSEIV-GE-GLRIHKmgtpAEQEAAIIAALK 409
Cdd:PRK13631 86 gdiyigdkKNNHELITNPYSKKikNFKELRRRVSMVFQFPEYQLFKDTIEKDIMfGPvALGVKK----SEAKKLAKFYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 410 EVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVK 489
Cdd:PRK13631 162 KMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVL 240
|
250 260
....*....|....*....|....
gi 799207702 490 ALSHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK13631 241 EVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-241 |
8.19e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 8.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTG-DHHQRVVNNVSFDIKRGETIALVGESGSGKSV-TAHSILRLLPyplarhPSGTINYAGQDLLTLKE 84
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLNALLLP------DTGTIEWIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 ---------------------KTIRHIRgNRIAMIFQEPMTSLNPlHNIEKQIneVLG-LHKGLTGKVATQRTLELLELV 142
Cdd:PRK13651 77 tkekekvleklviqktrfkkiKKIKEIR-RRVGVVFQFAEYQLFE-QTIEKDI--IFGpVSMGVSKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 143 GIlePHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQArlGMALLLISHDLNLV 221
Cdd:PRK13651 153 GL--DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQ--GKTIILVTHDLDNV 228
|
250 260
....*....|....*....|
gi 799207702 222 RRIAHRVCVMQKGCIVEQAD 241
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGD 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-250 |
8.26e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 8.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKS-VTAHSILRLLPyplarhPSGTINYAGQDL-LTLKEKTIRHIRgNRIAMIFQEPM 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKStLMQHFNALLKP------SSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 TSL---NPLHNIEkqinevLG-LHKGLTGKVATQRTLELLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PRK13641 96 AQLfenTVLKDVE------FGpKNFGFSEDEAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 180 IADEPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQ 250
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
255-497 |
8.83e-24 |
|
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: 104.68 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 255 QELLAAE--PSGGPATNVIGPPL-LEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLA 331
Cdd:TIGR02857 298 FAVLDAAprPLAGKAPVTAAPASsLEFSGVSVAYP----------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 332 ILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPFgslsprmCVSEIVGEGLRihkMGTPAEQEAAIIAALKE 410
Cdd:TIGR02857 368 LLGFVDPTEGsIAVNGVPLADADADS---WRDQIAWVPQHPF-------LFAGTIAENIR---LARPDASDAEIREALER 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 411 VGLD------PESRHR----YPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLF 480
Cdd:TIGR02857 435 AGLDefvaalPQGLDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLL 512
|
250
....*....|....*..
gi 799207702 481 ISHDLAVVKALSHQLMV 497
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
308-507 |
1.03e-23 |
|
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: 99.10 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 308 SLPQGQTLGIVGESGSGKSTLglaiLRLIGSkggirFEGQQLDRLTQQQV-----RPLRREMQVVFQDpfGSLSPRMCVS 382
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTL----LNLIAG-----FETPQSGRVLINGVdvtaaPPADRPVSMLFQE--NNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGLRIHKMGTPAEQEAAIIAaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ 462
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDRQAIEVA-LARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 799207702 463 VVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
299-516 |
1.16e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGQQLdrlTQQQVRPLRREMQVVFQDPFG 373
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLfrhfnGI----LKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SL-SPrmCVSEIVGEGlRIHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:PRK13652 90 QIfSP--TVEQDIAFG-PINLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 453 SALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-260 |
1.26e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYAGQDLL 80
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALsgelsPD------SGEVRLNGRPLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKektiRHIRGNRIAMIFQEpmTSLN-PLhniekQINEV--LGLHKGLTGKVATQRTL-ELLELVGILEPHKRLKalpH 156
Cdd:PRK13548 68 DWS----PAELARRRAVLPQH--SSLSfPF-----TVEEVvaMGRAPHGLSRAEDDALVaAALAQVDLAHLAGRDY---P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALA------NEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCV 230
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
250 260 270
....*....|....*....|....*....|
gi 799207702 231 MQKGCIVEQAdcetlfqSPQHPYTQELLAA 260
Cdd:PRK13548 214 LHQGRLVADG-------TPAEVLTPETLRR 236
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-245 |
1.35e-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: 105.04 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRdlSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL---PYPLarhpSGTINYAGQDLLTLK 83
Cdd:TIGR03797 452 IEVD--RVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKS----TLLRLLlgfETPE----SGSVFYDGQDLAGLD 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRhirgnriamifqepmtslnplhnieKQINEVLGLHKGLTGKV------ATQRTL----ELLELVGILEPhkrLKA 153
Cdd:TIGR03797 522 VQAVR-------------------------RQLGVVLQNGRLMSGSIfeniagGAPLTLdeawEAARMAGLAED---IRA 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 LP---H--------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLkelqARLGMALLLISHDLNLVR 222
Cdd:TIGR03797 574 MPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIR 649
|
250 260
....*....|....*....|...
gi 799207702 223 RiAHRVCVMQKGCIVEQADCETL 245
Cdd:TIGR03797 650 N-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-237 |
1.49e-23 |
|
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: 97.11 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvTAHSILrllpYPLARHPSGTINYAGQDLLTLkekT 86
Cdd:cd03216 1 LELRGITKRF--GGVK--ALDGVSLSVRRGEVHALLGENGAGKS-TLMKIL----SGLYKPDSGEILVDGKEVSFA---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQepmtslnplhniekqinevlglhkgltgkvatqrtlellelvgilephkrlkalpheLSGGQRQRV 166
Cdd:cd03216 69 PRDARRAGIAMVYQ---------------------------------------------------------LSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-350 |
1.51e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 103.72 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEF--VtgdhhqRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRllpyplARHPSGTinYAGQDLLTLK 83
Cdd:NF040905 1 ILEMRGITKTFpgV------KALDDVNLSVREGEIHALCGENGAGKS-TLMKVLS------GVYPHGS--YEGEILFDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRHIRGNR---IAMIFQEpmTSLNPLHNIEKQI---NEVLglHKGLTGKVAT-QRTLELLELVGILE-PHKRLKalp 155
Cdd:NF040905 66 VCRFKDIRDSEalgIVIIHQE--LALIPYLSIAENIflgNERA--KRGVIDWNETnRRARELLAKVGLDEsPDTLVT--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 hELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGC 235
Cdd:NF040905 139 -DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 236 IVEQADCETlfqspqHPYTQ----------ELLAAEPsggPATNVIGPPLLEVDDLKVWFPIKKGflRttvdyvKAVDGI 305
Cdd:NF040905 217 TIETLDCRA------DEVTEdriirgmvgrDLEDRYP---ERTPKIGEVVFEVKNWTVYHPLHPE--R------KVVDDV 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 799207702 306 NFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSK--GGIRFEGQQLD 350
Cdd:NF040905 280 SLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNisGTVFKDGKEVD 327
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
296-517 |
1.71e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 296 VDYV---------KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGQQLDRLT-QQQVRPL 360
Cdd:PRK13641 8 VDYIyspgtpmekKGLDNISFELEEGSFVALVGHTGSGKSTLmqhfnAL----LKPSSGTITIAGYHITPETgNKNLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 361 RREMQVVFQDPFGSLSPRMcVSEIVGEGLRihKMG-TPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARAL 439
Cdd:PRK13641 84 RKKVSLVFQFPEAQLFENT-VLKDVEFGPK--NFGfSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 440 VLKPRLILLDEPTSALDRTVQRQVVELLRSLQaKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-517 |
2.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGL---AILRliGSKGGIRFEGQQLDr 351
Cdd:PRK13639 1 ILETRDLKYSYP----------DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLhfnGILK--PTSGEVLIKGEPIK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 352 LTQQQVRPLRREMQVVFQDPFGSL-SPRmcVSEIVGEGLRihKMGTPAEQEAAIIA-ALKEVGLDPESRhRYPHEFSGGQ 429
Cdd:PRK13639 68 YDKKSLLEVRKTVGIVFQNPDDQLfAPT--VEEDVAFGPL--NLGLSKEEVEKRVKeALKAVGMEGFEN-KPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 430 RQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQaKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDA 509
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*...
gi 799207702 510 AGIFAAPQ 517
Cdd:PRK13639 222 KEVFSDIE 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-239 |
2.05e-23 |
|
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: 98.10 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLPyPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03301 1 VELENVTKRF--GNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIA-GLEEPTSGRIYIGGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irhiRGnrIAMIFQEpmTSLNPLHNIEKQINEVLGLHKgLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQRQRV 166
Cdd:cd03301 72 ----RD--IAMVFQN--YALYPHMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQIEH---LLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGcIVEQ 239
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG-QIQQ 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
300-507 |
2.74e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.03 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTlGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRltqqQVRPLRREMQVVFQDPfgS 374
Cdd:cd03264 14 RALDGVSLTLGPGMY-GLLGPNGAGKTTL----MRILAtltppSSGTIRIDGQDVLK----QPQKLRRRIGYLPQEF--G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSPRMCVSEIVGEGLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:cd03264 83 VYPNFTVREFLDYIAWLKGI-PSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 455 LDrTVQRQVV-ELLRSLQAkyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03264 161 LD-PEERIRFrNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-234 |
3.41e-23 |
|
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: 97.96 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQDLLTlkekT 86
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLTGELRP----TSGTAYINGYSIRT----D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNrIAMIFQEPM--TSLNPLHNIEkqineVLGLHKGLTGKVATQRTLELLELVGiLEPHKRLKAlpHELSGGQRQ 164
Cdd:cd03263 70 RKAARQS-LGYCPQFDAlfDELTVREHLR-----FYARLKGLPKSEIKEEVELLLRVLG-LTDKANKRA--RTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDV--------TVQlkilellkelQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPasrraiwdLIL----------EVRKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
302-501 |
4.20e-23 |
|
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: 97.92 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRltqqqvrPLRREMqVVFQDPfgSLS 376
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTL----LNLISglaqpTSGGVILEGKQITE-------PGPDRM-VVFQNY--SLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRMCVSEIVGEGLR--IHKMGTPAEQEAAIIAaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:TIGR01184 67 PWLTVRENIALAVDrvLPDLSKSERRAIVEEH-IALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 455 LDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHG 501
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-250 |
4.50e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYaGQDLLT--LKEKTIRHIRgNRIAMIFQ 100
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKS----TLLQHLN-GLLQPTSGTVTI-GERVITagKKNKKLKPLR-KKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPMTSLNPlHNIEKQIneVLG-LHKGLTGKVATQRTLELLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PRK13634 93 FPEHQLFE-ETVEKDI--CFGpMNFGVSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 180 IADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQ 250
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
299-515 |
5.48e-23 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 102.47 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLdrltqQQVRP--LRREMQVVFQDP---F 372
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDpQSGRILLDGVDL-----RQLDPaeLRARMALVPQDPvlfA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 GSlsprmcvseiVGEGLRihkMGTPAEQEAAIIAALKEVGLD------PESRHRYPHE----FSGGQRQRIAIARALVLK 442
Cdd:TIGR02204 428 AS----------VMENIR---YGRPDATDEEVEAAARAAHAHefisalPEGYDTYLGErgvtLSGGQRQRIAIARAILKD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 443 PRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFAA 515
Cdd:TIGR02204 495 APILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-258 |
5.54e-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: 99.88 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 41 LVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLlTLKEKTIRHIrgnriAMIFQEpmTSLNPLHNIEKQIneVL 120
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLA-GFEQPDSGSIMLDGEDV-TNVPPHLRHI-----NMVFQS--YALFPHMTVEENV--AF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 121 GLH-KGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILEL 199
Cdd:TIGR01187 66 GLKmRKVPRAEIKPRVLEALRLVQLEEFADRK---PHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 200 LKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQELL 258
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-248 |
6.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.70 E-value: 6.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYagqDLLTL----KEKTIRHIRgNRIAMIFQE 101
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL-----KPTTGTVTV---DDITIthktKDKYIRPVR-KRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMTSLNPlHNIEKQIneVLGLHK-GLTGKVATQRTLELLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK13646 94 PESQLFE-DTVEREI--IFGPKNfKMNLDEVKNYAHRLLMDLGF--SRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 181 ADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQS 248
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-507 |
7.25e-23 |
|
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: 97.05 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKGflrttvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGqqL 349
Cdd:cd03266 1 MITADALTKRFRDVKK-------TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDG--F 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DrlTQQQVRPLRREMQVVFqDPFGsLSPRMCVSEIVGEGLRIHKM-GTPAEQEAAIIAALKEVGldpESRHRYPHEFSGG 428
Cdd:cd03266 68 D--VVKEPAEARRRLGFVS-DSTG-LYDRLTARENLEYFAGLYGLkGDELTARLEELADRLGME---ELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 429 QRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
287-504 |
9.51e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 9.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQqvrplR 361
Cdd:COG1101 7 LSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAIAgslppDSGSILIDGKDVTKLPEY-----K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 362 REMQV--VFQDPFGSLSPRMCVSEIV------GE--GLRIhkmGTPAEQEAAIIAALKEVGLDPESRHRYPHEF-SGGQR 430
Cdd:COG1101 78 RAKYIgrVFQDPMMGTAPSMTIEENLalayrrGKrrGLRR---GLTKKRRELFRELLATLGLGLENRLDTKVGLlSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 431 QRIAIARALVLKPRLILLDEPTSALD-RTVQrQVVELLRSLQAKYNLTYLFISHDLAvvKALSH--QLMVVKHGQVV 504
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpKTAA-LVLELTEKIVEENNLTTLMVTHNME--QALDYgnRLIMMHEGRII 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
303-507 |
1.25e-22 |
|
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: 101.82 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDP---------- 371
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDvTSGRILIDGQDIRDVTQAS---LRAAIGIVPQDTvlfndtiayn 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 --FGSLSPRMcvSEI--VGEGLRIHK--MGTPAEQEAAiiaaLKEVGLdpesrhryphEFSGGQRQRIAIARALVLKPRL 445
Cdd:COG5265 452 iaYGRPDASE--EEVeaAARAAQIHDfiESLPDGYDTR----VGERGL----------KLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 446 ILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLA-VVKAlsHQLMVVKHGQVVEQG 507
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
300-507 |
1.64e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 95.75 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQqqvrPLRReMQVVFQDP--FGSLS 376
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeITFDGKSYQKNIE----ALRR-IGALIEAPgfYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRmcvseivgEGLRIHKMGtPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:cd03268 89 AR--------ENLRLLARL-LGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 799207702 457 RTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03268 159 PDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
304-514 |
1.69e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.39 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDrLTQQQVRPLRREMQVVFQDPFGSLSPRMCVS 382
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQIFYTDIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIvgeGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ 462
Cdd:PRK13638 98 DI---AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 799207702 463 VVELLRSLQAKYNLTyLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:PRK13638 175 MIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
273-532 |
1.72e-22 |
|
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: 96.69 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFpikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG------SKGGIRFEG 346
Cdd:COG1119 1 DPLLELRNVTVRR-----------GGKTILDDISWTVKPGEHWAILGPNGAGKSTL----LSLITgdlpptYGNDVRLFG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 347 QQLDRLTqqqVRPLRREMQVVFQDPFGSLSPRMCVSEIVGEGL----RIHKMGTPAEQEAAIIAaLKEVGLDPESRHRYp 422
Cdd:COG1119 66 ERRGGED---VWELRKRIGLVSPALQLRFPRDETVLDVVLSGFfdsiGLYREPTDEQRERAREL-LELLGLAHLADRPF- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 423 HEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLA-VVKALSHQLMvVKHG 501
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLL-LKDG 219
|
250 260 270
....*....|....*....|....*....|.
gi 799207702 502 QVVEQGDAAGIFaapqhgyTRQLLEAAFLVP 532
Cdd:COG1119 220 RVVAAGPKEEVL-------TSENLSEAFGLP 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
300-504 |
1.89e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.71 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDP--- 371
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTL----LKLIcgierPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 -----FGSLSPRMCVSEIVGEGLRihkmgtpaeqeAAIIAALKEVGLDPESRHrYPHEFSGGQRQRIAIARALVLKPRLI 446
Cdd:PRK10908 92 mdrtvYDNVAIPLIIAGASGDDIR-----------RRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 447 LLDEPTSALDRTVQRQVVELLRSLQaKYNLTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
297-519 |
2.06e-22 |
|
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: 101.10 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEG---QQLDRLTqqqvrpLRREMQVVFQDP- 371
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQpTEGSVLLDGvdiRQIDPAD------LRRNIGYVPQDPr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 --FGSLSPRMCvseivgeglrihkMGTPAEQEAAIIAALKEVGLDPESRhRYPHEF-----------SGGQRQRIAIARA 438
Cdd:TIGR03375 550 lfYGTLRDNIA-------------LGAPYADDEEILRAAELAGVTEFVR-RHPDGLdmqigergrslSGGQRQAVALARA 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 439 LVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKynLTYLFISHDLAVVKaLSHQLMVVKHGQVVEQGDAAGIFAAPQH 518
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLEALRK 692
|
.
gi 799207702 519 G 519
Cdd:TIGR03375 693 G 693
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
304-507 |
2.36e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQqldRLTQQQVRPLRREMQVVFQDPfgsLSPRMCVS 382
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGqVLLDGV---PLVQYDHHYLHRQVALVGQEP---VLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGLRIHKMgtpaeqeAAIIAALKEVGLDP---ESRHRYPHE-------FSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:TIGR00958 573 ENIAYGLTDTPD-------EEIMAAAKAANAHDfimEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 453 SALDRTVQRqvveLLRSLQAKYNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-245 |
2.39e-22 |
|
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: 95.76 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDlsVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLArhpSGTINYAGQDLLTLKE 84
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPrfYDVD---SGRILIDGHDVRDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KTIRhirgNRIAMIFQEPMTSLNPLHNiekqiNEVLGLHKgltgkvATQRtlELLELVGILEPHKRLKALPH-------- 156
Cdd:cd03251 72 ASLR----RQIGLVSQDVFLFNDTVAE-----NIAYGRPG------ATRE--EVEEAARAANAHEFIMELPEgydtvige 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ---ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVRRiAHRVCVMQK 233
Cdd:cd03251 135 rgvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLED 211
|
250
....*....|..
gi 799207702 234 GCIVEQADCETL 245
Cdd:cd03251 212 GKIVERGTHEEL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
273-512 |
2.40e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.39 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDlkvwfpIKKGFlrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI---GS-KGGIRFEGQQ 348
Cdd:PRK13549 3 EYLLEMKN------ITKTF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVyphGTyEGEIIFEGEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LdrlTQQQVRPLRRE-MQVVFQDPfgSLSPRMCVSEIVGEGLRIHKMGTP--AEQEAAIIAALKEVGLD--PESRHRyph 423
Cdd:PRK13549 71 L---QASNIRDTERAgIAIIHQEL--ALVKELSVLENIFLGNEITPGGIMdyDAMYLRAQKLLAQLKLDinPATPVG--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 424 EFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRH 221
|
....*....
gi 799207702 504 VEQGDAAGI 512
Cdd:PRK13549 222 IGTRPAAGM 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
297-507 |
2.51e-22 |
|
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: 95.26 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGSKGGIRFEGQQLDRltqqQVRPLRREMQVVFQDP--F 372
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtgELRPTSGTAYINGYSIRT----DRKAARQSLGYCPQFDalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 GSLSPRmcvseivgEGLRIHKM--GTPAEQE-AAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLD 449
Cdd:cd03263 88 DELTVR--------EHLRFYARlkGLPKSEIkEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 450 EPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-281 |
2.58e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.61 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHQ-RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTIN----YAGQD 78
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI-----KSKYGTIQvgdiYIGDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 79 L---------LTLKEKTIRHIRgNRIAMIFQEPMTSLNPlHNIEKQIN---EVLGLHKgltgKVATQRTLELLELVGILE 146
Cdd:PRK13631 94 KnnhelitnpYSKKIKNFKELR-RRVSMVFQFPEYQLFK-DTIEKDIMfgpVALGVKK----SEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 147 PHkrLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAH 226
Cdd:PRK13631 168 SY--LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVAD 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 227 RVCVMQKGCIVEQADCETLFqspqhpYTQELLAaepsggpATNVIGPPLLEV-DDL 281
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEIF------TDQHIIN-------STSIQVPRVIQViNDL 287
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-255 |
2.79e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.95 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplarHPS-GTINYAGQDLLTLKEKTIRHIRGNRIAMIFQepmt 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI------EPTrGQVLIDGVDIAKISDAELREVRRKKIAMVFQ---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLNPLHNIEKQINEVLGLH-KGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMElAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 184 PTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQ 255
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-239 |
3.21e-22 |
|
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: 95.37 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLL-FRFYDVSSGSILIDGQDIREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEpmTSL---NPLHNIEkqinevlglhkglTGKV-ATQRtlELLELVGILEPHKRLKALPH------ 156
Cdd:cd03253 73 LR----RAIGVVPQD--TVLfndTIGYNIR-------------YGRPdATDE--EVIEAAKAAQIHDKIMRFPDgydtiv 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 -----ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL-----GMALLLISHDLNLVRRiAH 226
Cdd:cd03253 132 gerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE-------REIQAALrdvskGRTTIVIAHRLSTIVN-AD 203
|
250
....*....|...
gi 799207702 227 RVCVMQKGCIVEQ 239
Cdd:cd03253 204 KIIVLKDGRIVER 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-249 |
3.60e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLl 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRF--GSN--TVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLVA-GLEKPTEGQIFIDGEDV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 tlkekTIRHIRGNRIAMIFQE----PMTSLNplHNIEkqinevLGLH-KGLTGKVATQRTLELLELVGILEPHKRLKalp 155
Cdd:PRK11432 71 -----THRSIQQRDICMVFQSyalfPHMSLG--ENVG------YGLKmLGVPKEERKQRVKEALELVDLAGFEDRYV--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGC 235
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
250
....*....|....
gi 799207702 236 IVEQADCETLFQSP 249
Cdd:PRK11432 215 IMQIGSPQELYRQP 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-248 |
4.08e-22 |
|
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: 95.25 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQDLLTLKEKTIRHirgnRIAMIFQEpmt 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV-----PENGRVLVDGHDLALADPAWLRR----QVGVVLQE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 slNPLHNieKQINEVLGLhkGLTGkVATQRTLELLELVGilePHKRLKALPH-----------ELSGGQRQRVMIAMALA 173
Cdd:cd03252 85 --NVLFN--RSIRDNIAL--ADPG-MSMERVIEAAKLAG---AHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 174 NEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQADCETLFQS 248
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
301-537 |
4.90e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL-RLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPfgslspr 378
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTL-INLLqRVFDPQSGrILIDGTDIRTVTRAS---LRRNIAVVFQDA------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIhkmGTPAEQEAAIIAAL-----------KEVGLDPESRHRyPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:PRK13657 419 GLFNRSIEDNIRV---GRPDATDEEMRAAAeraqahdfierKPDGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLqaKYNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG------DAAGIFAApqhgyt 521
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGsfdelvARGGRFAA------ 565
|
250
....*....|....*.
gi 799207702 522 rqLLEAAFLVPAARVD 537
Cdd:PRK13657 566 --LLRAQGMLQEDERR 579
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
306-508 |
5.59e-22 |
|
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: 94.16 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 306 NFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTqqqvrPLRREMQVVFQDpfGSLSPRMC 380
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTL----LNLIAgfiepASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRiHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:TIGR01277 87 VRQNIGLGLH-PGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 461 RQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGD 508
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-248 |
6.12e-22 |
|
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: 94.60 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03254 3 IEFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-----PQKGQILIDGIDIRDISRKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEP-MTSLNPLHNIEkqinevlglhkgLTGKVATQ-RTLELLELVGIlepHKRLKALP--------- 155
Cdd:cd03254 75 LR----SMIGVVLQDTfLFSGTIMENIR------------LGRPNATDeEVIEAAKEAGA---HDFIMKLPngydtvlge 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 --HELSGGQRQRVMIAMALANEPELLIADEPTTALDV----TVQLKILELlkelqaRLGMALLLISHDLNLVRRiAHRVC 229
Cdd:cd03254 136 ngGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTetekLIQEALEKL------MKGRTSIIIAHRLSTIKN-ADKIL 208
|
250
....*....|....*....
gi 799207702 230 VMQKGCIVEQADCETLFQS 248
Cdd:cd03254 209 VLDDGKIIEEGTHDELLAK 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-260 |
6.34e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYAGQDLL 80
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRgnriAMIFQEpmTSLN-PLHniekqINEV--LGLHKGLTGKVATQR-TLELLELVGILEPHKRLKalpH 156
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFT-----VEEVvaLGRAPHGSSAAQDRQiVREALALVGLAHLAGRSY---Q 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALA-------NEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVC 229
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRIL 211
|
250 260 270
....*....|....*....|....*....|.
gi 799207702 230 VMQKGCIVEQAdcetlfqSPQHPYTQELLAA 260
Cdd:COG4559 212 LLHQGRLVAQG-------TPEEVLTDELLER 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-526 |
6.62e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQdpfgs 374
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdpQQGEILLNGQPIADYSEAA---LRQAISVVSQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 lsprmcvseivgeglRIH----------KMGTPAEQEAAIIAALKEVGL-----DPESRHRYPHE----FSGGQRQRIAI 435
Cdd:PRK11160 422 ---------------RVHlfsatlrdnlLLAAPNASDEALIEVLQQVGLeklleDDKGLNAWLGEggrqLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 436 ARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLavvKALSH--QLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL---TGLEQfdRICVMDNGQIIEQGTHQELL 561
|
250
....*....|...
gi 799207702 514 AapQHGYTRQLLE 526
Cdd:PRK11160 562 A--QQGRYYQLKQ 572
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-240 |
6.67e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.82 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI-----KPDSGEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irhirgNRIAMIFQEPmtSLNPLHNIEKQInEVLGLHKGLtGKVATQRTLELLELVGilEPHKRLKALphelSGGQRQRV 166
Cdd:cd03268 72 ------RRIGALIEAP--GFYPNLTARENL-RLLARLLGI-RKKRIDEVLDVVGLKD--SAKKKVKGF----SLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 167 MIAMALANEPELLIADEPTTALDvTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQA 240
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLD-PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
6.88e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFVTGDHhqrVVNNVSFDIKRGETIALVGESGSGKSVtahsilrllpypLARHPSGTINYAGQDLLTLKE 84
Cdd:PRK13652 2 HLIETRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKST------------LFRHFNGILKPTSGSVLIRGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 ----KTIRHIRgNRIAMIFQEPMTSL-NPlhNIEKQIneVLG-LHKGLTGKVATQRTLELLELVGILEPHKRLkalPHEL 158
Cdd:PRK13652 67 pitkENIREVR-KFVGLVFQNPDDQIfSP--TVEQDI--AFGpINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVE 238
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
250
....*....|.
gi 799207702 239 QADCETLFQSP 249
Cdd:PRK13652 219 YGTVEEIFLQP 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-527 |
8.02e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GSLsprmcv 381
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPES---WRKHLSWVGQNPQlphGTL------ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 382 seivGEGLRihkMGTPAEQEAAIIAALKEVGLD---PESRHRYPHE-------FSGGQRQRIAIARALVLKPRLILLDEP 451
Cdd:PRK11174 440 ----RDNVL---LGNPDASDEQLQQALENAWVSeflPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 452 TSALDRTVQRQVVELLRslQAKYNLTYLFISHDLAVVKALShQLMVVKHGQVVEQGDAAGIfaAPQHGYTRQLLEA 527
Cdd:PRK11174 513 TASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQWD-QIWVMQDGQIVQQGDYAEL--SQAGGLFATLLAH 583
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
1.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 3 QDNLIEIRDLSVEFVTGDHhqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLlTL 82
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL-----KPSSGRILFDGKPI-DY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 KEKTIRHIRGNrIAMIFQEPMTSLNPLHNIEKQINEVLGLhkGLTGKVATQRTLELLELVGIlephKRLKALP-HELSGG 161
Cdd:PRK13636 73 SRKGLMKLRES-VGMVFQDPDNQLFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQAD 241
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*
gi 799207702 242 CETLF 246
Cdd:PRK13636 226 PKEVF 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
295-512 |
1.25e-21 |
|
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: 97.97 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 295 TVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI---GS-KGGIRFEGQQLdrlTQQQVRPLRREMQVVFQD 370
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVyphGTwDGEIYWSGSPL---KASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 PFgSLSPRMCV-------SEIVGEGLRIHKmgtpAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKP 443
Cdd:TIGR02633 86 EL-TLVPELSVaeniflgNEITLPGGRMAY----NAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 444 RLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGI 512
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-258 |
1.26e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLLTLKEKTIrhirGNRIAMIFQEP 102
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT-PQ----SGTVFLGDKPISMLSSRQL----ARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 MT----SLNPLhnIEKQINEVLGLHKGLTGK------VATQRTlELLELVgilepHKRLKalphELSGGQRQRVMIAMAL 172
Cdd:PRK11231 86 LTpegiTVREL--VAYGRSPWLSLWGRLSAEdnarvnQAMEQT-RINHLA-----DRRLT----DLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 173 ANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQAdcetlfqSPQHP 252
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEV 225
|
....*.
gi 799207702 253 YTQELL 258
Cdd:PRK11231 226 MTPGLL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-245 |
1.29e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 30 SFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHpSGTINYAGQDlltlkektirHIR---GNR-IAMIFQEpmTS 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGFLTPA-SGSLTLNGQD----------HTTtppSRRpVSMLFQE--NN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 LNPLHNIEKQINevLGLHKGLTGKVATQRTLE-LLELVGILEPHKRLkalPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:PRK10771 82 LFSHLTVAQNIG--LGLNPGLKLNAAQREKLHaIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 185 TTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
299-506 |
2.23e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDrltqqQVRPLRREMQVVFQDPfg 373
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVAgleriTSGEIWIGGRVVN-----ELEPADRDIAMVFQNY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAAlKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK11650 86 ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAA-RILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 454 ALDRTVQRQV-VElLRSLQAKYNLTYLFISHDLavVKA--LSHQLMVVKHGqVVEQ 506
Cdd:PRK11650 164 NLDAKLRVQMrLE-IQRLHRRLKTTSLYVTHDQ--VEAmtLADRVVVMNGG-VAEQ 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-249 |
2.23e-21 |
|
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: 95.55 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTlKEKTIR---HIRgnRIAMIFQEPmt 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKT----TLLRAIA-GLERPDSGRIRLGGEVLQD-SARGIFlppHRR--RIGYVFQEA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLNPLHNIEKqiNevlgLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:COG4148 87 RLFPHLSVRG--N----LLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 185 TTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSP 249
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
255-485 |
2.89e-21 |
|
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: 97.05 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 255 QELLAAEPSG-GPATNVIGPPLLEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL 333
Cdd:TIGR02868 313 AAGPVAEGSApAAGAVGLGKPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 334 RLIGSKGG-IRFEGQQLDRLTQQQVRplrREMQVVFQDP--FGSlsprmcvseIVGEGLRIhkmGTPAEQEAAIIAALKE 410
Cdd:TIGR02868 383 GLLDPLQGeVTLDGVPVSSLDQDEVR---RRVSVCAQDAhlFDT---------TVRENLRL---ARPDATDEELWAALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 411 VGLD------PESRHRYPHE----FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLrsLQAKYNLTYLF 480
Cdd:TIGR02868 448 VGLAdwlralPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVL 525
|
....*
gi 799207702 481 ISHDL 485
Cdd:TIGR02868 526 ITHHL 530
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
304-484 |
4.58e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.15 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLgLAILRLI--GSKGGIRFEGQQLDRLTQQQVRPLR-REMQVVFQDPFgsLSPRMC 380
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTL-LAILAGLddGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFM--LIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIV-------GEGLRIHKMGTpaeqeaaiIAALKEVGLDPESRHrYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK10584 105 ALENVelpallrGESSRQSRNGA--------KALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHD 484
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-256 |
4.93e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLP-YPLARHPSGTINYAGQDLLTLKEKTIRhirgNRIAMIFQEPm 103
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 tslNPLHNIEKQINEVLGLHK-GLTGKVATQRTLE-LLELVGIL-EPHKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK14246 100 ---NPFPHLSIYDNIAYPLKShGIKEKREIKKIVEeCLRKVGLWkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 181 ADEPTTALDVTvqLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQE 256
Cdd:PRK14246 177 MDEPTSMIDIV--NSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-217 |
5.77e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.62 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLArhPSgtinyAGQdlLTLKEKT 86
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIAGFLA--PS-----SGE--ITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRiAMIFQEP--MTSLNPLHNIEkqinevLGLH-KGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGGQR 163
Cdd:COG4525 71 VTGPGADR-GVVFQKDalLPWLNVLDNVA------FGLRlRGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHD 217
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-190 |
5.94e-21 |
|
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: 91.00 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:COG4133 2 MLEAENLSCRR--GER--LLFSGLSFTLAAGEALALTGPNGSGKT----TLLRIL-AGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIrgnriAMIFQEPM--TSLNPLHNiekqinevLGLHKGLTGKVATQRTL-ELLELVGiLEPHKRLKAlpHELSGGQ 162
Cdd:COG4133 73 YRRRL-----AYLGHADGlkPELTVREN--------LRFWAALYGLRADREAIdEALEAVG-LAGLADLPV--RQLSAGQ 136
|
170 180
....*....|....*....|....*...
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDA 164
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-260 |
6.92e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQDLLTLKEK 85
Cdd:PRK13657 334 AVEFDDVSFSY---DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDP----QSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHirgnRIAMIFQEPMtslnpLHNieKQINEVLGLhkgltGKV-ATQRtlELLELVGILEPHKRLKALPH-------- 156
Cdd:PRK13657 406 SLRR----NIAVVFQDAG-----LFN--RSIEDNIRV-----GRPdATDE--EMRAAAERAQAHDFIERKPDgydtvvge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ---ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVqlkilellkelQARLGMAL---------LLISHDLNLVRRi 224
Cdd:PRK13657 468 rgrQLSGGERQRLAIARALLKDPPILILDEATSALDVET-----------EAKVKAALdelmkgrttFIIAHRLSTVRN- 535
|
250 260 270
....*....|....*....|....*....|....*.
gi 799207702 225 AHRVCVMQKGCIVEQADCETLFQSPQHPYtqELLAA 260
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVARGGRFA--ALLRA 569
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
297-516 |
9.37e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGqqLDRLTQQQVRPLRREMQVVFQDPFGSL 375
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SPRMCVSEIV--GEGLRIhkmgTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK13644 91 VGRTVEEDLAfgPENLCL----PPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 454 ALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-236 |
9.96e-21 |
|
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: 90.99 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHQrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLlpYPLArhpSGTINYAGQDLLTLK 83
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF--YQPQ---GGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRhirgNRIAMIFQEPMTSLNPLHNiekqiNEVLGLHKGLTGKVatqrtlelLELVGILEPHKRLKALPHE------ 157
Cdd:cd03248 83 HKYLH----SKVSLVGQEPVLFARSLQD-----NIAYGLQSCSFECV--------KEAAQKAHAHSFISELASGydtevg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 -----LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlgMALLLISHDLNLVRRiAHRVCVMQ 232
Cdd:cd03248 146 ekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLD 222
|
....
gi 799207702 233 KGCI 236
Cdd:cd03248 223 GGRI 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-253 |
1.08e-20 |
|
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: 93.64 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 29 VSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKTIRHIRGNRIAMIFQEpmTSLNP 108
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKT----TLIRLIA-GLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 109 LHNIEKqiNEVLGLhKGLTGKVATQRTLELLELVGIlEPhkRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:TIGR02142 89 HLSVRG--NLRYGM-KRARPSERRISFERVIELLGI-GH--LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPY 253
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
301-528 |
1.72e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.78 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQqldRLTQQQVRPLRREMQVVFQDPFgslsprm 379
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDI---PLTKLQLDSWRSRLAVVSQTPF------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 CVSEIVGEGLrihKMGTPAEQEAA--IIAALKEVGLD----PESrhrYPHE-------FSGGQRQRIAIARALVLKPRLI 446
Cdd:PRK10789 400 LFSDTVANNI---ALGRPDATQQEieHVARLASVHDDilrlPQG---YDTEvgergvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 447 LLDEPTSALDRTVQRQVVELLRslQAKYNLTYLFISHDL-AVVKAlsHQLMVVKHGQVVEQGDAAGIFAAP---QHGYTR 522
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLsALTEA--SEILVMQHGHIAQRGNHDQLAQQSgwyRDMYRY 549
|
....*.
gi 799207702 523 QLLEAA 528
Cdd:PRK10789 550 QQLEAA 555
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-510 |
2.17e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.03 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 306 NFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTqqqvrPLRREMQVVFQDpfGSLSPRMC 380
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL----LNLIAgfltpASGSLTLNGQDHTTTP-----PSRRPVSMLFQE--NNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVG----EGLRIHkmgtpAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:PRK10771 88 VAQNIGlglnPGLKLN-----AAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 457 RTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAA 510
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTD 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
302-503 |
2.49e-20 |
|
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: 88.43 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDP--F-GSlsp 377
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNE---LGDHVGYLPQDDelFsGS--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 rmcVSEIVgeglrihkmgtpaeqeaaiiaalkevgldpesrhrypheFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:cd03246 92 ---IAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 799207702 458 TVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALShQLMVVKHGQV 503
Cdd:cd03246 130 EGERALNQAIAALKAA-GATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
299-507 |
2.52e-20 |
|
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: 89.26 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQV------RPLRREMQVVFQ-D 370
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGeVLFDGKPLDIAARNRIgylpeeRGLYPKMKVIDQlV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 PFGSLSPrMCVSEIVGEGLRIhkmgtpaeqeaaiiaaLKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:cd03269 93 YLAQLKG-LKKEEARRRIDEW----------------LERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 451 PTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
302-515 |
3.31e-20 |
|
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: 94.04 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGlailRLI-G----SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDP----- 371
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLvGvwppTAGSVRLDGADLSQWDREE---LGRHIGYLPQDVelfdg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 --------FGSLSPRMCVS--EIVGeglrIHKM--------GTPaeqeaaiiaalkeVGldpESRHRypheFSGGQRQRI 433
Cdd:COG4618 421 tiaeniarFGDADPEKVVAaaKLAG----VHEMilrlpdgyDTR-------------IG---EGGAR----LSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 434 AIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIF 513
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 799207702 514 AA 515
Cdd:COG4618 555 AR 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
301-524 |
4.03e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTqqqVRPLRREMQVV------FQDPFG 373
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYT---LASLRNQVALVsqnvhlFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 -----SLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLdpesrhryphEFSGGQRQRIAIARALVLKPRLILL 448
Cdd:PRK11176 435 nniayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGV----------LLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 449 DEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFAapQHGYTRQL 524
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA--QNGVYAQL 575
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-247 |
4.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLL-TLKEKTIRHIRgNRIAMIFQEP 102
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLN-GLHVPTQGSVRVDDTLITsTSKNKDIKQIR-KKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 mtslnplhniEKQINEVLGLHK--------GLTGKVATQRTLELLELVGILEphKRLKALPHELSGGQRQRVMIAMALAN 174
Cdd:PRK13649 95 ----------ESQLFEETVLKDvafgpqnfGVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 175 EPELLIADEPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQ 247
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
289-507 |
5.16e-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: 89.31 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 289 KGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR-LIGSKGGirfEGQQLDRLTQQQVRPLRREMQVV 367
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-LKILSgLLQPTSG---EVRVAGLVPWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 368 F---QDPFGSLSPRmcvseivgEGLRIHK--MGTPAEQEAAIIAALKEVgLDPESRHRYP-HEFSGGQRQRIAIARALVL 441
Cdd:cd03267 100 FgqkTQLWWDLPVI--------DSFYLLAaiYDLPPARFKKRLDELSEL-LDLEELLDTPvRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
289-524 |
6.23e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 289 KGFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGqqldrltqqqVRPLRRE 363
Cdd:COG4586 25 KGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltGI----LVPTSGEVRVLG----------YVPFKRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 364 MQ------VVF-------QDpfgsLSPRmcvseivgEGLRIhkmgtpaeqeaaiiaaLKEV-GLDPESRHRYPHEFSG-- 427
Cdd:COG4586 91 KEfarrigVVFgqrsqlwWD----LPAI--------DSFRL----------------LKAIyRIPDAEYKKRLDELVEll 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 428 ---------------GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALS 492
Cdd:COG4586 143 dlgelldtpvrqlslGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALC 222
|
250 260 270
....*....|....*....|....*....|..
gi 799207702 493 HQLMVVKHGQVVEQGDAAGIFAapQHGYTRQL 524
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKE--RFGPYKTI 252
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
300-527 |
7.44e-20 |
|
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: 93.27 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GSL 375
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeILLNGFSLKDIDRHT---LRQFINYLPQEPYifsGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 -------SPRMCVSEIVGEGLRIHKMGTPAEQEaaiiaalkEVGLDPE-SRHRYphEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:TIGR01193 565 lenlllgAKENVSQDEIWAACEIAEIKDDIENM--------PLGYQTElSEEGS--SISGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAKynlTYLFISHDLAVVKaLSHQLMVVKHGQVVEQGDAAGIFAapQHGYTRQLLEA 527
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLD--RNGFYASLIHN 708
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-507 |
8.17e-20 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 88.37 E-value: 8.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 307 FSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQldrltqqqVRPLRREMQVVFQDPFGSLSPRMCVSEIV 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKVAGAS--------PGKGWRHIGYVPQRHEFAWDFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 386 GEGlRIHKMG----TPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQR 461
Cdd:TIGR03771 73 MSG-RTGHIGwlrrPCVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 799207702 462 QVVELLRSLQAKYNlTYLFISHDLAVVKALSHQLMVVkHGQVVEQG 507
Cdd:TIGR03771 151 LLTELFIELAGAGT-AILMTTHDLAQAMATCDRVVLL-NGRVIADG 194
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-234 |
8.42e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:PRK10908 1 MIRFEHVSKAYLGG---RQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLI-CGIERPSAGKIWFSGHDITRLKNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRHIRgNRIAMIFQEPMTSLNPLHNIEKQINEVLGlhkGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQRQR 165
Cdd:PRK10908 73 EVPFLR-RQIGMIFQDHHLLMDRTVYDNVAIPLIIA---GASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-249 |
9.02e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLlpYplarHP-SGTINYAGQDLLTLKE 84
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--Y----QPtGGQVLLDGVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KTIRhirgNRIAMIFQEPMtslnpLHNIEKQINEVLGLHKGLTGKV-ATQRTLELLELVGILEPHKRLKALPH--ELSGG 161
Cdd:TIGR00958 551 HYLH----RQVALVGQEPV-----LFSGSVRENIAYGLTDTPDEEImAAAKAANAHDFIMEFPNGYDTEVGEKgsQLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQlkilELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQAD 241
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
....*...
gi 799207702 242 CETLFQSP 249
Cdd:TIGR00958 697 HKQLMEDQ 704
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-260 |
9.48e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 13 SVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTINYAGQDLLTLKEktIRHIRg 92
Cdd:PRK14271 24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRD--VLEFR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 93 NRIAMIFQEPmtslNPL-HNIEKQINEVLGLHKGLTGK----VATQRTLEllelVGILEPHK-RLKALPHELSGGQRQRV 166
Cdd:PRK14271 101 RRVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKefrgVAQARLTE----VGLWDAVKdRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLgmALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLF 246
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
250
....*....|....
gi 799207702 247 QSPQHPYTQELLAA 260
Cdd:PRK14271 251 SSPKHAETARYVAG 264
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
276-507 |
1.01e-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: 87.47 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVwfpikkgflRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGQQLDRLtq 354
Cdd:cd03369 7 IEVENLSV---------RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 355 qQVRPLRREMQVVFQDPF---GSLSPRMCV-----SEIVGEGLRIhkmgtpaeqeaaiiaalKEVGLDpesrhrypheFS 426
Cdd:cd03369 76 -PLEDLRSSLTIIPQDPTlfsGTIRSNLDPfdeysDEEIYGALRV-----------------SEGGLN----------LS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 427 GGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkyNLTYLFISHDLAVVkALSHQLMVVKHGQVVEQ 506
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTI-IDYDKILVMDAGEVKEY 204
|
.
gi 799207702 507 G 507
Cdd:cd03369 205 D 205
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
302-507 |
1.01e-19 |
|
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: 92.70 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGlailRLIG-----SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---G 373
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIPREEIPREV---LANSVAMVDQDIFlfeG 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SL-------SPRMCVSEIVgEGLR---IHK--MGTPAEQEAAiiaaLKEVGLDpesrhrypheFSGGQRQRIAIARALVL 441
Cdd:TIGR03796 568 TVrdnltlwDPTIPDADLV-RACKdaaIHDviTSRPGGYDAE----LAEGGAN----------LSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRslqaKYNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQG 507
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
301-512 |
1.16e-19 |
|
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: 87.97 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRL-TQQQVRplrREMQVVFQ--DPFGSLS 376
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGsIRLDGEDITKLpPHERAR---AGIAYVPQgrEIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 prmcvseiVGEGLRIHKMGTPAEQEAAIIAA------LKEVgldpesRHRYPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:TIGR03410 92 --------VEENLLTGLAALPRRSRKIPDEIyelfpvLKEM------LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 451 PTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGI 512
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-237 |
1.26e-19 |
|
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: 88.16 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLPYPLarHP-SGTINYAGqdLLTLKEKtIRHIRgnRIAMIFQE- 101
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTT----LKILSGLL--QPtSGEVRVAG--LVPWKRR-KKFLR--RIGVVFGQk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 --------PMTSLNPLHNIekqinevlglhKGLTGKVATQRTLELLELvgiLEPHKRLKALPHELSGGQRQRVMIAMALA 173
Cdd:cd03267 104 tqlwwdlpVIDSFYLLAAI-----------YDLPPARFKKRLDELSEL---LDLEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 174 NEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-239 |
1.50e-19 |
|
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: 87.55 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYplarhPSGTINYAGQDLLTLKEKT 86
Cdd:cd03244 3 IEFKNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEPMT-------SLNPLHNI-EKQINEVlglhkgltgkvatqrtlelLELVGILEPHKRL-KALPHE 157
Cdd:cd03244 76 LR----SRISIIPQDPVLfsgtirsNLDPFGEYsDEELWQA-------------------LERVGLKEFVESLpGGLDTV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 -------LSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVrrI-AHRVC 229
Cdd:cd03244 133 veeggenLSVGQRQLLCLARALLRKSKILVLDEATASVD--PETDALIQKTIREAFKDCTVLTIAHRLDTI--IdSDRIL 208
|
250
....*....|
gi 799207702 230 VMQKGCIVEQ 239
Cdd:cd03244 209 VLDKGRVVEF 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
1.72e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHhqrVVNNVSFDIKRGETIALVGESGSGKSVTahsILRLLPYPLARHpsGTINYAGQDlltLK 83
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLNGIYLPQR--GRVKVMGRE---VN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRHIRgNRIAMIFQEPmtslnplhniEKQI-------NEVLG-LHKGLTGKVATQRTLELLELVGILEphKRLKAlP 155
Cdd:PRK13647 71 AENEKWVR-SKVGLVFQDP----------DDQVfsstvwdDVAFGpVNMGLDKDEVERRVEEALKAVRMWD--FRDKP-P 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGC 235
Cdd:PRK13647 137 YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
250
....*....|
gi 799207702 236 IVEQADCETL 245
Cdd:PRK13647 216 VLAEGDKSLL 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-258 |
1.75e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.98 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTINYAGQDLLTLKE 84
Cdd:PRK14267 3 FAIETVNLRVYY--GSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KTIRHIRgnRIAMIFQEPmtslNPLHNIEKQINEVLGLHkgLTGKVATQRTLE-----LLELVGILEPHK-RLKALPHEL 158
Cdd:PRK14267 79 DPIEVRR--EVGMVFQYP----NPFPHLTIYDNVAIGVK--LNGLVKSKKELDervewALKKAALWDEVKdRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTvqLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVE 238
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPV--GTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|
gi 799207702 239 QADCETLFQSPQHPYTQELL 258
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYV 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-239 |
1.84e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKT 86
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHirgnRIAMIFQEPMTslnplhNIEKQINEVLGL-----HKG-LTG--KVATQRTLELLELVGIlePHKRLkalpHEL 158
Cdd:COG4604 73 LAK----RLAILRQENHI------NSRLTVRELVAFgrfpySKGrLTAedREIIDEAIAYLDLEDL--ADRYL----DEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVtvqlkilellkeLQARLGMALL------------LISHDLNLVRRIAH 226
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM------------KHSVQMMKLLrrladelgktvvIVLHDINFASCYAD 204
|
250
....*....|...
gi 799207702 227 RVCVMQKGCIVEQ 239
Cdd:COG4604 205 HIVAMKDGRVVAQ 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-237 |
1.93e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 87.04 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLpYPLARHPSGTINYAGQDLLTLKEK 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRML-AGLLEPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgnRIAMIFQEpmTSLNPLHNIEKQINEVLGLHkGLTGKVATQRTLELLELVGILEPHKRLKAlphELSGGQRQR 165
Cdd:cd03266 76 ARR-----RLGFVSDS--TGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 166 VMIAMALANEPELLIADEPTTALDVTVqLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMA-TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-231 |
2.39e-19 |
|
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: 91.19 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDhhqRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhP-SGTINYAGQDLLTLKEK 85
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD------PtEGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgNRIAMIFQEPmtslnplHNIEKQINEVLGLHKGLTGKVATQRTLE---LLELVGILEP--HKRLKALPHELSG 160
Cdd:TIGR02857 393 SWR----DQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREALEragLDEFVAALPQglDTPIGEGGAGLSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVRRiAHRVCVM 231
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETE--AEVLEALRALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
2.74e-19 |
|
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: 85.56 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEfvtgdhhqRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpYPLARHPSGTINYAGQDLltlK 83
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL-----FGLRPPASGEITLDGKPV---T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRHIRGNRIAMIFQEPM-TSLNPLHNIEKQInevlglhkgltgkvatqrtlellelvgilephkrlkALPHELSGGQ 162
Cdd:cd03215 66 RRSPRDAIRAGIAYVPEDRKrEGLVLDLSVAENI------------------------------------ALSSLLSGGN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDV-TVQlkILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVgAKA--EIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
300-507 |
2.82e-19 |
|
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: 85.44 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGQQLDRLTQQqvrpLRREMQVVFQDPFgslsp 377
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTgdLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 rmCVSEIVGEGLrihkmGTPaeqeaaiiaalkevgldpesrhrypheFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:cd03247 86 --LFDTTLRNNL-----GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 799207702 458 TVQRQVVELLrsLQAKYNLTYLFISHDLAVVKALShQLMVVKHGQVVEQG 507
Cdd:cd03247 132 ITERQLLSLI--FEVLKDKTLIWITHHLTGIEHMD-KILFLENGKIIMQG 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-261 |
3.54e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.06 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYplarhpSGTINYAGQDLLT 81
Cdd:PRK11174 345 NDPVTIEAEDLEILSPDG---KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY------QGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHirgnRIAMIFQEPMTslnpLHNIEKQiNEVLGLHKgltgkvATQRTLE-LLELVGILEPHKRL-KALPHE-- 157
Cdd:PRK11174 416 LDPESWRK----HLSWVGQNPQL----PHGTLRD-NVLLGNPD------ASDEQLQqALENAWVSEFLPLLpQGLDTPig 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 -----LSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVRRIaHRVCVMQ 232
Cdd:PRK11174 481 dqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQ 557
|
250 260
....*....|....*....|....*....
gi 799207702 233 KGCIVEQADCETLfqSPQHPYTQELLAAE 261
Cdd:PRK11174 558 DGQIVQQGDYAEL--SQAGGLFATLLAHR 584
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
256-483 |
4.31e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 256 ELLAAEPSGGPATNVIGPPLLEVDDLKVWFPikkgflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRL 335
Cdd:COG4178 343 EAADALPEAASRIETSEDGALALEDLTLRTP----------DGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 336 I------GSkGGIRfegqqldrltqqqvRPLRREMQVVFQDPF---GSL-------SPRMCVSEivgEGLRihkmgtpae 399
Cdd:COG4178 409 IaglwpyGS-GRIA--------------RPAGARVLFLPQRPYlplGTLreallypATAEAFSD---AELR--------- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 400 qeaaiiAALKEVGLDP-----ESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRslQAKY 474
Cdd:COG4178 462 ------EALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELP 533
|
....*....
gi 799207702 475 NLTYLFISH 483
Cdd:COG4178 534 GTTVISVGH 542
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-242 |
4.74e-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: 85.68 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 30 SFDIKRGETIALVGESGSGKSvTAHSILRLLPYPLarhpSGTINYAGQDLLTLKEKTirhirgNRIAMIFQEPmtslNPL 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPA----SGSIKVNDQSHTGLAPYQ------RPVSMLFQEN----NLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 110 HNIEKQINEVLGLHKGLT-GKVATQRTLELLELVGILEPHKRLkalPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLKlNAEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADC 242
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-239 |
5.17e-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: 85.62 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFD--IKRGETIALVGESGSGKSvtahSILRLLP-YPLARhpSGTINYAGQDLlTLKEKTIRhirgnRIAMIFQEpmT 104
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKS----TLLNLIAgFETPQ--SGRVLINGVDV-TAAPPADR-----PVSMLFQE--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLNPLHNIEKQINevLGLHKGLT-GKVATQRTLELLELVGILEPHKRLkalPHELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:cd03298 80 NLFAHLTVEQNVG--LGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 184 PTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-250 |
6.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEKTIRHirgnRIAMIFQEPMts 105
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF-----EEFEGKVKIDGELLTAENVWNLRR----KIGMVFQNPD-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 lNPLHNIEKQINEVLGL-HKGLTGKVATQRTLELLELVGILEPHKRLkalPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:PRK13642 92 -NQFVGATVEDDVAFGMeNQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 185 TTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQADCETLFQSPQ 250
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
299-535 |
6.38e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQV------RPLRREM----QVV 367
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGeVLWDGEPLDPEDRRRIgylpeeRGLYPKMkvgeQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 368 FqdpFGSLsprmcvseivgEGLrihkmgTPAEQEAAIIAALKEVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:COG4152 94 Y---LARL-----------KGL------SKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAapQHGYTRQLLEA 527
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QFGRNTLRLEA 229
|
....*...
gi 799207702 528 AFLVPAAR 535
Cdd:COG4152 230 DGDAGWLR 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-236 |
6.43e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLArhpsGTINYAGQDLLTLKEKT 86
Cdd:PRK09536 4 IDVSDLSVEF--GD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PTA----GTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IrhirGNRIAMIFQEpmTSLNPLHNIEkQINEvLGLHKGL--------TGKVATQRTLELLELVgilephkRLKALP-HE 157
Cdd:PRK09536 75 A----SRRVASVPQD--TSLSFEFDVR-QVVE-MGRTPHRsrfdtwteTDRAAVERAMERTGVA-------QFADRPvTS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLkelqARL---GMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV----RRLvddGKTAVAAIHDLDLAARYCDELVLLADG 215
|
..
gi 799207702 235 CI 236
Cdd:PRK09536 216 RV 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-239 |
6.63e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.47 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFvtgDHHQrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLL 80
Cdd:PRK09452 9 SSLSPLVELRGISKSF---DGKE-VISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIA-GFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TL-KEKtiRHIRgnriaMIFQEpmTSLNPLHNIEKQINEVLGLHKGLTGKVATqRTLELLELVGiLEPHKRLKalPHELS 159
Cdd:PRK09452 80 HVpAEN--RHVN-----TVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQ-LEEFAQRK--PHQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIvEQ 239
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI-EQ 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
276-515 |
8.18e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPI--------KKGFLR---TTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SK 339
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslKELLLRrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAgilepTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 340 GGIRFEGqqldrltqqQVRPLrREMQVVFQdpfGSLSPRmcvsEIVGEGLRIHKMgtpaeqeaaiiaALKEVgldpesRH 419
Cdd:COG1134 81 GRVEVNG---------RVSAL-LELGAGFH---PELTGR----ENIYLNGRLLGL------------SRKEI------DE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 420 RYPH--EFSG--------------GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISH 483
Cdd:COG1134 126 KFDEivEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSH 204
|
250 260 270
....*....|....*....|....*....|..
gi 799207702 484 DLAVVKALSHQLMVVKHGQVVEQGDAAGIFAA 515
Cdd:COG1134 205 SMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-259 |
9.94e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 9.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHPSGTInyAGQDLLTLKEKTIRHIRGNR--IAMIFQE 101
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKS----TMIQLTNGLIISETGQTI--VGDYAIPANLKKIKEVKRLRkeIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMTSLNPlHNIEKQIneVLG-LHKGLTGKVATQRTLELLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK13645 99 PEYQLFQ-ETIEKDI--AFGpVNLGENKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 181 ADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSpqhpytQELLA 259
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN------QELLT 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-234 |
1.00e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDhhQRVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLpYPLARHPSGTINYAGQDLltlkEKT 86
Cdd:PRK13537 8 IDFRNVEKRY--GD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTT----LRML-LGLTHPDAGSISLCGEPV----PSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQepMTSLNPLHNIEKQInEVLGLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRV 166
Cdd:PRK13537 75 ARHAR-QRVGVVPQ--FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-237 |
1.16e-18 |
|
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: 84.95 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDlsVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:cd03245 3 IEFRN--VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS----TLLKLL-AGLYKPTSGSVLLDGTDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHirgnRIAMIFQEPMTSLNPLHNiekqiNEVLGLhkgltGKVATQRTLELLELVGIlepHKRLKALPH---------- 156
Cdd:cd03245 76 LRR----NIGYVPQDVTLFYGTLRD-----NITLGA-----PLADDERILRAAELAGV---TDFVNKHPNgldlqigerg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 -ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVrRIAHRVCVMQKGC 235
Cdd:cd03245 139 rGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE--ERLKERLRQLLGDKTLIIITHRPSLL-DLVDRIIVMDSGR 215
|
..
gi 799207702 236 IV 237
Cdd:cd03245 216 IV 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-250 |
1.24e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.90 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVT---AHSILRllpyplarhPSG--------TINY 74
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILK---------PTSgevlikgePIKY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 75 AGQDLLTLKEKtirhirgnrIAMIFQEPMTSL-NPlhNIEKQIneVLG-LHKGLTGKVATQRTLELLELVGILEPHKRLk 152
Cdd:PRK13639 69 DKKSLLEVRKT---------VGIVFQNPDDQLfAP--TVEEDV--AFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKP- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 153 alPHELSGGQRQRVMIAMALANEPELLIADEPTTALDvTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQ 232
Cdd:PRK13639 135 --PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD-PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMS 211
|
250
....*....|....*...
gi 799207702 233 KGCIVEQADCETLFQSPQ 250
Cdd:PRK13639 212 DGKIIKEGTPKEVFSDIE 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-189 |
1.54e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQRVV-NNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLArhpSGTINYAGQDLLTLK 83
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRAlDGLNLTIEEGDFVTVIGSNGAGKS----TLLNAIAgsLPPD---SGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EktirHIRGNRIAMIFQEPMT----SLNPLHN--IEKQINEVLGLHKGLTGKvatQRTL--ELLELVGI-LEphKRLKAL 154
Cdd:COG1101 75 E----YKRAKYIGRVFQDPMMgtapSMTIEENlaLAYRRGKRRGLRRGLTKK---RRELfrELLATLGLgLE--NRLDTK 145
|
170 180 190
....*....|....*....|....*....|....*
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-190 |
1.85e-18 |
|
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: 84.75 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpypLARHPSGtinyAGQDLLTLK 83
Cdd:COG1119 1 DPLLELRNVTVRR--GGK--TILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI---TGDLPPT----YGNDVRLFG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EK----TIRHIRgNRIAMIFQEPMTSLNPLHNIEkqinEV--------LGLHKGLTgKVATQRTLELLELVGILepHKRL 151
Cdd:COG1119 66 ERrggeDVWELR-KRIGLVSPALQLRFPRDETVL----DVvlsgffdsIGLYREPT-DEQRERARELLELLGLA--HLAD 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 799207702 152 KALpHELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:COG1119 138 RPF-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
276-509 |
1.87e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.73 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVwfpikkgflrtTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILrliGS------KGGIRFEGQQL 349
Cdd:COG0396 1 LEIKNLHV-----------SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM---GHpkyevtSGSILLDGEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 DRLTQQQvRPlRREMQVVFQDPfgslsprmcvSEI----VGEGLRI---HKMGTPAEQEAAIIA---ALKEVGLDPESRH 419
Cdd:COG0396 67 LELSPDE-RA-RAGIFLAFQYP----------VEIpgvsVSNFLRTalnARRGEELSAREFLKLlkeKMKELGLDEDFLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 420 RYPHE-FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHD---LAVVKAlsHQL 495
Cdd:COG0396 135 RYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYqriLDYIKP--DFV 211
|
250
....*....|....
gi 799207702 496 MVVKHGQVVEQGDA 509
Cdd:COG0396 212 HVLVDGRIVKSGGK 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
304-503 |
2.35e-18 |
|
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: 84.06 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLdrlTQQQVRPLRREMQVVFQDPfgSLSPRmCVS 382
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqVLLDGKPI---SQYEHKYLHSKVSLVGQEP--VLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGLRihkmGTPAEQEAAIIAALKEVGLDPESRHRYPHE-------FSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:cd03248 106 DNIAYGLQ----SCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 456 DRTVQRQVVELLRslQAKYNLTYLFISHDLAVVKAlSHQLMVVKHGQV 503
Cdd:cd03248 182 DAESEQQVQQALY--DWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
2.75e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFvTGDHhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLL 80
Cdd:PRK13648 2 EDKNSIIVFKNVSFQY-QSDA-SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-----SGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRhirgNRIAMIFQEPMtslNPLHNIEKQINEVLGL------HKGLTGKVAtqrtlELLELVGILEphkRLKAL 154
Cdd:PRK13648 75 DDNFEKLR----KHIGIVFQNPD---NQFVGSIVKYDVAFGLenhavpYDEMHRRVS-----EALKQVDMLE---RADYE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHrVCVMQKG 234
Cdd:PRK13648 140 PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKG 218
|
250
....*....|....*.
gi 799207702 235 CIVEQADCETLFQSPQ 250
Cdd:PRK13648 219 TVYKEGTPTEIFDHAE 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-236 |
2.96e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVEFVTGDHHQR-VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYplARHPSGTINYAGQDLLTLKEKTIRhi 90
Cdd:PRK11247 13 LLLNAVSKRYGERtVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAG--LETPSAGELLAGTAPLAEAREDTR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 91 rgnriaMIFQEpmTSLNPLhniEKQINEVlGLhkGLTGKvATQRTLELLELVGILEphkRLKALPHELSGGQRQRVMIAM 170
Cdd:PRK11247 85 ------LMFQD--ARLLPW---KKVIDNV-GL--GLKGQ-WRDAALQALAAVGLAD---RANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 171 ALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-245 |
3.16e-18 |
|
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: 83.73 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEktirHIRGNR-IA------M 97
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK-----SGSIRLDGEDITKLPP----HERARAgIAyvpqgrE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 98 IFqepmTSLNPLHNIEkqinevLGLhkGLTGKVATQRTLELLELVGILepHKRLKALPHELSGGQRQRVMIAMALANEPE 177
Cdd:TIGR03410 86 IF----PRLTVEENLL------TGL--AALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 178 LLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETL 245
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
300-513 |
3.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLT--QQQVRPLRREMQVVFQDPFGSLSP 377
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIV--GEGLRIHKmgtpAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:PRK13643 100 ETVLKDVAfgPQNFGIPK----EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 456 DRTVQRQVVELLRSLQaKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK13643 176 DPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
301-529 |
3.93e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTlglaILR-------LIGS---KGGIRFEGQQLdrlTQQQVRP--LRREMQVVF 368
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKST----ILRcfnrlndLIPGfrvEGKVTFHGKNL---YAPDVDPveVRRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 369 Q--DPFgslsPRmCVSEIVGEGLRIHkmGTPAEQEAAIIAALKEVGLDPESRHRYPHE---FSGGQRQRIAIARALVLKP 443
Cdd:PRK14243 98 QkpNPF----PK-SIYDNIAYGARIN--GYKGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 444 RLILLDEPTSALDRTVQRQVVELLRSLQAKYnlTYLFISHDLAVVKALSHQLMVV---------KHGQVVEQGDAAGIFA 514
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFN 248
|
250
....*....|....*
gi 799207702 515 APQHGYTRQLLEAAF 529
Cdd:PRK14243 249 SPQQQATRDYVSGRF 263
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-238 |
4.38e-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: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQR------------------VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLlpypLAR-- 66
Cdd:cd03220 1 IELENVSKSYPTYKGGSSslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKS----TLLRL----LAGiy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 67 HP-SGTINyagqdlltlkektirhIRGnRIAMIFqEPMTSLNP----LHNIekqinEVLGLHKGLTGKVATQRTLELLEL 141
Cdd:cd03220 73 PPdSGTVT----------------VRG-RVSSLL-GLGGGFNPeltgRENI-----YLNGRLLGLSRKEIDEKIDEIIEF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 142 VGILEP-HKRLKalphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNL 220
Cdd:cd03220 130 SELGDFiDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSS 204
|
250
....*....|....*...
gi 799207702 221 VRRIAHRVCVMQKGCIVE 238
Cdd:cd03220 205 IKRLCDRALVLEKGKIRF 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-507 |
4.77e-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: 82.97 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPIKKGFLR-----------TTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SK 339
Cdd:cd03220 1 IELENVSKSYPTYKGGSSslkklgilgrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLAgiyppDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 340 GGIRFEGqqldrltqqQVRPLrREMQVVFQdpfGSLSPRMCVsEIVGeglRIHkmgtpaeqeaaiiaalkevGLDP-ESR 418
Cdd:cd03220 77 GTVTVRG---------RVSSL-LGLGGGFN---PELTGRENI-YLNG---RLL-------------------GLSRkEID 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 419 HRYP--HEFSG--------------GQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFIS 482
Cdd:cd03220 121 EKIDeiIEFSElgdfidlpvktyssGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVS 199
|
250 260
....*....|....*....|....*
gi 799207702 483 HDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03220 200 HDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-218 |
4.80e-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: 87.03 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLLTLKEKT 86
Cdd:TIGR02868 335 LELRDLSAGYPGA---PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-PL----QGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEPmtslnplHNIEKQINEVLGLHKGltgKVATQRTLELLELVGILEPhkrLKALPH---------- 156
Cdd:TIGR02868 407 VR----RRVSVCAQDA-------HLFDTTVRENLRLARP---DATDEELWAALERVGLADW---LRALPDgldtvlgegg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 157 -ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVqlKILELLKELQARLGMALLLISHDL 218
Cdd:TIGR02868 470 aRLSGGERQRLALARALLADAPILLLDEPTEHLDAET--ADELLEDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
255-515 |
5.53e-18 |
|
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: 87.02 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 255 QELLAAEPSGGPATNVIGPP-LLEVDDLKVWFPIKKgflRTTVDyvkavdGINFSLPQGQTLGIVGESGSGKSTLGLAIL 333
Cdd:TIGR01842 295 NELLANYPSRDPAMPLPEPEgHLSVENVTIVPPGGK---KPTLR------GISFSLQAGEALAIIGPSGSGKSTLARLIV 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 334 RLIG-SKGGIRFEGQQLDRLTQQQVRP----LRREMQVvFQdpfGSLSPRMC------VSEIVGEGLRI---HKM--GTP 397
Cdd:TIGR01842 366 GIWPpTSGSVRLDGADLKQWDRETFGKhigyLPQDVEL-FP---GTVAENIArfgenaDPEKIIEAAKLagvHELilRLP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 398 AEQEAaiiaalkEVGLDPESrhrypheFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLT 477
Cdd:TIGR01842 442 DGYDT-------VIGPGGAT-------LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GIT 506
|
250 260 270
....*....|....*....|....*....|....*...
gi 799207702 478 YLFISHDLAVVkALSHQLMVVKHGQVVEQGDAAGIFAA 515
Cdd:TIGR01842 507 VVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
274-507 |
6.29e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.50 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFpikKGFLrttvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGQQ 348
Cdd:PRK11300 4 PLLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTT----VFNCLTgfykpTGGTILLRGQH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQQVRplRREMQVVFQDPfgSLSPRMCVSE--------IVGEGLRIHKMGTP------AEQEAAIIAALKEVGLD 414
Cdd:PRK11300 69 IEGLPGHQIA--RMGVVRTFQHV--RLFREMTVIEnllvaqhqQLKTGLFSGLLKTPafrraeSEALDRAATWLERVGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 415 PESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQ 494
Cdd:PRK11300 145 EHA-NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDR 223
|
250
....*....|...
gi 799207702 495 LMVVKHGQVVEQG 507
Cdd:PRK11300 224 IYVVNQGTPLANG 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-257 |
6.37e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.66 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSveFVTGDhhQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLaRHPSGTINYAGQDLL 80
Cdd:PRK11831 2 QSVANLVDMRGVS--FTRGN--RCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQI-APDHGEILFDGENIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRgNRIAMIFQEP--MTSLNPLHNIEKQINEvlglHKGLTGKVATQRTLELLELVGIlepHKRLKALPHEL 158
Cdd:PRK11831 73 AMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGL---RGAAKLMPSEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVE 238
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
250
....*....|....*....
gi 799207702 239 QADCETLFQSPQHPYTQEL 257
Cdd:PRK11831 225 HGSAQALQANPDPRVRQFL 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-260 |
8.14e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.55 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTgdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTINYAGQDLLTlKEKT 86
Cdd:PRK14258 8 IKVNNLSFYYDT----QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYE-RRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQEPmtSLNPLH---NIEKQInEVLGLHKGLTGKVATQRTLELLELVGilEPHKRLKALPHELSGGQR 163
Cdd:PRK14258 83 LNRLR-RQVSMVHPKP--NLFPMSvydNVAYGV-KIVGWRPKLEIDDIVESALKDADLWD--EIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQK-----GCIVE 238
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236
|
250 260
....*....|....*....|..
gi 799207702 239 QADCETLFQSPQHPYTQELLAA 260
Cdd:PRK14258 237 FGLTKKIFNSPHDSRTREYVLS 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-257 |
8.82e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAgqDLL---TLKEKTIRHIRgNRIAMIFQ 100
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-----QPTEGKVTVG--DIVvssTSKQKEIKPVR-KKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPMTSLNPlHNIEKQIN---EVLGLHKGLTGKVATQRtlelLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPE 177
Cdd:PRK13643 92 FPESQLFE-ETVLKDVAfgpQNFGIPKEKAEKIAAEK----LEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 178 LLIADEPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQHPYTQEL 257
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHEL 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
300-514 |
1.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQ-----QLDRLtqQQVRPLRREMQVVFQDPFGS 374
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipaNLKKI--KEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSPRMCVSEIV-GEglrIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK13645 103 LFQETIEKDIAfGP---VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
7-251 |
1.26e-17 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 86.15 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKekt 86
Cdd:TIGR03796 478 VELRNITFGYSPLEPP--LIENFSLTLQPGQRVALVGGSGSGKS----TIAKLVA-GLYQPWSGEILFDGIPREEIP--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 iRHIRGNRIAMIFQEpmTSLnplhnIEKQINEVLGLHkgltgkvatQRTLELLELVGILEP---HKRLKALPHE------ 157
Cdd:TIGR03796 548 -REVLANSVAMVDQD--IFL-----FEGTVRDNLTLW---------DPTIPDADLVRACKDaaiHDVITSRPGGydaela 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 -----LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLkelqARLGMALLLISHDLNLVRRiAHRVCVMQ 232
Cdd:TIGR03796 611 egganLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLSTIRD-CDEIIVLE 685
|
250
....*....|....*....
gi 799207702 233 KGCIVEQADCETLFQSPQH 251
Cdd:TIGR03796 686 RGKVVQRGTHEELWAVGGA 704
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-239 |
1.29e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.92 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYAGQDLLTLKEK 85
Cdd:TIGR02203 330 DVEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPR-FYEPDSGQILLDGHDLADYTLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRhirgNRIAMIFQEPMTSLNPLHNiekqinevlGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHE-------- 157
Cdd:TIGR02203 403 SLR----RQVALVSQDVVLFNDTIAN---------NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvl 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL-----GMALLLISHDLNLVRRiAHRVCVMQ 232
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESE-------RLVQAALerlmqGRTTLVIAHRLSTIEK-ADRIVVMD 541
|
....*..
gi 799207702 233 KGCIVEQ 239
Cdd:TIGR02203 542 DGRIVER 548
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-228 |
1.88e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.36 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTInyagqdlltlkektiRHIRGNRIAMIFQE- 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL-----RPTSGTV---------------RRAGGARVAYVPQRs 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 ------PMTslnplhniekqINEVLGL----HKGLTGKV---ATQRTLELLELVGILEPHKRlkALpHELSGGQRQRVMI 168
Cdd:NF040873 65 evpdslPLT-----------VRDLVAMgrwaRRGLWRRLtrdDRAAVDDALERVGLADLAGR--QL-GELSGGQRQRALL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 169 AMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRV 228
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
302-502 |
1.90e-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: 79.89 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIrfegqqldrltqqqVRPLRREMQVVFQDPFgsls 376
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSL----FRALAglwpwGSGRI--------------GMPEGEDLLFLPQRPY---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 prMCVseivgeglrihkmGTpaeqeaaiiaaLKEVGLdpesrhrYP--HEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:cd03223 75 --LPL-------------GT-----------LREQLI-------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 799207702 455 LDRTVQRQVVELLRSLQAkynlTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:cd03223 122 LDEESEDRLYQLLKELGI----TVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-189 |
1.96e-17 |
|
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: 81.09 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgdHHQRVVNNVSFDIKRGeTIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKt 86
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILA-TLTPPSSGTIRIDGQDVLKQPQK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irhIRGnRIAMIFQEPMTSlnPLHNIEKQINeVLGLHKGLTGKVATQRTLELLELVGILEphkRLKALPHELSGGQRQRV 166
Cdd:cd03264 70 ---LRR-RIGYLPQEFGVY--PNFTVREFLD-YIAWLKGIPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRV 139
|
170 180
....*....|....*....|...
gi 799207702 167 MIAMALANEPELLIADEPTTALD 189
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-236 |
2.21e-17 |
|
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: 79.95 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLLTLKEKT 86
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-PT----SGRVRLDGADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IrhirGNRIAMIFQEPMTslnplhniekqinevlglhkgLTGKVATQrtlellelvgILephkrlkalphelSGGQRQRV 166
Cdd:cd03246 74 L----GDHVGYLPQDDEL---------------------FSGSIAEN----------IL-------------SGGQRQRL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRiAHRVCVMQKGCI 236
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-503 |
2.59e-17 |
|
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: 79.78 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 272 GPPLLEVDDLKVWfpikkgflrttvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLD 350
Cdd:cd03215 1 GEPVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGeITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 351 RLtqqqvrplrremqvvfqdpfgslSPRmcvseivgeglRIHKMGtpaeqeaaiiaalkeVGLDPESRHRY--------- 421
Cdd:cd03215 66 RR-----------------------SPR-----------DAIRAG---------------IAYVPEDRKREglvldlsva 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 422 -----PHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLM 496
Cdd:cd03215 97 enialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRIL 175
|
....*..
gi 799207702 497 VVKHGQV 503
Cdd:cd03215 176 VMYEGRI 182
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
305-507 |
2.90e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.54 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDrltqqQVRPLRREMQVVFQDPfgSLSPRM 379
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTL----LRMIAglediTSGDLFIGEKRMN-----DVPPAERGVGMVFQSY--ALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 CVSEIVGEGLRIHKMGTPAEQEAaiiaaLKEVGLDPESRH---RYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQR-----VNQVAEVLQLAHlldRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 799207702 457 RTVQRQV-VELLRsLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:PRK11000 166 AALRVQMrIEISR-LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-238 |
3.09e-17 |
|
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: 80.53 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 3 QDNLIEIRDLSVEFvtGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYplarhPSGTINYAGQDLLTL 82
Cdd:cd03369 3 EHGEIEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 KEKTIRhirgNRIAMIFQEPM-------TSLNPL-HNIEKQINEVLglhkgltgkvatqrtlellelvgilephkRLKAL 154
Cdd:cd03369 76 PLEDLR----SSLTIIPQDPTlfsgtirSNLDPFdEYSDEEIYGAL-----------------------------RVSEG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLnlvRRIA--HRVCVMQ 232
Cdd:cd03369 123 GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRL---RTIIdyDKILVMD 197
|
....*.
gi 799207702 233 KGCIVE 238
Cdd:cd03369 198 AGEVKE 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
302-512 |
3.23e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.28 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPfgSLSPRMC 380
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGeVLVDGLDVATTPSRE---LAKRLAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHKMGTPAEQ-EAAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTV 459
Cdd:COG4604 92 VRELVAFGRFPYSKGRLTAEdREIIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 799207702 460 QRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGI 512
Cdd:COG4604 171 SVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
305-517 |
4.89e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLP-QGQTlGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQL-DRLTQQQVRPLRREMQVVFQDpfGSLSPRMCV 381
Cdd:PRK11144 17 VNLTLPaQGIT-AIFGRSGAGKTSLINAISGLTRpQKGRIVLNGRVLfDAEKGICLPPEKRRIGYVFQD--ARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 382 SEIVGEGLRiHKMgtpaeqEAAIIAALKEVGLDPESRhRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQR 461
Cdd:PRK11144 94 RGNLRYGMA-KSM------VAQFDKIVALLGIEPLLD-RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 462 QVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-257 |
6.93e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDlsVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpyplARH---PSGTINYAGQDLLTL 82
Cdd:PRK11160 338 SLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLL----TRAwdpQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 KEKTIRhirgNRIAMIFQEPMTSLNPLHNiekqiNEVLGLHKgltgkvAT-QRTLELLELVGI---LEPHKRLKALPHE- 157
Cdd:PRK11160 408 SEAALR----QAISVVSQRVHLFSATLRD-----NLLLAAPN------ASdEALIEVLQQVGLeklLEDDKGLNAWLGEg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 ---LSGGQRQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQarlGMALLLISHDLNLVRRIaHRVCVMQK 233
Cdd:PRK11160 473 grqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaETERQILELLAEHAQ---NKTVLMITHRLTGLEQF-DRICVMDN 548
|
250 260
....*....|....*....|....
gi 799207702 234 GCIVEQADCETLFQspQHPYTQEL 257
Cdd:PRK11160 549 GQIIEQGTHQELLA--QQGRYYQL 570
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
276-507 |
8.31e-17 |
|
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: 78.75 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVWFPIKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGS--KGGIRFEGQQLDR 351
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQL-----LKNVSGKAKPGELTAIMGPSGAGKSTL-LNALagRRTGLgvSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 352 LTqqqvrpLRREMQVVFQDP--FGSLSPRmcvseivgEGLRIHkmgtpaeqeaaiiAALKevGLdpesrhryphefSGGQ 429
Cdd:cd03213 78 RS------FRKIIGYVPQDDilHPTLTVR--------ETLMFA-------------AKLR--GL------------SGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 430 RQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDL-AVVKALSHQLMVVKHGQVVEQG 507
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
273-505 |
1.10e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKVWFPikkGflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGQQL- 349
Cdd:PRK11288 2 SPYLSFDGIGKTFP---G--------VKALDDISFDCRAGQVHALMGENGAGKSTL-LKILSgnYQPDAGSILIDGQEMr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 -----DRLTQQqVRPLRREMQVVfqdpfgslsPRMCVSEIVGEGLRIHKMG--TPAEQEAAIIAALKEVG--LDPESRHR 420
Cdd:PRK11288 70 fasttAALAAG-VAIIYQELHLV---------PEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGvdIDPDTPLK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 421 YpheFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKH 500
Cdd:PRK11288 140 Y---LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKD 215
|
....*
gi 799207702 501 GQVVE 505
Cdd:PRK11288 216 GRYVA 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
25-248 |
1.19e-16 |
|
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: 83.25 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLlpYPLARhpsGTINYAGQDLLTLKEKTIRHirgnRIAMIFQEpmt 104
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRL--YTPQH---GQVLVDGVDLAIADPAWLRR----QMGVVLQE--- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 slNPLHNieKQINEVLGLHKGltgKVATQRTLELLELVGilePHKRLKALPH-----------ELSGGQRQRVMIAMALA 173
Cdd:TIGR01846 540 --NVLFS--RSIRDNIALCNP---GAPFEHVIHAAKLAG---AHDFISELPQgyntevgekgaNLSGGQRQRIAIARALV 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 174 NEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQADCETLFQS 248
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLAL 681
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
303-505 |
1.36e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLGLAILrligskggirfeGQQLDRLTQQQVRplrremqvVFQDPFGSLSPrmcVS 382
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLA------------GALKGTPVAGCVD--------VPDNQFGREAS---LI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGeglrihkmgtPAEQEAAIIAALKEVGL-DPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQR 461
Cdd:COG2401 104 DAIG----------RKGDFKDAVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 799207702 462 QVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKH-GQVVE 505
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGyGGVPE 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-488 |
1.47e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 82.69 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLarhPSGTINYAgQDLLT-- 81
Cdd:PRK11147 3 LISIHGAWLSF--SDA--PLLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNgeVLL---DDGRIIYE-QDLIVar 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LKEKTIRHIRGN---RIAMIFQEPMTSLNPLHNI---------EKQINEVLGLHKGLTGKVATQ---RTLELLELVGiLE 146
Cdd:PRK11147 71 LQQDPPRNVEGTvydFVAEGIEEQAEYLKRYHDIshlvetdpsEKNLNELAKLQEQLDHHNLWQlenRINEVLAQLG-LD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 147 PHKRLKalphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVRRIAH 226
Cdd:PRK11147 150 PDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMAT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 227 RVCVMQKGCIV--------------EQADCETLfqspQHPYTQELLAAEPS----GGPA--------------------- 267
Cdd:PRK11147 222 RIVDLDRGKLVsypgnydqyllekeEALRVEEL----QNAEFDRKLAQEEVwirqGIKArrtrnegrvralkalrrerse 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 268 -TNVIGPPLLEVDDL----KVWFPIKKgfLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL-GLAILRLIGSKGG 341
Cdd:PRK11147 298 rREVMGTAKMQVEEAsrsgKIVFEMEN--VNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLlKLMLGQLQADSGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 342 IRFeGQQLDRLTQQQVRplrremqvvfqdpfGSLSPRMCVSEIVGEGlrihKmgtpaeqeaaiiaalKEVGLDPESRH-- 419
Cdd:PRK11147 376 IHC-GTKLEVAYFDQHR--------------AELDPEKTVMDNLAEG----K---------------QEVMVNGRPRHvl 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 420 RYPHEF--------------SGGQRQRIAIARaLVLKP-RLILLDEPTSALDrtvqRQVVELLRSLQAKYNLTYLFISHD 484
Cdd:PRK11147 422 GYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
....
gi 799207702 485 LAVV 488
Cdd:PRK11147 497 RQFV 500
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
302-533 |
1.66e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.29 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLTQQQvrpLRREMQVVFQDPfgsLSPR-M 379
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtVFLGDKPISMLSSRQ---LARRLALLPQHH---LTPEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 380 CVSEIVGEGLRIH-----KMGTpaEQEAAIIAALKEVGLDPESRHRYPhEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:PRK11231 92 TVRELVAYGRSPWlslwgRLSA--EDNARVNQAMEQTRINHLADRRLT-DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 455 LDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGdaagifaAPQHGYTRQLLEAAFLVPA 533
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLRTVFDVEA 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
298-470 |
2.64e-16 |
|
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: 78.08 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 298 YVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSK----GGIRFEGQQLDRLTQQQvrplrremQVVFQDPFG 373
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQPRKPDQFQK--------CVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SLSPRMCVSEIV--GEGLRIH-KMGTPAEQEAAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:cd03234 91 ILLPGLTVRETLtyTAILRLPrKSSDAIRKKRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180
....*....|....*....|
gi 799207702 451 PTSALDRTVQRQVVELLRSL 470
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQL 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-507 |
3.84e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRltqqQVRPLRREMQVVFQdpFGSLSPRMC 380
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPA----RARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHKMGTpAEQEAAIIAALKEVGLDPESRHRYPhEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:PRK13536 131 VRENLLVFGRYFGMST-REIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 461 RQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:PRK13536 209 HLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
305-516 |
5.56e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDrltQQQVRPLRREMQVVFQdpfgSLSPR- 378
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTL----LKMLGrhqppSEGEILLDAQPLE---SWSSKAFARKVAYLPQ----QLPAAe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 -MCVSEIVGEGlRIHKMGTPAEQEAAIIAALKE----VGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK10575 99 gMTVRELVAIG-RYPWHGALGRFGAADREKVEEaislVGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 454 ALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
299-504 |
5.93e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLIG--SKGGIRFEGQQLDRLTQQQVRPLRRE-MQVVFQDPfgSL 375
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLDkpTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRY--HL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SPRMCVSEIVgEGLRIHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:PRK10535 98 LSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207702 456 DRTVQRQVVELLRSLQAKYNlTYLFISHDLAVVkALSHQLMVVKHGQVV 504
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-509 |
6.27e-16 |
|
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: 76.41 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 LEVDDLKVwfpikkgflrtTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL---RLIGSKGGIRFEGQQLDRL 352
Cdd:cd03217 1 LEIKDLHV-----------SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 353 TQQQvRPlRREMQVVFQDPFgslsprmcvsEIvgEGLRIHKMgtpaeqeaaiiaaLKEVGLDpesrhrypheFSGGQRQR 432
Cdd:cd03217 70 PPEE-RA-RLGIFLAFQYPP----------EI--PGVKNADF-------------LRYVNEG----------FSGGEKKR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 433 IAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHD---LAVVKALSHQLMVvkHGQVVEQGDA 509
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIKPDRVHVLY--DGRIVKSGDK 189
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
274-484 |
7.37e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLkvwfpikkGFLrttVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGS-----KGGIRFEGQQ 348
Cdd:PRK10247 6 PLLQLQNV--------GYL---AGDAKILNNISFSLRAGEFKLITGPSGCGKSTL----LKIVASlisptSGTLLFEGED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQQvrpLRREMQVVFQDP--FGslsprmcvsEIVGEGL----RIHKMgTPAEQEAAIIaaLKEVGLDPESRHRYP 422
Cdd:PRK10247 71 ISTLKPEI---YRQQVSYCAQTPtlFG---------DTVYDNLifpwQIRNQ-QPDPAIFLDD--LERFALPDTILTKNI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 423 HEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHD 484
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-504 |
7.57e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYplARHP-SGTINYAGQdllTLKEKTIRHIRGNRIAMIFQEp 102
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKS----TLLKILSG--NYQPdAGSILIDGQ---EMRFASTTAALAAGVAIIYQE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 mtslnpLHNI-EKQINEVLGL----HKG--LTGKVATQRTLELLELVGI-LEPHKRLKalphELSGGQRQRVMIAMALAN 174
Cdd:PRK11288 88 ------LHLVpEMTVAENLYLgqlpHKGgiVNRRLLNYEAREQLEHLGVdIDPDTPLK----YLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 175 EPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ-ADCETLfqspqhpy 253
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV-------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 254 TQELLAAEPSGGPATNVIGppllevddlkvWFPIKKGFLRTTVDYVKAV---DGINFSLPQGQTLGIVGESGSGKSTLgl 330
Cdd:PRK11288 229 DRDQLVQAMVGREIGDIYG-----------YRPRPLGEVRLRLDGLKGPglrEPISFSVRAGEIVGLFGLVGAGRSEL-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 331 aiLRLI-----GSKGGIRFEGQQLD-RLTQQQVR------PLRREMQVVFQ----------------DPFGSLSPRMCVS 382
Cdd:PRK11288 296 --MKLLygatrRTAGQVYLDGKPIDiRSPRDAIRagimlcPEDRKAEGIIPvhsvadninisarrhhLRAGCLINNRWEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGLRIHKMGTPaeqeaaiiaalkevgldpeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ 462
Cdd:PRK11288 374 ENADRFIRSLNIKTP-------------------SREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHE 434
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 799207702 463 VVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVV 504
Cdd:PRK11288 435 IYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-503 |
7.76e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 27 NNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLarhPSGTINYAGQDlltlkektiRHIRGNR------IAMI 98
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKS----TMMKVLTgiYTR---DAGSILYLGKE---------VTFNGPKssqeagIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 99 FQEpmtsLNPLHNIEKQINEVLGLHK-----GLTGKVATQRTLELLELVGILEPHKRLKAlphELSGGQRQRVMIAMALA 173
Cdd:PRK10762 85 HQE----LNLIPQLTIAENIFLGREFvnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 174 NEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKG-----CIVEQADCETLFQ- 247
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGqfiaeREVADLTEDSLIEm 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 248 ------SPQHPYtqelLAAEPsggpatnviGPPLLEVDDLKvwfpikkGflrttvdyvKAVDGINFSLPQGQTLGIVGES 321
Cdd:PRK10762 237 mvgrklEDQYPR----LDKAP---------GEVRLKVDNLS-------G---------PGVNDVSFTLRKGEILGVSGLM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 322 GSGKSTLGLAIL-RLIGSKGGIRFEGQQLDRLTQQQ------------------VRPL--RREMQVVFQDPFGSLSPRMC 380
Cdd:PRK10762 288 GAGRTELMKVLYgALPRTSGYVTLDGHEVVTRSPQDglangivyisedrkrdglVLGMsvKENMSLTALRYFSRAGGSLK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSE---IVGEGLRIHKMGTPaeqeaaiiaalkevgldpeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:PRK10762 368 HADeqqAVSDFIRLFNIKTP-------------------SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 799207702 458 TVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK10762 429 GAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-219 |
7.84e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.37 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 21 HHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLarHPSGTINYAGQDLLTLKektirhIRGNRIAMIFQ 100
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAF--SASGEVLLNGRRLTALP------AEQRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPMtsLNPLHNIEKqiNEVLGLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:COG4136 84 DDL--LFPHLSVGE--NLAFALPPTIGRAQRRARVEQALEEAGL---AGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 799207702 181 ADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLN 219
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-237 |
8.06e-16 |
|
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: 80.68 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEKT 86
Cdd:TIGR03375 464 IEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGRIGSGKS----TLLKLL-LGLYQPTEGSVLLDGVDIRQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHirgnRIAMIFQEPMTSLNPL-HNIekqineVLGlhkglTGKVATQRTLELLELVGILEPHKRLKA---LP-HE---- 157
Cdd:TIGR03375 537 LRR----NIGYVPQDPRLFYGTLrDNI------ALG-----APYADDEEILRAAELAGVTEFVRRHPDgldMQiGErgrs 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHD---LNLVRRIAhrvcVMQKG 234
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMD--NRSEERFKDRLKRWLAGKTLVLVTHRtslLDLVDRII----VMDNG 675
|
...
gi 799207702 235 CIV 237
Cdd:TIGR03375 676 RIV 678
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
300-513 |
8.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 8.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGQQLDRLTQ-QQVRPLRREMQVVFQDPFGSL- 375
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTI-MQLLNglHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 ----------SPR-MCVSEIVGEGLRIHKmgtpaeqeaaiiaaLKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPR 444
Cdd:PRK13649 100 eetvlkdvafGPQnFGVSQEEAEALAREK--------------LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 445 LILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIF 513
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-237 |
1.35e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLPYPLarHP-SGTINYAGqdlLTLKEKTIRHIRgnRIAMIF-QE 101
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLTGIL--VPtSGEVRVLG---YVPFKRRKEFAR--RIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 --------PMTSLNplhnIEKQINEVlglhkgltGKVATQRTLEllELVGILEPHKRLKALPHELSGGQRQRVMIAMALA 173
Cdd:COG4586 105 sqlwwdlpAIDSFR----LLKAIYRI--------PDAEYKKRLD--ELVELLDLGELLDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 174 NEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-244 |
1.76e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFVTGDHHQR------------------VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLlpypLAR 66
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKS----TLLKL----IAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 67 --HP-SGTInyagqdlltlkektirHIRGnRIAMIFqEPMTSLNP----LHNIEkqINevlGLHKGLTGKVATQRTLELL 139
Cdd:COG1134 75 ilEPtSGRV----------------EVNG-RVSALL-ELGAGFHPeltgRENIY--LN---GRLLGLSRKEIDEKFDEIV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 140 ELVGILE----PHKRlkalpheLSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL------GM 209
Cdd:COG1134 132 EFAELGDfidqPVKT-------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ-------KKCLARIrelresGR 197
|
250 260 270
....*....|....*....|....*....|....*
gi 799207702 210 ALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCET 244
Cdd:COG1134 198 TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-218 |
2.07e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTInyagqdllTLKEKTIRHIRGNRiAMIFQEp 102
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-----HGSI--------TLDGKPVEGPGAER-GVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 103 mTSLNPLHNIekQINEVLGLHKGLTGKVA-TQRTLELLELVGILEPHKRLkalPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:PRK11248 79 -EGLLPWRNV--QDNVAFGLQLAGVEKMQrLEIAHQMLKKVGLEGAEKRY---IWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 799207702 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDL 218
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-239 |
2.17e-15 |
|
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: 74.27 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSveFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHpSGTINYAGQDLLTLkEKT 86
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQ-QGEITLDGVPVSDL-EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIrgnrIAMIFQEPmtslnplHNIEKQINEVLGLhkgltgkvatqrtlellelvgilephkrlkalphELSGGQRQRV 166
Cdd:cd03247 73 LSSL----ISVLNQRP-------YLFDTTLRNNLGR----------------------------------RFSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQ 239
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITE--RQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-238 |
2.41e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLArhpsGTINYAGQDLltlkEKTIRHIRGnRIAMIFQepMT 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS-PDA----GKITVLGVPV----PARARLARA-RIGVVPQ--FD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLNPLHNIEKQInEVLGLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:PRK13536 124 NLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 185 TTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGC-IVE 238
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRkIAE 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-507 |
2.53e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.77 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKST-----LGLAIlrliGSKGGIRFEGQQLdrltQQQVRPLRREMQVVFQdpFGSLS 376
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTtlrmlLGLTH----PDAGSISLCGEPV----PSRARHARQRVGVVPQ--FDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRMCVSEivgeGLRI--HKMGTPAEQEAAIIAALKEVGlDPESRHRYP-HEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:PRK13537 93 PDFTVRE----NLLVfgRYFGLSAAAARALVPPLLEFA-KLENKADAKvGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 454 ALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
274-529 |
2.92e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVwfpikkGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRL 352
Cdd:PRK09536 2 PMIDVSDLSV------EFGDTTV-----LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 353 TqqqVRPLRREMQVVFQDPfgSLSPRMCVSEIVGEGLRIH--KMGTPAEQEAAIIAALKEVGLDPESRHRYPHEFSGGQR 430
Cdd:PRK09536 71 S---ARAASRRVASVPQDT--SLSFEFDVRQVVEMGRTPHrsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 431 QRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAA 510
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
250
....*....|....*....
gi 799207702 511 GIFAAPQhgytrqlLEAAF 529
Cdd:PRK09536 225 DVLTADT-------LRAAF 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
305-526 |
3.32e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVRplrREMQVVFQDpfGSLSPRMCVSE 383
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVA---RRIGLLAQN--ATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 384 IVGEGLRIHK-MGTP--AEQEAAIIAALKEVGLDPESRHRYpHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:PRK10253 101 LVARGRYPHQpLFTRwrKEDEEAVTKAMQATGITHLADQSV-DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 461 RQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGdaagifaAPQHGYTRQLLE 526
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIE 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-243 |
3.34e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 8 EIRDLSVEfVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpyplARHP-----SGTINYAGQDLLTL 82
Cdd:COG0396 2 EIKNLHVS-VEG---KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--------MGHPkyevtSGSILLDGEDILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 kEKTIRHIRGnrIAMIFQEP-----MTSLNPLHNIEKQINEvlglhKGLTGKVATQRTLELLELVGIlePHKRLK-ALPH 156
Cdd:COG0396 70 -SPDERARAG--IFLAFQYPveipgVSVSNFLRTALNARRG-----EELSAREFLKLLKEKMKELGL--DEDFLDrYVNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDV--------TVQLKILEllkelqarlGMALLLISHDLNLVRRI-AHR 227
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalrivaeGVNKLRSP---------DRGILIITHYQRILDYIkPDF 210
|
250
....*....|....*.
gi 799207702 228 VCVMQKGCIVEQADCE 243
Cdd:COG0396 211 VHVLVDGRIVKSGGKE 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-234 |
3.74e-15 |
|
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: 74.81 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTInyagqdllTLKEKTIRHIRGNRIaMIFQEpmTS 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLIS-GLAQPTSGGV--------ILEGKQITEPGPDRM-VVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 LNPL----HNIEKQINEVLGlhkglTGKVATQRTL--ELLELVGILEP-HKRlkalPHELSGGQRQRVMIAMALANEPEL 178
Cdd:TIGR01184 65 LLPWltvrENIALAVDRVLP-----DLSKSERRAIveEHIALVGLTEAaDKR----PGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 179 LIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:TIGR01184 136 LLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
301-496 |
4.28e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTL--GLA-ILRLIGskGGIRFEGQQLDRLTQQQVR-----PLRremqvvfqdpf 372
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLlkVLAgVLRPTS--GTVRRAGGARVAYVPQRSEvpdslPLT----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 gslsprmcVSEIVGEGL--RIHKMGTPAEQ-EAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLD 449
Cdd:NF040873 74 --------VRDLVAMGRwaRRGLWRRLTRDdRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 450 EPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLM 496
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
274-509 |
5.69e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVwfpikkgflrtTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-----LRLIgsKGGIRFEGQQ 348
Cdd:CHL00131 6 PILEIKNLHA-----------SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKIL--EGDILFKGES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQQvrplRREMQV--VFQDPFgslsprmcvsEIVG----EGLRI-----HK-MG----TPAEQEAAIIAALKEVG 412
Cdd:CHL00131 73 ILDLEPEE----RAHLGIflAFQYPI----------EIPGvsnaDFLRLaynskRKfQGlpelDPLEFLEIINEKLKLVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 413 LDPESRHRYPHE-FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISH-----DLa 486
Cdd:CHL00131 139 MDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHyqrllDY- 216
|
250 260
....*....|....*....|...
gi 799207702 487 VVKALSHqlmVVKHGQVVEQGDA 509
Cdd:CHL00131 217 IKPDYVH---VMQNGKIIKTGDA 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-221 |
5.79e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhPSgtinyagqdlltlkE 84
Cdd:PRK09544 3 SLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA------PD--------------E 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 KTIRHIRGNRIAMIFQEpmTSLNPlhNIEKQINEVLGLHKGltgkVATQRTLELLELVgilEPHKRLKALPHELSGGQRQ 164
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPG----TKKEDILPALKRV---QAGHLIDAPMQKLSGGETQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:PRK09544 128 RVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-256 |
6.31e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILR-------LLPYPLArhpSGTINY 74
Cdd:PRK14243 6 GTETVLRTENLNVYY--GSF--LAVKNVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRV---EGKVTF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 75 AGQDLLTLKEKTIRHIRgnRIAMIFQEPmtslNPLhniEKQINE-------VLGLHKGLTGKVatQRTLELLELVGilEP 147
Cdd:PRK14243 75 HGKNLYAPDVDPVEVRR--RIGMVFQKP----NPF---PKSIYDniaygarINGYKGDMDELV--ERSLRQAALWD--EV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 148 HKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD--VTVQLKILELLKELQarlgMALLLISHDLNLVRRIA 225
Cdd:PRK14243 142 KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpiSTLRIEELMHELKEQ----YTIIIVTHNMQQAARVS 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 799207702 226 HRVCVM---------QKGCIVEQADCETLFQSPQHPYTQE 256
Cdd:PRK14243 218 DMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-239 |
7.77e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.20 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 29 VSFDIKRGETIALVGESGSGKSVTAHSILRLLPYplarhpSGTINYAGQDLLTLKEKTIRHIRgnriAMIFQepmtSLNP 108
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG------SGSIQFAGQPLEAWSAAELARHR----AYLSQ----QQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 109 LHNIEkqINEVLGLHKGlTGKVATQRTLELLELVGILEPHKRLKALPHELSGGQRQRVMIAMAL-----ANEPE--LLIA 181
Cdd:PRK03695 81 PFAMP--VFQYLTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 182 DEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:PRK03695 158 DEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-260 |
8.21e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 29 VSFDIKRGETIALVGESGSGKSVTAHSILRLLPYplarhpSGTINYAGQDLLTLKEKTIRHIRgnriAMIFQEPMTSLN- 107
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG------QGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 108 PLHniekqinEVLGLHKGLTGKVATQRTLeLLELVGILEPHKRLKALPHELSGGQRQRVMIAMAL------AN-EPELLI 180
Cdd:COG4138 85 PVF-------QYLALHQPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 181 ADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFqspqhpyTQELLAA 260
Cdd:COG4138 157 LDEPMNSLDVA-QQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-------TPENLSE 228
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
292-522 |
1.00e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.83 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 292 LRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL---RLIGSKGGIRFEGQQLDRLTQQQvRPlRREMQVVF 368
Cdd:TIGR01978 6 LHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGQDLLELEPDE-RA-RAGLFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 369 QDPfgSLSPRMCVSEIVGEGLRIH--KMGTPAEQEAAIIAALKE----VGLDPESRHRYPHE-FSGGQRQRIAIARALVL 441
Cdd:TIGR01978 84 QYP--EEIPGVSNLEFLRSALNARrsARGEEPLDLLDFEKLLKEklalLDMDEEFLNRSVNEgFSGGEKKRNEILQMALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISHDLAVVKALS----HQLMvvkHGQVVEQGDAAGIFAAPQ 517
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKpdyvHVLL---DGRIVKSGDVELAKELEA 237
|
....*
gi 799207702 518 HGYTR 522
Cdd:TIGR01978 238 KGYDW 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-234 |
1.13e-14 |
|
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: 71.33 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDhhQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpyplarhpsgtinyAGQDLLTlkEKT 86
Cdd:cd03221 1 IELENLSKTY--GG--KLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI--------------AGELEPD--EGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQepmtslnplhniekqinevlglhkgltgkvatqrtlellelvgilephkrlkalpheLSGGQRQRV 166
Cdd:cd03221 57 VTWGSTVKIGYFEQ---------------------------------------------------------LSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-234 |
1.55e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVtahsilrllpypLARHPSGTI--NYAGQDLLTLK 83
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKST------------LLRHLSGLItgDKSAGSHIELL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTI-------RHIRGNR--IAMIFQEpMTSLNPLHNIEKQINEVLGLHK------GLTGKVATQRTLELLELVGILE-P 147
Cdd:PRK09984 68 GRTVqregrlaRDIRKSRanTGYIFQQ-FNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGMVHfA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 148 HKRLKALphelSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHR 227
Cdd:PRK09984 147 HQRVSTL----SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCER 222
|
....*..
gi 799207702 228 VCVMQKG 234
Cdd:PRK09984 223 IVALRQG 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-189 |
1.64e-14 |
|
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: 72.20 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFV--TGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHP-SGTINYAGQDLltlK 83
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS----TLLNALAGRRTGLGvSGEVLINGRPL---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRhirgNRIAMIFQEPMtslnplhniekqinevlgLHKGLTgkvaTQRTLEL-LELVGIlephkrlkalphelSGGQ 162
Cdd:cd03213 77 KRSFR----KIIGYVPQDDI------------------LHPTLT----VRETLMFaAKLRGL--------------SGGE 116
|
170 180
....*....|....*....|....*..
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALD 189
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
305-515 |
1.92e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLglAILrLIG----SKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPFgSLSPRMC 380
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTL--ASL-LMGyyplTEGEIRLDGRPLSSLSHSV---LRQGVAMVQQDPV-VLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 381 VSEIVGEGLRIHKMGTpaeqeaaiiaALKEVGLD------PESRHRYPHE----FSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:PRK10790 433 ANVTLGRDISEEQVWQ----------ALETVQLAelarslPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 451 PTSALDRTVQRQVVELLRSLQAKynLTYLFISHDLA-VVKAlsHQLMVVKHGQVVEQGDAAGIFAA 515
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLStIVEA--DTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-243 |
2.05e-14 |
|
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: 71.79 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEfVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpyplARHPS-----GTINYAGQDLLT 81
Cdd:cd03217 1 LEIKDLHVS-VGG---KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--------MGHPKyevteGEILFKGEDITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 82 LkEKTIRHIRGnrIAMIFQEPMtslnplhniekqinEVLGLhkgltgkvatqRTLELLELVGIlephkrlkalphELSGG 161
Cdd:cd03217 69 L-PPEERARLG--IFLAFQYPP--------------EIPGV-----------KNADFLRYVNE------------GFSGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVtVQLKILELLKELQARLGMALLLISHDLNLVRRI-AHRVCVMQKGCIVEQA 240
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
...
gi 799207702 241 DCE 243
Cdd:cd03217 188 DKE 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-249 |
2.44e-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: 72.58 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKektiRHIRGnRIAMIF--QE 101
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV-----KPDSGKILLDGQDITKLP----MHKRA-RLGIGYlpQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 P-----MTslnplhnIEKQINEVLGLHKgLTGKVATQRTLELLELVGILEPHKRLKAlphELSGGQRQRVMIAMALANEP 176
Cdd:cd03218 84 AsifrkLT-------VEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKAS---SLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 177 ELLIADEPTTALD-VTVQLKILELLKELQarLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSP 249
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQDIQKIIKILKD--RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-245 |
2.98e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHhqRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLlpYPLArhpSGTINYAGQDLltlKEKT 86
Cdd:PRK11176 342 IEFRNVTFTYPGKEV--PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF--YDID---EGEILLDGHDL---RDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQEpmtslnpLHNIEKQI-NEVLGLHKGLTGKVATQRTLELLELVGILEPHKR-LKALPHE----LSG 160
Cdd:PRK11176 412 LASLR-NQVALVSQN-------VHLFNDTIaNNIAYARTEQYSREQIEEAARMAYAMDFINKMDNgLDTVIGEngvlLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQA 240
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
....*
gi 799207702 241 DCETL 245
Cdd:PRK11176 561 THAEL 565
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
307-529 |
3.65e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 307 FSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQVrplrreMQVVFQDPFGSLSPRMCVSEIV 385
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 386 GEGlRIHKMG----TPAEQEAAIIAALKEVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQR 461
Cdd:PRK15056 102 MMG-RYGHMGwlrrAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 462 QVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKhGQVVEQGDAAGIFAAPQhgytrqlLEAAF 529
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAEN-------LELAF 238
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-231 |
7.07e-14 |
|
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: 71.04 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 31 FDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQDlltlKEKTIRHIR--GNRIAMIFQEPMTSLNp 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP-----PAKGTVKVAGAS----PGKGWRHIGyvPQRHEFAWDFPISVAH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 109 lhniekqinEVLGLHKGLTG-----KVATQRTL-ELLELVGILEPHKRLKAlphELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:TIGR03771 71 ---------TVMSGRTGHIGwlrrpCVADFAAVrDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLD 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207702 183 EPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVCVM 231
Cdd:TIGR03771 139 EPFTGLDMPTQELLTELFIEL-AGAGTAILMTTHDLAQAMATCDRVVLL 186
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
300-516 |
7.51e-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: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTQQQvrplRREMQVVF--QDP--FGS 374
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGKILLDGQDITKLPMHK----RARLGIGYlpQEAsiFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSPR---MCVSEIVG--EGLRIHKMgtpaeqeaaiIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLD 449
Cdd:cd03218 90 LTVEeniLAVLEIRGlsKKEREEKL----------EELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 450 EPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAP 516
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-189 |
8.65e-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: 70.76 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 11 DLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplaRHP--SGTINYAGQDLLtlKEKTIR 88
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE----GGGttSGQILFNGQPRK--PDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 89 HIRGNRIAMIFQEPMTSLNPLHNIEkqineVLGLHKGLTGKVATQRT-LELLELVGILE-PHKRLKALphelSGGQRQRV 166
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTA-----ILRLPRKSSDAIRKKRVeDVLLRDLALTRiGGNLVKGI----SGGERRRV 152
|
170 180
....*....|....*....|...
gi 799207702 167 MIAMALANEPELLIADEPTTALD 189
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
292-507 |
9.87e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 292 LRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLTQQQ------VRPLRREMQ 365
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREgrlardIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 366 VVFQDpfGSLSPRMCVSEIVgeglRIHKMG-TP----------AEQEAAIIAALKEVGLdPESRHRYPHEFSGGQRQRIA 434
Cdd:PRK09984 90 YIFQQ--FNLVNRLSVLENV----LIGALGsTPfwrtcfswftREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 435 IARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-239 |
1.03e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKTirhiRGnrIAMIFQE--- 101
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVA-GLERITSGEIWIGGRVVNELEPAD----RD--IAMVFQNyal 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 -P-MTSLN-----------PLHNIEKQINEVlglhkgltgkvatQRTLELLELvgilephkrLKALPHELSGGQRQRVMI 168
Cdd:PRK11650 88 yPhMSVREnmayglkirgmPKAEIEERVAEA-------------ARILELEPL---------LDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 169 AMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGcIVEQ 239
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG-VAEQ 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-239 |
1.52e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 73.32 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 27 NNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDLLTLKEKTIRHIrgnrIAMIFQEpmTSL 106
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKS----TLARLL-FRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIVPQD--TVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 107 -NP--LHNI--------EKQINE----------VLGLHKGLtgkvATQrtlellelVGilephKR-LKalpheLSGGQRQ 164
Cdd:COG5265 444 fNDtiAYNIaygrpdasEEEVEAaaraaqihdfIESLPDGY----DTR--------VG-----ERgLK-----LSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 165 RVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQARlgmALLLISHDLNLVRRiAHRVCVMQKGCIVEQ 239
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDsRTERAIQAALREVARGR---TTLVIAHRLSTIVD-ADEILVLEAGRIVER 573
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
304-507 |
1.83e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.66 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQldrLTQQQVRPLRREMQVVFQDPfgslsprMCVS 382
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGeIRVNGRE---IGAYGLRELRRQFSMIPQDP-------VLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGLRIHKMGTPaeqeAAIIAALKEVGLdpesRHRYPHE--------------FSGGQRQRIAIARALVLKPR-LIL 447
Cdd:PTZ00243 1398 GTVRQNVDPFLEASS----AEVWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARALLKKGSgFIL 1469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 448 LDEPTSALDRTVQRQVVELLRSLQAKYnlTYLFISHDLAVVkALSHQLMVVKHGQVVEQG 507
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTV-AQYDKIIVMDHGAVAEMG 1526
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-234 |
2.14e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.02 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDnLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSV-----------TAHSIlRLLPYPLARHPS 69
Cdd:PRK11300 1 MSQP-LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTvfncltgfykpTGGTI-LLRGQHIEGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 70 GTInyAGQDLLtlkeKTIRHIRgnriamIFQEpMTSL-NPLHNIEKQINEvlGLHKGL--------TGKVATQRTLELLE 140
Cdd:PRK11300 75 HQI--ARMGVV----RTFQHVR------LFRE-MTVIeNLLVAQHQQLKT--GLFSGLlktpafrrAESEALDRAATWLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 141 LVGILEPHKRLKAlphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNL 220
Cdd:PRK11300 140 RVGLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
250
....*....|....
gi 799207702 221 VRRIAHRVCVMQKG 234
Cdd:PRK11300 217 VMGISDRIYVVNQG 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-189 |
2.15e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQD--LLTLKEktiRHIRGnrIAMIFQ 100
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-----RDAGNIIIDDEDisLLPLHA---RARRG--IGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPmtSLNPLHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGIlePHKRlKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK10895 86 EA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLR-DSMGQSLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 799207702 181 ADEPTTALD 189
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-234 |
2.96e-13 |
|
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: 72.16 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHHQRVvNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplARHpSGTINYAGQDLLTLK 83
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---GKF-EGNVFINGKPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 -EKTIRHirgnRIAMIfqepmtslnPLHNIEKQINEVLGLHKGLTGKVATQ-----RTLELLELVGILEPHKRLKA---- 153
Cdd:TIGR02633 330 pAQAIRA----GIAMV---------PEDRKRHGIVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVktas 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 --LP-HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVCV 230
Cdd:TIGR02633 397 pfLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLV 475
|
....
gi 799207702 231 MQKG 234
Cdd:TIGR02633 476 IGEG 479
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
303-502 |
3.70e-13 |
|
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: 66.70 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGSKggirfegqqldrltqqqvrplrremqvvfqdpfgslsprmcvs 382
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTL----LKLIAGE------------------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 EIVGEGlrihkmgtpaeqeaaiiaalkEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ 462
Cdd:cd03221 50 LEPDEG---------------------IVTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 799207702 463 VVELLRslqaKYNLTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:cd03221 109 LEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
304-495 |
6.11e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.90 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDrltqQQVRPLRREMQVVFQDPF--GSLS 376
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTL----LRILAglsppLAGRVLLNGGPLD----FQRDSIARGLLYLGHAPGikTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRmcvseivgEGLRIHKmgtPAEQEAAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:cd03231 90 VL--------ENLRFWH---ADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 799207702 457 RTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQL 495
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-238 |
7.15e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFvtGDHHqrVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PYplarhpSGTINYaGQD 78
Cdd:COG0488 313 KKVLELEGLSKSY--GDKT--LLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLagelePD------SGTVKL-GET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 79 LltlkektirhirgnRIAMIFQEpMTSLNPLHNIekqINEVLGLHKGLTgkvatqrtleLLELVGILE----PHKRLKAL 154
Cdd:COG0488 378 V--------------KIGYFDQH-QEELDPDKTV---LDELRDGAPGGT----------EQEVRGYLGrflfSGDDAFKP 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDV-TVQLkilellkelqarLGMAL-------LLISHDLNLVRRIAH 226
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA------------LEEALddfpgtvLLVSHDRYFLDRVAT 497
|
250
....*....|..
gi 799207702 227 RVCVMQKGCIVE 238
Cdd:COG0488 498 RILEFEDGGVRE 509
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-497 |
7.76e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 33 IKRGETIALVGESGSGKSvTAHSILrllpyplarhpSGTI-----NYAGQDLltlKEKTIRHIRGNRIAMIFQEPMT-SL 106
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKT-TAVKIL-----------SGELipnlgDYEEEPS---WDEVLKRFRGTELQNYFKKLYNgEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 107 NPLHNIE--KQINEVLglhKGLTGKVATqRTLE---LLELVGILEPHKRLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:PRK13409 161 KVVHKPQyvDLIPKVF---KGKVRELLK-KVDErgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 182 DEPTTALDVtVQlkilellkelqaRLGMA-----------LLLISHDLNLVRRIAHRVCVM--QKGC--IVeqadcetlf 246
Cdd:PRK13409 237 DEPTSYLDI-RQ------------RLNVArlirelaegkyVLVVEHDLAVLDYLADNVHIAygEPGAygVV--------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 247 qspQHP---------YTQELLAAE-----------PSGGPATNVIGPPLLEVDDLKVWFP-----IKKGFLRttvdyvka 301
Cdd:PRK13409 295 ---SKPkgvrvgineYLKGYLPEEnmrirpepiefEERPPRDESERETLVEYPDLTKKLGdfsleVEGGEIY-------- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 vdginfslpQGQTLGIVGESGSGKSTLglaiLRLIGskGGIR-FEGQQLDRLT----QQQVRPlRREMQVvfQDPFGSLS 376
Cdd:PRK13409 364 ---------EGEVIGIVGPNGIGKTTF----AKLLA--GVLKpDEGEVDPELKisykPQYIKP-DYDGTV--EDLLRSIT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRMCVS----EIVgEGLRIHKMgtpaeqeaaiiaalkevgLDpesrhRYPHEFSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:PRK13409 426 DDLGSSyyksEII-KPLQLERL------------------LD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 799207702 453 SALDrtV-QR-QVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMV 497
Cdd:PRK13409 482 AHLD--VeQRlAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-483 |
7.77e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.81 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 30 SFDIKRGETIALVGESGSGKSVtahsilrllpypLARHPSGTIN-YAGQdlltlkektiRHIRGNRIAMIFQEpmtSLNP 108
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA------------LARALAGELPlLSGE----------RQSQFSHITRLSFE---QLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 109 LHNIEKQINEVLGLHKGL--TGKVA----------TQRTLELLELVGI---LEphKRLKalphELSGGQRQRVMIAMALA 173
Cdd:PRK10938 78 LVSDEWQRNNTDMLSPGEddTGRTTaeiiqdevkdPARCEQLAQQFGItalLD--RRFK----YLSTGETRKTLLCQALM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 174 NEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMqkgciveqADCETLFQSPQHPY 253
Cdd:PRK10938 152 SEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL--------ADCTLAETGEREEI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 254 TQELLAAEPSGgpATNVIGPPLLEVDDLKVWFPIKKG----FLRT-TVDY--VKAVDGINFSLPQGQTLGIVGESGSGKS 326
Cdd:PRK10938 223 LQQALVAQLAH--SEQLEGVQLPEPDEPSARHALPANepriVLNNgVVSYndRPILHNLSWQVNPGEHWQIVGPNGAGKS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 327 TLgLAI------------LRLIGSKGG-----------IRFEGQQL--DRLTQQQVRplrremQVVFQDPFGSLSPRMCV 381
Cdd:PRK10938 301 TL-LSLitgdhpqgysndLTLFGRRRGsgetiwdikkhIGYVSSSLhlDYRVSTSVR------NVILSGFFDSIGIYQAV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 382 SEivgeglRIHKMgtpaeqeaaIIAALKEVGLDPESRHRYPHEFSGGQrQRIA-IARALVLKPRLILLDEPTSALD---R 457
Cdd:PRK10938 374 SD------RQQKL---------AQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDplnR 437
|
490 500
....*....|....*....|....*.
gi 799207702 458 TVQRQVVELLRSlQAKYNLtyLFISH 483
Cdd:PRK10938 438 QLVRRFVDVLIS-EGETQL--LFVSH 460
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-221 |
8.87e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 22 HQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpyplarhpsgtinyagqdlltlkektIRHIRGNRIAMIFQE 101
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL--------------------------AGALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMTSLNPlhniEKQINEVLGLHKGLTGKVatqrtlELLELVGILEPHKrLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:COG2401 92 PDNQFGR----EASLIDAIGRKGDFKDAV------ELLNAVGLSDAVL-WLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 799207702 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVI 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
275-520 |
1.03e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFPIKKGFL------RTTVDYVKAVDGINFSlpqGQTLGIVGESGSGKSTL--GLAILRLIGSKGG--IRF 344
Cdd:TIGR00955 11 FGRVAQDGSWKQLVSRLRgcfcreRPRKHLLKNVSGVAKP---GELLAVMGSSGAGKTTLmnALAFRSPKGVKGSgsVLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 345 EGQQLDRltqqqvrplrREMQV----VFQDP--FGSLSPR---MCVSEivgegLRIHKMGTPAEQEAAIIAALKEVGLDP 415
Cdd:TIGR00955 88 NGMPIDA----------KEMRAisayVQQDDlfIPTLTVRehlMFQAH-----LRMPRRVTKKEKRERVDEVLQALGLRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 416 --------ESRHRyphEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAV 487
Cdd:TIGR00955 153 cantrigvPGRVK---GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSE 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 799207702 488 VKALSHQLMVVKHGQVVEQG---DAAGIFAapQHGY 520
Cdd:TIGR00955 230 LFELFDKIILMAEGRVAYLGspdQAVPFFS--DLGH 263
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-236 |
1.11e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 27 NNVSFDIKRGETIALVGESGSGKSvtahSILRLLpyplarhpsgtinyAGQDLLTLKEKTIRHIRGNR-------IAMIF 99
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKS----TLLRMI--------------AGLEDITSGDLFIGEKRMNDvppaergVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 100 QEpmTSLNPLHNIEKqiNEVLGLHKGLTGKVATQRTLEllELVGILEPHKRLKALPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PRK11000 82 QS--YALYPHLSVAE--NMSFGLKLAGAKKEEINQRVN--QVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 180 IADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCI 236
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-248 |
1.20e-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: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHsiLRLLPYPLArhpSGTINYAGQDLLTLKEKT 86
Cdd:PRK10790 341 IDIDNVSFAY---RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS--LLMGYYPLT---EGEIRLDGRPLSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEPMTSLNPLH-NI-------EKQINEVLglhkgltgkvatqRTLELLELV-----GIlepHKRLKA 153
Cdd:PRK10790 413 LR----QGVAMVQQDPVVLADTFLaNVtlgrdisEEQVWQAL-------------ETVQLAELArslpdGL---YTPLGE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellkelQArlgmalllISHDLNLVRR------IAHR 227
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE----------QA--------IQQALAAVREhttlvvIAHR 534
|
250 260 270
....*....|....*....|....*....|
gi 799207702 228 ---------VCVMQKGCIVEQADCETLFQS 248
Cdd:PRK10790 535 lstiveadtILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
304-468 |
1.22e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRltqqqvrPLRREmQVVFQDPFGSLSPR 378
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTL----LRLIAgllppAAGTIKLDGGDIDD-------PDVAE-ACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIV--------GEGLRIHkmgtpaeqeaaiiAALKEVGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:PRK13539 88 LTVAENLefwaaflgGEELDIA-------------AALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170
....*....|....*...
gi 799207702 451 PTSALDRTVQRQVVELLR 468
Cdd:PRK13539 154 PTAALDAAAVALFAELIR 171
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-221 |
1.54e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.61 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKTIRHIR--GNRIAMifqe 101
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILA-GLLRPDSGEVRWNGTPLAEQRDEPHENILylGHLPGL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 pMTSLNPLHNIeKQINEVLGlhkgltgkvATQRTL-ELLELVGiLEPHKRLKAlpHELSGGQRQRVMIAMALANEPELLI 180
Cdd:TIGR01189 85 -KPELSALENL-HFWAAIHG---------GAQRTIeDALAAVG-LTGFEDLPA--AQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 799207702 181 ADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-234 |
2.12e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLlpYPLArhpsgtinYAGQDLLTLK 83
Cdd:PRK13549 257 EVILEVRNLTAWDPV-NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA--YPGR--------WEGEIFIDGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 84 EKTIRH----IRgNRIAMIfqepmtslnPLHNIEKQINEVLGLHKGLTGKVATQRTL-----ELLELVGILEPHKRLK-- 152
Cdd:PRK13549 326 PVKIRNpqqaIA-QGIAMV---------PEDRKRDGIVPVMGVGKNITLAALDRFTGgsridDAAELKTILESIQRLKvk 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 153 -ALPH----ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHR 227
Cdd:PRK13549 396 tASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDR 474
|
....*..
gi 799207702 228 VCVMQKG 234
Cdd:PRK13549 475 VLVMHEG 481
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-249 |
2.20e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTL-KEKTIRHIRGnriaMIFQEPMT 104
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL-----RPQKGKVLVSGIDTGDFsKLQGIRKLVG----IVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLnplhnIEKQINEVLGLH-KGLTGKVATQRTLELLELVGI-LEPHKRLKalPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:PRK13644 89 QF-----VGRTVEEDLAFGpENLCLPPIEIRKRVDRALAEIgLEKYRHRS--PKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 183 EPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVrRIAHRVCVMQKGCIVEQADCETLFQSP 249
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-189 |
2.50e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDL--LTLkektirHIRGNR-IAMIFQ 100
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV-----KPDSGRIFLDGEDIthLPM------HKRARLgIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EP-----MTslnplhnIEKQINEVLGLHKgLTGKVATQRTLELLELVGILepHKRlKALPHELSGGQRQRVMIAMALANE 175
Cdd:COG1137 86 EAsifrkLT-------VEDNILAVLELRK-LSKKEREERLEELLEEFGIT--HLR-KSKAYSLSGGERRRVEIARALATN 154
|
170
....*....|....
gi 799207702 176 PELLIADEPTTALD 189
Cdd:COG1137 155 PKFILLDEPFAGVD 168
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
305-514 |
3.50e-12 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 66.47 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS-KGGIRFEGQQLDRLTQQQvrpLRREMQVVFQDPF---GS----LS 376
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHT---LRSRLSIILQDPIlfsGSirfnLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 P-RMCVSEIVGEGLRIHKMgtpaeqeaaiIAALKEV--GLDPESRHRyPHEFSGGQRQRIAIARALVLKPRLILLDEPTS 453
Cdd:cd03288 117 PeCKCTDDRLWEALEIAQL----------KNMVKSLpgGLDAVVTEG-GENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 454 ALDRTVQRQVVELLrsLQAKYNLTYLFISHDLAVVKAlSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:cd03288 186 SIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-189 |
3.67e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILR----LLPYplarhpsgtinYAGq 77
Cdd:COG4178 358 SEDGALALEDLTLRTPDG---RPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWPY-----------GSG- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 78 dlltlkekTIRHIRGNRIAMIFQEPMTSLNPLHniekqinEVLgLHKGLTGKVATQRTLELLELVGILEPHKRL---KAL 154
Cdd:COG4178 419 --------RIARPAGARVLFLPQRPYLPLGTLR-------EAL-LYPATAEAFSDAELREALEAVGLGHLAERLdeeADW 482
|
170 180 190
....*....|....*....|....*....|....*
gi 799207702 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-189 |
4.27e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLARHPSGTIN--------------YAGQDLLTLKEKTIRH 89
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNgmpidakemraisaYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 90 irgnriAMIFQEpmtslnplhniekqineVLGLHKGLTGKVATQRTLELLELVGILEPHKRLKALPHE---LSGGQRQRV 166
Cdd:TIGR00955 119 ------HLMFQA-----------------HLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRL 175
|
170 180
....*....|....*....|...
gi 799207702 167 MIAMALANEPELLIADEPTTALD 189
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
266-507 |
5.65e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 266 PATNVIGPPLLEVDDlkvwfpIKKGFlrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRF 344
Cdd:PRK15439 2 QTSDTTAPPLLCARS------ISKQY-----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtLEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 345 EGQQLDRLTQQQVRPLrrEMQVVFQDPFgsLSPRMCVSEIVGEGLRIHKmgtpaEQEAAIIAALKEVG--LDPESrhryp 422
Cdd:PRK15439 71 GGNPCARLTPAKAHQL--GIYLVPQEPL--LFPNLSVKENILFGLPKRQ-----ASMQKMKQLLAALGcqLDLDS----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 423 hefSGG-----QRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMV 497
Cdd:PRK15439 137 ---SAGslevaDRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISV 212
|
250
....*....|
gi 799207702 498 VKHGQVVEQG 507
Cdd:PRK15439 213 MRDGTIALSG 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
304-502 |
6.29e-12 |
|
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: 64.80 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAIL----RLIGS---------------------KGGIRFeGQQLD-RLTQQQV 357
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLgeleKLSGSvsvpgsiayvsqepwiqngtiRENILF-GKPFDeERYEKVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 358 RP--LRREMQVVfqdPFGSLSprmcvseIVGEglrihkmgtpaeqeaaiiaalKEVGLdpesrhryphefSGGQRQRIAI 435
Cdd:cd03250 102 KAcaLEPDLEIL---PDGDLT-------EIGE---------------------KGINL------------SGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 436 ARALVLKPRLILLDEPTSALDRTVQRQVVE-LLRSLQAKyNLTYLFISHDLAVVKAlSHQLMVVKHGQ 502
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-249 |
9.46e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 36 GETIALVGESGSGKSvtahSILRLLpyplARH---PSGTINYAGQDLLTLKEKTIrhirGNRIAMIFQ-----EPMTsln 107
Cdd:PRK10575 37 GKVTGLIGHNGSGKS----TLLKML----GRHqppSEGEILLDAQPLESWSSKAF----ARKVAYLPQqlpaaEGMT--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 108 plhniekqINEVLGLHK-------GLTGKVATQRTLELLELVGilephkrLKALPHEL----SGGQRQRVMIAMALANEP 176
Cdd:PRK10575 102 --------VRELVAIGRypwhgalGRFGAADREKVEEAISLVG-------LKPLAHRLvdslSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 177 ELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLFQSP 249
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
299-514 |
1.02e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKST-LGLAILRLIGSKGGIRFEGQqlDRLTQQQVRPLRREMQVVfqdPFGS-LS 376
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTlLGTLCGDPRATSGRIVFDGK--DITDWQTAKIMREAVAIV---PEGRrVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRMCVSEIVGeglrihkMGTPAEQEAAIIAALKEV-GLDP---ESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPT 452
Cdd:PRK11614 93 SRMTVEENLA-------MGGFFAERDQFQERIKWVyELFPrlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 453 SALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFA 514
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
302-507 |
1.02e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGgirFEGQQLDRlTQQQVRPLRREMQVVFQDPFgsLSPRMCV 381
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILAN-NRKPTKQILKRTGFVTQDDI--LYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 382 SE--IVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRHRYPHEF----SGGQRQRIAIARALVLKPRLILLDEPTSAL 455
Cdd:PLN03211 158 REtlVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 799207702 456 DRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-236 |
1.16e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 66.99 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVEFVTGDH---HQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKTIr 88
Cdd:TIGR01842 317 LSVENVTIVPpggKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT-----SGSVRLDGADLKQWDRETF- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 89 hirGNRIAMIFQEpmtslnplhnIEkqinevlgLHKG--------LTGKVATQRTLELLELVGIlepHKRLKALPH---- 156
Cdd:TIGR01842 391 ---GKHIGYLPQD----------VE--------LFPGtvaeniarFGENADPEKIIEAAKLAGV---HELILRLPDgydt 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 -------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVrRIAHRVC 229
Cdd:TIGR01842 447 vigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKIL 524
|
....*..
gi 799207702 230 VMQKGCI 236
Cdd:TIGR01842 525 VLQDGRI 531
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
293-515 |
1.28e-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: 67.66 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 293 RTTVDYVkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS-KGGIRFEGQQLDRLTqqqVRPLRREMQVVFQDP 371
Cdd:TIGR00957 1295 REDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIG---LHDLRFKITIIPQDP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 F---GSLspRMCV-------SEIVGEGLRIHKMGTPAEQEAAiiaalkevGLDPESRHRyPHEFSGGQRQRIAIARALVL 441
Cdd:TIGR00957 1370 VlfsGSL--RMNLdpfsqysDEEVWWALELAHLKTFVSALPD--------KLDHECAEG-GENLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 442 KPRLILLDEPTSALDRTVQRQVVELLRSlQAKyNLTYLFISHDLAVVKALShQLMVVKHGQVVEQGDAAGIFAA 515
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRT-QFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
299-512 |
1.39e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.73 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI--GSKGGIRFEGQQLDRLTQQQVRPLrrEMQVVFQDPfgSLS 376
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTL-MKVLSGIhePTKGTITINNINYNKLDHKLAAQL--GIGIIYQEL--SVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 377 PRMCVSE--IVGEGLRIHKMGTP----AEQEAAIIAALKEVGLdpesrHRYPHEFSG----GQRQRIAIARALVLKPRLI 446
Cdd:PRK09700 93 DELTVLEnlYIGRHLTKKVCGVNiidwREMRVRAAMMLLRVGL-----KVDLDEKVAnlsiSHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 447 LLDEPTSALDRTVQRQVVELLRSLQaKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGI 512
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
295-503 |
1.64e-11 |
|
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: 64.88 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 295 TVDYVKA----VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLTQQQVR------------ 358
Cdd:cd03289 9 TAKYTEGgnavLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRkafgvipqkvfi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 359 ---PLRREMqvvfqDPFGSLSPRMC--VSEIVGEGLRIHKMgtpaeqeaaiIAALKEVGLDPesrhryPHEFSGGQRQRI 433
Cdd:cd03289 89 fsgTFRKNL-----DPYGKWSDEEIwkVAEEVGLKSVIEQF----------PGQLDFVLVDG------GCVLSHGHKQLM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 434 AIARALVLKPRLILLDEPTSALDRTVQRQVVELLRslQAKYNLTYLFISHDLAVVKAlSHQLMVVKHGQV 503
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
305-489 |
2.33e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG--IRFEGQQLDRLTQQQ-------------------------- 356
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhIVFKNEHTNDMTNEQdyqgdeeqnvgmknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 357 ------------------------VRPLRREMQVVFQDPfgsLSPRMCVSEIVgeglrihKMGTPAEQEAAIIAALKEVG 412
Cdd:PTZ00265 1267 gedstvfknsgkilldgvdicdynLKDLRNLFSIVSQEP---MLFNMSIYENI-------KFGKEDATREDVKRACKFAA 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 413 LDpESRHRYPHEF-----------SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFI 481
Cdd:PTZ00265 1337 ID-EFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
....*...
gi 799207702 482 SHDLAVVK 489
Cdd:PTZ00265 1416 AHRIASIK 1423
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
304-490 |
2.35e-11 |
|
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: 63.15 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQLDRLTQQQVRplrremQVVFQDPFGSLSPR 378
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTL----LRILAgllrpDSGEVRWNGTPLAEQRDEPHE------NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIHkmgtpAEQEAAIIAALKEVGLDPESrHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:TIGR01189 88 LSALENLHFWAAIH-----GGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|..
gi 799207702 459 VQRQVVELLRSLQAKYNLTYLFISHDLAVVKA 490
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
158-258 |
2.48e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
90 100
....*....|....*....|.
gi 799207702 238 EQAdcetlfqSPQHPYTQELL 258
Cdd:PRK10253 224 AQG-------APKEIVTAELI 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-189 |
3.15e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDlsVEFVTGDhhQRVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPYPlarhPSGTINYAGQDLL 80
Cdd:PRK10247 2 QENSPLLQLQN--VGYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISP----TSGTLLFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHirgnRIAMIFQEPM----TSLNPL---HNIEKQINEvlglhkgltgKVATQRTLELLELvgilePHKRLKA 153
Cdd:PRK10247 73 TLKPEIYRQ----QVSYCAQTPTlfgdTVYDNLifpWQIRNQQPD----------PAIFLDDLERFAL-----PDTILTK 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 799207702 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:PRK10247 134 NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
295-509 |
3.71e-11 |
|
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: 66.09 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 295 TVDYVKA----VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLTQQQvrpLRREMQVVFQD 370
Cdd:TIGR01271 1224 TAKYTEAgravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQT---WRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 PFgslsprmcvseIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHE-----------FSGGQRQRIAIARAL 439
Cdd:TIGR01271 1301 VF-----------IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLK-SVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 440 VLKPRLILLDEPTSALDrTVQRQVVEllRSL-QAKYNLTYLFISHDLAVVkaLSHQLMVVKHGQVVEQGDA 509
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLD-PVTLQIIR--KTLkQSFSNCTVILSEHRVEAL--LECQQFLVIEGSSVKQYDS 1434
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
137-497 |
3.99e-11 |
|
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: 65.58 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 137 ELLELVGILEphKRLKalphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTvQLKILELLKELQARLGMALLLISH 216
Cdd:COG1245 198 EKLGLENILD--RDIS----ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY-QRLNVARLIRELAEEGKYVLVVEH 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 217 DLNLVRRIAHRVCVM--QKGC--IVeqadcetlfqSPQHP-------YTQELLAAE-----------PSGGPATNVIGPP 274
Cdd:COG1245 271 DLAILDYLADYVHILygEPGVygVV----------SKPKSvrvginqYLDGYLPEEnvrirdepiefEVHAPRREKEEET 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 275 LLEVDDLKVWFP-----IKKGFLRttvdyvkavdginfslpQGQTLGIVGESGSGKSTLglaiLRLI--------GSKGG 341
Cdd:COG1245 341 LVEYPDLTKSYGgfsleVEGGEIR-----------------EGEVLGIVGPNGIGKTTF----AKILagvlkpdeGEVDE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 342 ---IRFEGQQLDRLTQQQVRPLRREmqvVFQDPFGSlspRMCVSEIVgEGLRIHKMgtpaeqeaaiiaalkevgLDpesr 418
Cdd:COG1245 400 dlkISYKPQYISPDYDGTVEEFLRS---ANTDDFGS---SYYKTEII-KPLGLEKL------------------LD---- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 419 hRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDrtV-QR-QVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLM 496
Cdd:COG1245 451 -KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VeQRlAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
.
gi 799207702 497 V 497
Cdd:COG1245 528 V 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-484 |
5.44e-11 |
|
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: 64.96 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLL-----PY--PLARHPSGTINYAGQDLLTLKEKTIRHI------- 90
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKS----TLLRIMagvdkDFngEARPQPGIKVGYLPQEPQLDPTKTVRENveegvae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 91 ------RGNRIAMIFQEPMTSLNPLhnIEKQ--INEVLGLHKGLTgkvaTQRTLELLELVGILEPHKrlkALPHELSGGQ 162
Cdd:TIGR03719 96 ikdaldRFNEISAKYAEPDADFDKL--AAEQaeLQEIIDAADAWD----LDSQLEIAMDALRCPPWD---ADVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 163 RQRVMIAMALANEPELLIADEPTTALDV-TVQLKILELlkelqARLGMALLLISHDLNLVRRIAHRVCVMQKG-CI---- 236
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAeSVAWLERHL-----QEYPGTVVAVTHDRYFLDNVAGWILELDRGrGIpweg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 237 -----VEQ--------------------ADCETLFQSPQHPYT---------QELLAAEPSGGPATNVI----GPPL--- 275
Cdd:TIGR03719 242 nysswLEQkqkrleqeekeesarqktlkRELEWVRQSPKGRQAkskarlaryEELLSQEFQKRNETAEIyippGPRLgdk 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 276 -LEVDDLKvwfpikKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGSK-----GGIRF-EGQQ 348
Cdd:TIGR03719 322 vIEAENLT------KAFGDKLL-----IDDLSFKLPPGGIVGVIGPNGAGKSTL----FRMITGQeqpdsGTIEIgETVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 349 LDRLTQQqvrplrREmqvvfqdpfgSLSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDPESRhryPHEFSGG 428
Cdd:TIGR03719 387 LAYVDQS------RD----------ALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKK---VGQLSGG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 429 QRQRIAIARALVLKPRLILLDEPTSALDrtvqrqvVELLRSL-QAKYNL--TYLFISHD 484
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALeEALLNFagCAVVISHD 499
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
304-505 |
6.16e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTqqqVRPLRREMQVVFQDP-FGSLSPRMCV 381
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQSPvLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 382 ---SEIVGEGL-----RIHkmgtpaeqeaaiiaaLKEV------GLDPESRHRyPHEFSGGQRQRIAIARALVLKPRLIL 447
Cdd:PLN03232 1331 dpfSEHNDADLwealeRAH---------------IKDVidrnpfGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 448 LDEPTSALD-RT---VQRQVVELLRSlqakynLTYLFISHDLAVVKALShQLMVVKHGQVVE 505
Cdd:PLN03232 1395 LDEATASVDvRTdslIQRTIREEFKS------CTMLVIAHRLNTIIDCD-KILVLSSGQVLE 1449
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
138-256 |
7.74e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 138 LLELVGIlEPHkrLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHD 217
Cdd:PRK11144 112 IVALLGI-EPL--LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHS 188
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 799207702 218 LNLVRRIAHRVCVMQKGCIVEQADCETLFQSPQ-HPYTQE 256
Cdd:PRK11144 189 LDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPWLPK 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
299-505 |
8.01e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.43 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI---GS-KGGIRFEGQQldrltqQQVRPLR----REMQVVFQD 370
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVyphGSyEGEILFDGEV------CRFKDIRdseaLGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 PfgSLSPRMCVSEIVGEGLRIHKMGTP--AEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILL 448
Cdd:NF040905 87 L--ALIPYLSIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLD-ESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 449 DEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVE 505
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
302-537 |
1.11e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTL---------GLAILRLIGSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPF 372
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 GslsprMCVSEIVGEGLRIHKM---GTPAEQEAAIIAALKEVGLDPESRhRYPHEFSGGQRQRIAIARAL---------V 440
Cdd:PRK13547 97 A-----FSAREIVLLGRYPHARragALTHRDGEIAWQALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 441 LKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFaapqhgy 520
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL------- 243
|
250
....*....|....*..
gi 799207702 521 TRQLLEAAFLVPAARVD 537
Cdd:PRK13547 244 TPAHIARCYGFAVRLVD 260
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
299-507 |
1.15e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTlGLAILRLIGSKGG---IRFEGQQLDRLT-------QQQVRPLRREmqvvf 368
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGrrpWRF*TWCANRRAlrrtig*HRPVR*GRRE----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 369 qdpfgSLSPRMCVSeIVGEGLRIHKmgtpAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILL 448
Cdd:NF000106 100 -----SFSGRENLY-MIGR*LDLSR----KDARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 449 DEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
274-489 |
1.15e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEV-DDLKVWFPIKK------GFLRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFE 345
Cdd:PTZ00265 366 PLVENnDDGKKLKDIKKiqfknvRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIIN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 346 GQQldRLTQQQVRPLRREMQVVFQDPF------------------------------------GSLSPRMCVSEIVGE-G 388
Cdd:PTZ00265 446 DSH--NLKDINLKWWRSKIGVVSQDPLlfsnsiknnikyslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAGDlN 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 389 LRIHKM-GTPAEQEAAIIAALKEVGLDPESRHRYPHEF-------------------SGGQRQRIAIARALVLKPRLILL 448
Cdd:PTZ00265 524 DMSNTTdSNELIEMRKNYQTIKDSEVVDVSKKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILIL 603
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 799207702 449 DEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVK 489
Cdd:PTZ00265 604 DEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-246 |
3.16e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 23 QRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL-PYPLARHPSG-TINYAGQDLLTLKEKtirhirgnrIAMIFQ 100
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGkPLDYSKRGLLALRQQ---------VATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPMTSLNpLHNIEKQINEVLgLHKGLTGKVATQRTLELLELVGIlephKRLKALPHE-LSGGQRQRVMIAMALANEPELL 179
Cdd:PRK13638 85 DPEQQIF-YTDIDSDIAFSL-RNLGVPEAEITRRVDEALTLVDA----QHFRHQPIQcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 180 IADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCETLF 246
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
305-500 |
3.29e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGirfegqqldrlTQQQVRPLRREM--QVVFQDPFGSLSprmcvs 382
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-----------VIKRNGKLRIGYvpQKLYLDTTLPLT------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 383 eiVGEGLRIHkmgtPAEQEAAIIAALKEVglDPESRHRYP-HEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQR 461
Cdd:PRK09544 86 --VNRFLRLR----PGTKKEDILPALKRV--QAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 799207702 462 QVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKH 500
Cdd:PRK09544 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-249 |
4.04e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 15 EFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpyplARH---PSGTINYAGQDLLTLKektIRHIR 91
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLI----QRHfdvSEGDIRFHDIPLTKLQ---LDSWR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 92 GnRIAMIFQEPMTSLNPLHNiekqiNEVLGLHKgltgkvATQRTLEllELVGILEPHKRLKALPH-----------ELSG 160
Cdd:PRK10789 389 S-RLAVVSQTPFLFSDTVAN-----NIALGRPD------ATQQEIE--HVARLASVHDDILRLPQgydtevgergvMLSG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 161 GQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQKGCIVEQA 240
Cdd:PRK10789 455 GQKQRISIARALLLNAEILILDDALSAVD--GRTEHQILHNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
....*....
gi 799207702 241 DCETLFQSP 249
Cdd:PRK10789 532 NHDQLAQQS 540
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-243 |
5.46e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpyplARHPS-----GTINYA 75
Cdd:CHL00131 2 NKNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--------AGHPAykileGDILFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 76 GQDLLTLkEKTIRHIRGnrIAMIFQEP------------MTSLNPLHnIEKQINEV--LGLHKGLTGKvatqrtlelLEL 141
Cdd:CHL00131 70 GESILDL-EPEERAHLG--IFLAFQYPieipgvsnadflRLAYNSKR-KFQGLPELdpLEFLEIINEK---------LKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 142 VGiLEPHKRLKALPHELSGGQRQRVMI-AMALAnEPELLIADEPTTALDV----TVQLKILELlkelqARLGMALLLISH 216
Cdd:CHL00131 137 VG-MDPSFLSRNVNEGFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIdalkIIAEGINKL-----MTSENSIILITH 209
|
250 260
....*....|....*....|....*...
gi 799207702 217 DLNLVRRIA-HRVCVMQKGCIVEQADCE 243
Cdd:CHL00131 210 YQRLLDYIKpDYVHVMQNGKIIKTGDAE 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-220 |
6.02e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.12 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVEFVTGDHHQRVV-NNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKTIRHI 90
Cdd:PRK13539 3 LEGEDLACVRGGRVLfSGLSFTLAAGEALVLTGPNGSGKT----TLLRLIA-GLLPPAAGTIKLDGGDIDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 91 RGNRIAMifqepMTSLNPLHNIEKQINeVLGlhkglTGKVATQRTLELLELVGILEphkrLKAlpHELSGGQRQRVMIA- 169
Cdd:PRK13539 78 LGHRNAM-----KPALTVAENLEFWAA-FLG-----GEELDIAAALEAVGLAPLAH----LPF--GYLSAGQKRRVALAr 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 799207702 170 MALANEPeLLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNL 220
Cdd:PRK13539 141 LLVSNRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGL 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
274-485 |
1.10e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLKVWFPikkGflrttvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLIGSK--GGIRFEGQQldr 351
Cdd:PRK10762 3 ALLQLKGIDKAFP---G--------VKALSGAALNVYPGRVMALVGENGAGKSTM-MKVLTGIYTRdaGSILYLGKE--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 352 ltqqqvrplrremqVVFQDPFGS-------------LSPRMCVS-------EIVGEGLRI--HKMgtpaeqEAAIIAALK 409
Cdd:PRK10762 68 --------------VTFNGPKSSqeagigiihqelnLIPQLTIAeniflgrEFVNRFGRIdwKKM------YAEADKLLA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 410 EVGLdPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDL 485
Cdd:PRK10762 128 RLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRL 201
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-246 |
1.11e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSVEFVTGdhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILrllpyplarhpsGTINYAGQDLL 80
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNG---HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALM------------GFVRLASGKIS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 81 TLKEKTIRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKVAT---QRTLELLELVGILEPHKRLKAlphE 157
Cdd:PRK15056 66 ILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKrdrQIVTAALARVDMVEFRHRQIG---E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVcVMQKGCIV 237
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
|
....*....
gi 799207702 238 EQADCETLF 246
Cdd:PRK15056 221 ASGPTETTF 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-233 |
1.38e-09 |
|
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: 57.89 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVEFVTGDHHQRVV-NNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEKTIR-- 88
Cdd:cd03231 1 LEADELTCERDGRALfSGLSFTLAAGEALQVTGPNGSGKT----TLLRILA-GLSPPLAGRVLLNGGPLDFQRDSIARgl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 89 ----HIRGNRIAMIFQEPMTSLNPLHNIEkQINEVLGlHKGLTGkvatqrtlellelvgilephkrLKALP-HELSGGQR 163
Cdd:cd03231 76 lylgHAPGIKTTLSVLENLRFWHADHSDE-QVEEALA-RVGLNG----------------------FEDRPvAQLSAGQQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQK 233
Cdd:cd03231 132 RRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGFK 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
408-504 |
1.53e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 408 LKEVGLDPESRHRyphEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTvqrqVVELLRSLQAKYNLTYLFISHDLAV 487
Cdd:PRK11147 143 LAQLGLDPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSF 215
|
90
....*....|....*..
gi 799207702 488 VKALSHQLMVVKHGQVV 504
Cdd:PRK11147 216 IRNMATRIVDLDRGKLV 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-234 |
2.37e-09 |
|
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: 57.09 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHQ-RVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQDLLTLKEK 85
Cdd:cd03250 1 ISVEDASFTWDSGEQETsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-----KLSGSVSVPGSIAYVSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIRH--IRGNriaMIFQEPMtslnplhniekqiNEvlglhkgltgkvatQRTLELLELVGiLEPHkrLKALPH------- 156
Cdd:cd03250 76 WIQNgtIREN---ILFGKPF-------------DE--------------ERYEKVIKACA-LEPD--LEILPDgdlteig 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 157 E----LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRiAHRVCVMQ 232
Cdd:cd03250 123 EkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLD 201
|
..
gi 799207702 233 KG 234
Cdd:cd03250 202 NG 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
311-484 |
2.37e-09 |
|
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: 56.23 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 311 QGQTLGIVGESGSGKSTLGLAILRLIGSKGGIrfegqqldrltqqqvrplrremqvvfqdpfgslsprmcVSEIVGEGLR 390
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--------------------------------------VIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 391 ihkmgtpaeqeaaiiaALKEVGLDPESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRS- 469
Cdd:smart00382 43 ----------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELr 106
|
170
....*....|....*....
gi 799207702 470 ----LQAKYNLTYLFISHD 484
Cdd:smart00382 107 llllLKSEKNLTVILTTND 125
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-237 |
2.41e-09 |
|
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: 59.76 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVE---FVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLarhpSGTINYAGQDLltlkektir 88
Cdd:COG4618 331 LSVEnltVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-PT----AGSVRLDGADL--------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 89 hirgnriamifqepmTSLNPlhniekqinEVLGLHKG--------LTGKVA----------TQRTLELLELVGIlepHKR 150
Cdd:COG4618 397 ---------------SQWDR---------EELGRHIGylpqdvelFDGTIAeniarfgdadPEKVVAAAKLAGV---HEM 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 151 LKALP-----------HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLN 219
Cdd:COG4618 450 ILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS 528
|
250
....*....|....*...
gi 799207702 220 LVrRIAHRVCVMQKGCIV 237
Cdd:COG4618 529 LL-AAVDKLLVLRDGRVQ 545
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
415-483 |
2.50e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 2.50e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 415 PESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDrtvqRQVVELLRSLQAKYNLTYLFISH 483
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-245 |
2.55e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARhPSGTINYAGQDLLTLKEKT-----IRHIRGNR------ 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALPR-TSGYVTLDGHEVVTRSPQDglangIVYISEDRkrdglv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 95 IAMIFQEPM--TSLNPLHNIEKQINevlglHKgltgkvATQRTLE-LLELVGILEPHkrLKALPHELSGGQRQRVMIAMA 171
Cdd:PRK10762 343 LGMSVKENMslTALRYFSRAGGSLK-----HA------DEQQAVSdFIRLFNIKTPS--MEQAIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 172 LANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCI-----VEQADCETL 245
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKL 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
2.74e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 1 MNQDNLIEIRDLSvefvtgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpYPLARHPSGTINYAGQDL- 79
Cdd:PRK09700 260 LAHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDIs 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 ----LTLKEKTIRHIRGNRIAMIFQePMTSLNPLHNIEKQINevLGLHKGLTGKVATQRTLEllelvgILEPHKRLKALP 155
Cdd:PRK09700 329 prspLDAVKKGMAYITESRRDNGFF-PNFSIAQNMAISRSLK--DGGYKGAMGLFHEVDEQR------TAENQRELLALK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 156 --------HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHR 227
Cdd:PRK09700 400 chsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDR 478
|
250
....*....|.
gi 799207702 228 VCVMQKGCIVE 238
Cdd:PRK09700 479 IAVFCEGRLTQ 489
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
287-485 |
2.80e-09 |
|
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: 57.34 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVDyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGQQLDRLTQQQVRPLRR--- 362
Cdd:cd03290 3 VTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRNRysv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 363 --------------EMQVVFQDPFGSLSPRMCVSEI-VGEGLRIHKMGTpaeqeaaiIAALKEVGLDpesrhrypheFSG 427
Cdd:cd03290 82 ayaaqkpwllnatvEENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGD--------QTEIGERGIN----------LSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 428 GQRQRIAIARALVLKPRLILLDEPTSAL-----DRTVQRQVVELLRSLQAkynlTYLFISHDL 485
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALdihlsDHLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-503 |
3.12e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLpYPLARHPSGTINYAGQDlltLKEKTIRHIRGNRIAMIFQEpm 103
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKS----TLLKCL-FGIYQKDSGSILFQGKE---IDFKSSKEALENGISMVHQE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 tsLNPLHNIEKQINEVLGLH--KGL--TGKVATQRTLELLELVGI-LEPHKRLKalphELSGGQRQRVMIAMALANEPEL 178
Cdd:PRK10982 82 --LNLVLQRSVMDNMWLGRYptKGMfvDQDKMYRDTKAIFDELDIdIDPRAKVA----TLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 179 LIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQADCE--TLFQSPQHPYTQE 256
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAglTMDKIIAMMVGRS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 257 LLAAEPsggPATNVIGPPLLEVDDLkvwfpikkgflrtTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI 336
Cdd:PRK10982 235 LTQRFP---DKENKPGEVILEVRNL-------------TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 337 GSKGG-IRFEGQQLDRLTQQQ--------VRPLRREMQVV----------------FQDPFGSLSPRMCVSEI--VGEGL 389
Cdd:PRK10982 299 EKSAGtITLHGKKINNHNANEainhgfalVTEERRSTGIYayldigfnslisnirnYKNKVGLLDNSRMKSDTqwVIDSM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 390 RIHkmgTPaeqeaaiiaalkevgldpeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRS 469
Cdd:PRK10982 379 RVK---TP-------------------GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE 436
|
490 500 510
....*....|....*....|....*....|....
gi 799207702 470 LqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK10982 437 L-AKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
300-517 |
3.25e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDRLtqqqvrPL----RREMQVVFQDPfgS 374
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGnIIIDDEDISLL------PLharaRRGIGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSPRMCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSA 454
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 455 LDRTVQ---RQVVELLRSlqakYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGIFAAPQ 517
Cdd:PRK10895 168 VDPISVidiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-225 |
3.87e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEfvTGDHhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQDLLTLKEK 85
Cdd:PRK13538 1 MLEARNLACE--RDER--ILFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILA-GLARPDAGEVLWQGEPIRRQRDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 TIR------HIRGnriamIFQEpmtsLNPLHNiekqinevLGLHKGLTGKVATQRTLELLELVGIlepHKRLKALPHELS 159
Cdd:PRK13538 72 YHQdllylgHQPG-----IKTE----LTALEN--------LRFYQRLHGPGDDEALWEALAQVGL---AGFEDVPVRQLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNL----VRRIA 225
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVasdkVRKLR 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
304-505 |
4.61e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGQQLDRLTqqqVRPLRREMQVVFQ------------- 369
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKFG---LMDLRKVLGIIPQapvlfsgtvrfnl 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 370 DPFGSLSprmcvSEIVGEGL-RIHkmgtpaeqeaaiiaaLKEV------GLDPESRHRyPHEFSGGQRQRIAIARALVLK 442
Cdd:PLN03130 1334 DPFNEHN-----DADLWESLeRAH---------------LKDVirrnslGLDAEVSEA-GENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 443 PRLILLDEPTSALD-RT---VQRQVVELLRSlqakynLTYLFISHDLAVVKAlSHQLMVVKHGQVVE 505
Cdd:PLN03130 1393 SKILVLDEATAAVDvRTdalIQKTIREEFKS------CTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
305-537 |
7.87e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGQQLDRLTQ-----------QQVRPlrremqvVFQDPfg 373
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAaelarhraylsQQQTP-------PFAMP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 slsprmcvseiVGEGLRIHK-MGTPAEQEAAIIAALKE-VGLDPEsRHRYPHEFSGG--QRQRIA-----IARALVLKPR 444
Cdd:PRK03695 86 -----------VFQYLTLHQpDKTRTEAVASALNEVAEaLGLDDK-LGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 445 LILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGdaagifaAPQHGYTRQL 524
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG-------RRDEVLTPEN 225
|
250
....*....|...
gi 799207702 525 LEAAFLVPAARVD 537
Cdd:PRK03695 226 LAQVFGVNFRRLD 238
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
273-456 |
1.16e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.81 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 273 PPLLEVDDLKvwfpikKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGQQLDR 351
Cdd:COG1137 1 MMTLEAENLV------KSYGKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGrIFLDGEDITH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 352 LtqqqvrPL----RREMQVVFQDP--FGSLSPR---MCVseivgegLRIHKMgTPAEQEAAIIAALKEVGLDpESRHRYP 422
Cdd:COG1137 70 L------PMhkraRLGIGYLPQEAsiFRKLTVEdniLAV-------LELRKL-SKKEREERLEELLEEFGIT-HLRKSKA 134
|
170 180 190
....*....|....*....|....*....|....
gi 799207702 423 HEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-189 |
1.66e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 10 RDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVtahsILRLLPyplARHPSGTINyaGQDLLTLKEKTIRH 89
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLA---GRKTAGVIT--GEILINGRPLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 90 IRgnRIAMIFQepmtslNPLHNIEKQINEVLglhkgltgkvatqrtlellelvgilephkRLKALPHELSGGQRQRVMIA 169
Cdd:cd03232 78 QR--STGYVEQ------QDVHSPNLTVREAL-----------------------------RFSALLRGLSVEQRKRLTIG 120
|
170 180
....*....|....*....|
gi 799207702 170 MALANEPELLIADEPTTALD 189
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLD 140
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-216 |
1.71e-08 |
|
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: 54.08 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVefVTGDHHqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLArhpSGTINYAgqdlltlke 84
Cdd:cd03223 1 IELENLSL--ATPDGR-VLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRALAglWPWG---SGRIGMP--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 85 ktirhiRGNRIAMIFQEP-MTSLNplhniekqinevlglhkgltgkvatqrtleLLELVgilephkrlkALP--HELSGG 161
Cdd:cd03223 62 ------EGEDLLFLPQRPyLPLGT------------------------------LREQL----------IYPwdDVLSGG 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKelqaRLGMALLLISH 216
Cdd:cd03223 96 EQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-222 |
1.80e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYpLARHPSGTINYagQDLLTLKEKTIRHIRgNRIAMIFQEPMT 104
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIER-LYDPTEGDIII--NDSHNLKDINLKWWR-SKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 --------------SLNPLHNIEKQINE---------------VLGLHKGLTGKVATQRTLELL------------ELVG 143
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEALSNYYNEdgndsqenknkrnscRAKCAGDLNDMSNTTDSNELIemrknyqtikdsEVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 144 ILEP---HKRLKALP-----------HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGM 209
Cdd:PTZ00265 552 VSKKvliHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250
....*....|...
gi 799207702 210 ALLLISHDLNLVR 222
Cdd:PTZ00265 632 ITIIIAHRLSTIR 644
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-503 |
2.11e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHpSGTINYAG--------QDLLTLKEKTIRH-IRGNRI 95
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKS----TLLALLKNEISAD-GGSYTFPGnwqlawvnQETPALPQPALEYvIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 96 AMIFQEPMTSLNPlHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGILEPhkRLKALPHELSGGQRQRVMIAMALANE 175
Cdd:PRK10636 91 YRQLEAQLHDANE-RNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNE--QLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 176 PELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVRRIAHRVCVMQKGCIVEQ---------------A 240
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSLFEYtgnyssfevqratrlA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 241 DCETLFQSPQHPYTQ----------------------------ELLAAEPSGGP------ATNVIGPPLLEVDDlkvwfp 286
Cdd:PRK10636 244 QQQAMYESQQERVAHlqsyidrfrakatkakqaqsrikmlermELIAPAHVDNPfhfsfrAPESLPNPLLKMEK------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 287 IKKGFLRTTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTL------GLAILR-LIGSKGGIR---FEGQQLDRLT--- 353
Cdd:PRK10636 318 VSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLikllagELAPVSgEIGLAKGIKlgyFAQHQLEFLRade 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 354 ---QQQVRPLRREMQVVFQDPFGslsprmcvseivGEGLRIHKMGtpaeqeaaiiaalkevglDPESRhrypheFSGGQR 430
Cdd:PRK10636 393 splQHLARLAPQELEQKLRDYLG------------GFGFQGDKVT------------------EETRR------FSGGEK 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 431 QRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAkynlTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
298-489 |
2.25e-08 |
|
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: 53.87 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 298 YVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFegqqldrltqqqvRPLRREMQVVFQDPFGSLSp 377
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISF-------------LPKFSRNKLIFIDQLQFLI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 rmcvseivgeglrihkmgtpaeqeaaiiaalkEVGLDPESRHRYPHEFSGGQRQRIAIARALV--LKPRLILLDEPTSAL 455
Cdd:cd03238 73 --------------------------------DVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....
gi 799207702 456 DRTVQRQVVELLRSLQAKYNlTYLFISHDLAVVK 489
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLS 153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-189 |
2.41e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHhqRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyplarhPSgtinyAGQdlltlkekt 86
Cdd:NF033858 267 IEARGLTMRF--GDF--TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP------AS-----EGE--------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 irhirgnriAMIFQEPMTSlnplHNIE--KQI----------NEV-----LGLHK---GLTGKVATQRTLELLELVGiLE 146
Cdd:NF033858 323 ---------AWLFGQPVDA----GDIAtrRRVgymsqafslyGELtvrqnLELHArlfHLPAAEIAARVAEMLERFD-LA 388
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 799207702 147 PHkrLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:NF033858 389 DV--ADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
302-511 |
9.96e-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: 53.18 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSlpQGQTLGIVGESGSGKSTLglaiLRLIGskGGIRFEGQQLDRLTQ------QQVRPlRREMQVvfQDPFGSL 375
Cdd:cd03237 17 VEGGSIS--ESEVIGILGPNGIGKTTF----IKMLA--GVLKPDEGDIEIELDtvsykpQYIKA-DYEGTV--RDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 376 SPRMCV-----SEIvgeglrihkmgtpaeqeaaiiaaLKEVGLDPESRHRYPhEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:cd03237 86 TKDFYThpyfkTEI-----------------------AKPLQIEQILDREVP-ELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 799207702 451 PTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKhGQVVEQGDAAG 511
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVANP 201
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
274-508 |
1.19e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 274 PLLEVDDLkvWFPIKKGflrttvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGQQL--- 349
Cdd:PRK13545 20 PFDKLKDL--FFRSKDG------EYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKGSAAlia 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 350 ------DRLTQQQVRPLRREMQVVFQDPFGSLSPRmcVSEIVGEGLRIHKmgtPAEQeaaiiaalkevgldpesrhryph 423
Cdd:PRK13545 92 issglnGQLTGIENIELKGLMMGLTKEKIKEIIPE--IIEFADIGKFIYQ---PVKT----------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 424 eFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PRK13545 144 -YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
....*
gi 799207702 504 VEQGD 508
Cdd:PRK13545 222 KEYGD 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
305-490 |
1.27e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGQQL--DRLTQQQvrplrremQVVFQDPFGSLSP 377
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTL----LKLIAgllnpEKGEILFERQSIkkDLCTYQK--------QLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RMCVSEIVgeGLRIHKMGTPAEQEAAIIAALKEVGLDpesrhrYP-HEFSGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:PRK13540 88 YLTLRENC--LYDIHFSPGAVGITELCRLFSLEHLID------YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....
gi 799207702 457 RTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKA 490
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
307-498 |
1.33e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 307 FSLP---QGQTLGIVGESGSGKSTLgLAIL--RLI---------GSKGGI--RFEGQQL----DRLTQQQVRPLRReMQV 366
Cdd:PRK13409 91 YGLPipkEGKVTGILGPNGIGKTTA-VKILsgELIpnlgdyeeePSWDEVlkRFRGTELqnyfKKLYNGEIKVVHK-PQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 367 VFQDPfgslsprMCVSEIVGEGL-RIHKMGtpaeqeaAIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRL 445
Cdd:PRK13409 169 VDLIP-------KVFKGKVRELLkKVDERG-------KLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 446 ILLDEPTSALDrTVQR-QVVELLRSLQAKYNLtyLFISHDLAVVKALSHQLMVV 498
Cdd:PRK13409 234 YFFDEPTSYLD-IRQRlNVARLIRELAEGKYV--LVVEHDLAVLDYLADNVHIA 284
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
307-492 |
1.61e-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: 52.75 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 307 FSLP---QGQTLGIVGESGSGKSTlGLAIL--RLIGSKGGIR-----------FEGQQL----DRLTQQQVRPLRREMQV 366
Cdd:cd03236 18 HRLPvprEGQVLGLVGPNGIGKST-ALKILagKLKPNLGKFDdppdwdeildeFRGSELqnyfTKLLEGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 367 vfqdpfgSLSPRMcVSEIVGEGL-RIHKMGTpaeqeaaIIAALKEVGLDPeSRHRYPHEFSGGQRQRIAIARALVLKPRL 445
Cdd:cd03236 97 -------DLIPKA-VKGKVGELLkKKDERGK-------LDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 446 ILLDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVVKALS 492
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLS 206
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-245 |
2.06e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGK---SVTAHsilrlLPYPLA-RHPSGTINY-AGQDL 79
Cdd:NF000106 12 NAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**rgALPAH-----V*GPDAgRRPWRF*TWcANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 LTLKEKTIRHIRGNRiamifQEPMTSLNPLHNIEKQINevlglhkgLTGKVATQRTLELLELVGILEPHKRLKAlphELS 159
Cdd:NF000106 83 LRRTIG*HRPVR*GR-----RESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAA---KYS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQlKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR-NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
....*.
gi 799207702 240 ADCETL 245
Cdd:NF000106 226 GKVDEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-190 |
2.25e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 32 DIKRGETIALVGESGSGKSvTAHSIL--RLLPYPLARHPSGTINYAGQDLLTLKEKTIRHIRGNRIAMIFQEPMtslnpl 109
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKT-TFAKILagVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRSANTDDFGSSY------ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 110 hnIEKQINEVLGLHKgltgkvatqrtleLLElvgilephKRLKalphELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG1245 435 --YKTEIIKPLGLEK-------------LLD--------KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
.
gi 799207702 190 V 190
Cdd:COG1245 488 V 488
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
299-512 |
2.53e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLIGSK--GGIRFEGQQLDRLTQQQ-----VRPLRREMQVVFQDp 371
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTL-LKCLFGIYQKdsGSILFQGKEIDFKSSKEalengISMVHQELNLVLQR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 372 fgSLSPRMCVSEIVGEGLRI--HKMgtpaeqEAAIIAALKEVGLDPESRHRYPhEFSGGQRQRIAIARALVLKPRLILLD 449
Cdd:PRK10982 89 --SVMDNMWLGRYPTKGMFVdqDKM------YRDTKAIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 450 EPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQGDAAGI 512
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
302-507 |
2.60e-07 |
|
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: 53.80 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAIL----RLIGS---KGGIRFEGQQldrlTQQQVRPLRRemQVVF----QD 370
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLaemdKVEGHvhmKGSVAYVPQQ----AWIQNDSLRE--NILFgkalNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 PFGSLSPRMCVS----EIVGEGLRIHkmgtpaeqeaaiiaaLKEVGLDpesrhrypheFSGGQRQRIAIARALVLKPRLI 446
Cdd:TIGR00957 728 KYYQQVLEACALlpdlEILPSGDRTE---------------IGEKGVN----------LSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 447 LLDEPTSALDRTVQRQVVE-LLRSLQAKYNLTYLFISHDLAVVKALSHqLMVVKHGQVVEQG 507
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDV-IIVMSGGKISEMG 843
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
424-517 |
3.04e-07 |
|
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: 50.65 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 424 EFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHgqv 503
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG--- 147
|
90
....*....|....
gi 799207702 504 veQGDAAGIFAAPQ 517
Cdd:cd03222 148 --EPGVYGIASQPK 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
424-498 |
3.33e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 3.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 799207702 424 EFSGGQRQRIAIARALVLKPRLILLDEPTSALDrTVQR-QVVELLRSLqAKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-IYQRlNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
302-483 |
3.47e-07 |
|
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: 52.83 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGS----KGGirfegqqldRLTqqqvRPLRREMQVVFQDPF---GS 374
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSL----FRILGElwpvYGG---------RLT----KPAKGKLFYVPQRPYmtlGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 375 LSPR----MCVSEIVGEGLRIHKMGTPAEQEAAIIAALKEVGLDpeSRHRYPHEFSGGQRQRIAIARALVLKPRLILLDE 450
Cdd:TIGR00954 531 LRDQiiypDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWS--AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 799207702 451 PTSALDRTVQRQVVELLRslqaKYNLTYLFISH 483
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-245 |
3.66e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVefvtgdHHQ-----RVVNNVSFDIKRGETIALVGESGSGKSVTAHSIL-RllPYplARHPSGTINYAGQ 77
Cdd:NF040905 255 EVVFEVKNWTV------YHPlhperKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgR--SY--GRNISGTVFKDGK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 78 DLLTlkeKTIRHIRGNRIA----------MIFQEPM---TSLNPLHNIEKqiNEVLGLHKGLtgKVATQ-------RTLE 137
Cdd:NF040905 325 EVDV---STVSDAIDAGLAyvtedrkgygLNLIDDIkrnITLANLGKVSR--RGVIDENEEI--KVAEEyrkkmniKTPS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 138 LLELVGilephkrlkalphELSGGQRQRVMIAMALANEPELLIADEPTTALDV-------TVqlkilellKELQARLGMA 210
Cdd:NF040905 398 VFQKVG-------------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyeiyTI--------INELAAEGKG 456
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 799207702 211 LLLISHDLNLVRRIAHRVCVMQKGCIV-----EQADCETL 245
Cdd:NF040905 457 VIVISSELPELLGMCDRIYVMNEGRITgelprEEASQERI 496
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
305-465 |
3.83e-07 |
|
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: 53.38 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSE 383
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 384 IVGE---GLRIHKMGTPaeqeaaiiaaLKEVGLdpesrhryphEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQ 460
Cdd:TIGR01271 525 CQLEediALFPEKDKTV----------LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....*
gi 799207702 461 RQVVE 465
Cdd:TIGR01271 585 KEIFE 589
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-223 |
4.22e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 4 DNLIEIRDLSVEFVTGDHhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL----------------------- 60
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 61 ---------------PYPLARHPSGTINYA-----GQDLL---TLKEKTIRHIRgNRIAMIFQEPMtslnpLHNIekQIN 117
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnEFSLTKEGGSGEDSTvfknsGKILLdgvDICDYNLKDLR-NLFSIVSQEPM-----LFNM--SIY 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 118 EVLGLHKGLTGKVATQRTLELLELVGILE--PHK---RLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTV 192
Cdd:PTZ00265 1314 ENIKFGKEDATREDVKRACKFAAIDEFIEslPNKydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270
....*....|....*....|....*....|.
gi 799207702 193 QLKILELLKELQARLGMALLLISHDLNLVRR 223
Cdd:PTZ00265 1394 EKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
303-470 |
5.40e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTL--GLAILRLIGS-KGGIRFEGQQLDRltqqqvrPLRREMQVVFQDP--FGSLSP 377
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLldVLAGRKTAGViTGEILINGRPLDK-------NFQRSTGYVEQQDvhSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 378 RmcvseivgEGLRIHkmgtpaeqeaaiiAALKevGLDPEsrhryphefsggQRQRIAIARALVLKPRLILLDEPTSALDR 457
Cdd:cd03232 97 R--------EALRFS-------------ALLR--GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170
....*....|...
gi 799207702 458 TVQRQVVELLRSL 470
Cdd:cd03232 142 QAAYNIVRFLKKL 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-234 |
5.92e-07 |
|
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: 52.71 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFdiKRGETIALVGESGSGKSVTAHSILRLLPyplarHPSGTINYAGQDLltlkEKTIRHIRGNriamifqepmTSLN 107
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLVGGKDI----ETNLDAVRQS----------LGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 108 PLHNI---EKQINEVLGLHKGLTGKVATQRTLEL---LELVGIlepHKRLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:TIGR01257 1009 PQHNIlfhHLTVAEHILFYAQLKGRSWEEAQLEMeamLEDTGL---HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 799207702 182 DEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:TIGR01257 1086 DEPTSGVDPYSR--RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-222 |
6.04e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 21 HHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPyPLARHPSGTINYAGQ----DLLTLKEKtirhirgnria 96
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKT----TLLKLIA-GLLNPEKGEILFERQsikkDLCTYQKQ----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 97 MIFQEPMTSLNPlhNIEKQINEVLGLHKGLTgkvatqrTLELLELVGILEPHKRLKALPHELSGGQRQRVMIAMALANEP 176
Cdd:PRK13540 76 LCFVGHRSGINP--YLTLRENCLYDIHFSPG-------AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 799207702 177 ELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISH-DLNLVR 222
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAK-GGAVLLTSHqDLPLNK 192
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-254 |
6.52e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.68 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFvtGDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKT 86
Cdd:cd03288 20 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEP-MTSLNPLHNIEKQInevlglhkgltgKVATQRTLELLElvgILEPHKRLKALPHEL------- 158
Cdd:cd03288 93 LR----SRLSIILQDPiLFSGSIRFNLDPEC------------KCTDDRLWEALE---IAQLKNMVKSLPGGLdavvteg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 159 ----SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVRRiAHRVCVMQKG 234
Cdd:cd03288 154 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAHRVSTILD-ADLVLVLSRG 230
|
250 260
....*....|....*....|
gi 799207702 235 CIVEQADCETLFQSPQHPYT 254
Cdd:cd03288 231 ILVECDTPENLLAQEDGVFA 250
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-216 |
6.58e-07 |
|
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: 52.06 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 2 NQDNLIEIRDLSVEFVTGDhhqRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLP--YPLarhpsgtinYAGqdL 79
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPNGD---VLIESLSFEVPSGNNLLICGPNGCGKS----SLFRILGelWPV---------YGG--R 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 80 LTLKEKtirhirgNRIAMIFQEPMTSLNPLHN-------IEKQINevlglhKGLTGKVATQrTLELLELVGILEPHKRLK 152
Cdd:TIGR00954 509 LTKPAK-------GKLFYVPQRPYMTLGTLRDqiiypdsSEDMKR------RGLSDKDLEQ-ILDNVQLTHILEREGGWS 574
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 153 ALPH---ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKelqaRLGMALLLISH 216
Cdd:TIGR00954 575 AVQDwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
426-507 |
1.23e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVE--LLRSLQAKynlTYLFISHDLAVvkaLSH--QLMVVKHG 501
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHF---LSQvdRIILVHEG 815
|
....*.
gi 799207702 502 QVVEQG 507
Cdd:PLN03130 816 MIKEEG 821
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
426-502 |
1.58e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQ------RIAIARALVLKPRLILLDEPTSALDR-TVQRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 799207702 499 KHGQ 502
Cdd:cd03240 197 KDGR 200
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-190 |
1.85e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 6 LIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLArhpSGTINYAGQDLLTLKEK 85
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT---GGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 86 tirHIRGNRIAMIFQEPMtSLNPLHN---IEKQINEVLglhkgltgKVATQRTLELLELVGILEPHKRLKALPHEL---- 158
Cdd:PRK09580 74 ---DRAGEGIFMAFQYPV-EIPGVSNqffLQTALNAVR--------SYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrs 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 799207702 159 -----SGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:PRK09580 142 vnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDI 178
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-263 |
1.90e-06 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 45.82 E-value: 1.90e-06
10 20
....*....|....*....|....*...
gi 799207702 236 IVEQADCETLFQSPQHPYTQELLAAEPS 263
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPT 29
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
256-484 |
2.13e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 256 ELLAAEPSGGPATNVI----GPPL----LEVDDLKvwfpikKGF----LrttvdyvkaVDGINFSLPQGQTLGIVGESGS 323
Cdd:PRK11819 297 ELLSEEYQKRNETNEIfippGPRLgdkvIEAENLS------KSFgdrlL---------IDDLSFSLPPGGIVGIIGPNGA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 324 GKSTLglaiLRLIGSK-----GGIRF-EGQQLDRLTQQqvrplrREmqvvfqdpfgSLSPRMCVSEIVGEGLRIHKMGTp 397
Cdd:PRK11819 362 GKSTL----FKMITGQeqpdsGTIKIgETVKLAYVDQS------RD----------ALDPNKTVWEEISGGLDIIKVGN- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 398 aeqeaaiiaalKEVgldpESRhRYPHEF--------------SGGQRQRIAIARALVLKPRLILLDEPTSALDrtvqrqv 463
Cdd:PRK11819 421 -----------REI----PSR-AYVGRFnfkggdqqkkvgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD------- 477
|
250 260
....*....|....*....|....
gi 799207702 464 VELLRSLQ---AKYNLTYLFISHD 484
Cdd:PRK11819 478 VETLRALEealLEFPGCAVVISHD 501
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-237 |
2.16e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 24 RVVNNVSFDIKRGETIALVGESGSGKSvTAHSILRLLPyplaRHPSGTINYAGQDlltlkektirhIRGNRIAMIFQEPM 103
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKT-TLLGTLCGDP----RATSGRIVFDGKD-----------ITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 104 TSLNPLHNIEKQINEVLGLHKGltGKVAT-QRTLELLELVGILEP--HKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG--GFFAErDQFQERIKWVYELFPrlHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 181 ADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-231 |
2.61e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 34 KRGETIALVGESGSGKSvTAHSIL--RLLPyPLARHPSGTiNYagqdlltlkEKTIRHIRGNRIamifQEPMTSLnplhn 111
Cdd:cd03236 24 REGQVLGLVGPNGIGKS-TALKILagKLKP-NLGKFDDPP-DW---------DEILDEFRGSEL----QNYFTKL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 112 IEKQINEVLG------LHKGLTGKV-----ATQRTLELLELVGILEPHKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:cd03236 83 LEGDVKVIVKpqyvdlIPKAVKGKVgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 799207702 181 ADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVM 231
Cdd:cd03236 163 FDEPSSYLDIK-QRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
305-507 |
3.06e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.76 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL------RLIGSKG----GIRFEG-QQLDRLTqqqvrplrremqVVFQDPFG 373
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarRLHLKKEqpgnHDRIEGlEHIDKVI------------VIDQSPIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 374 SlSPRMC---------------------------VSEIVGEGLRIH-----------KMGTPAEQEAAIIAALKEVGLDP 415
Cdd:cd03271 82 R-TPRSNpatytgvfdeirelfcevckgkrynreTLEVRYKGKSIAdvldmtveealEFFENIPKIARKLQTLCDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 416 ESRHRYPHEFSGGQRQRIAIARALVLKPR---LILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISHDLAVVKALS 492
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKCAD 239
|
250 260
....*....|....*....|
gi 799207702 493 HQLMV-----VKHGQVVEQG 507
Cdd:cd03271 240 WIIDLgpeggDGGGQVVASG 259
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-190 |
3.37e-06 |
|
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: 48.56 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 32 DIKRGETIALVGESGSGKSvtahSILRLLpyplarhpSGTINYAGQDLLTLKEKTirhirgnriamifqepmtSLNPLHN 111
Cdd:cd03237 21 SISESEVIGILGPNGIGKT----TFIKML--------AGVLKPDEGDIEIELDTV------------------SYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 112 IEKQINEVLGLHKGLTGKVATQ-----RTLELLELVGILEphkrlKALPhELSGGQRQRVMIAMALANEPELLIADEPTT 186
Cdd:cd03237 71 KADYEGTVRDLLSSITKDFYTHpyfktEIAKPLQIEQILD-----REVP-ELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
....
gi 799207702 187 ALDV 190
Cdd:cd03237 145 YLDV 148
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-239 |
4.24e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 22 HQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPLArhpSGTINYAGQdlLTLKEKTIRHIRGNRIAMIFQE 101
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGA---PRGARVTGD--VTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMTSLNPLHNIEKQINEVLGL--HKGLTGKVaTQRTLEL----LELVGILEPHKRLKAlphELSGGQRQRVMIAMALAN- 174
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLGRypHARRAGAL-THRDGEIawqaLALAGATALVGRDVT---TLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799207702 175 --------EPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQKGCIVEQ 239
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
426-516 |
6.49e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVE--LLRSLQAKynlTYLFISHDLAVVkALSHQLMVVKHGQV 503
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGK---TRVLATHQVHVV-PRADYVVALGDGRV 859
|
90
....*....|...
gi 799207702 504 VEQGDAAGIFAAP 516
Cdd:PTZ00243 860 EFSGSSADFMRTS 872
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
305-465 |
7.29e-06 |
|
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: 47.93 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGQQLDRLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSE 383
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 384 IVGEGlRIHKMgtpaeqEAAIIAALKEVGLDpesrhrypheFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQV 463
Cdd:cd03291 136 CQLEE-DITKF------PEKDNTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
..
gi 799207702 464 VE 465
Cdd:cd03291 199 FE 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
426-495 |
7.53e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 7.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 426 SGGQRQRIAIARALVL---KPR-LILLDEPTSALDRTVQRQVVELLRSlQAKYNLTYLFISHDLAVVKALSHQL 495
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAELADKLI 151
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
301-507 |
8.02e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.86 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGQQLdrltQQQVRPLRREMQVVFQDPFgsLSPR 378
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTT-LSILTglLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNI--LFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 379 MCVSEIVGEGLRIhKMGTPAEQEAAIIAALKEVGLDpESRHRYPHEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRT 458
Cdd:TIGR01257 1018 LTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 799207702 459 VQRQVVELLrsLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQVVEQG 507
Cdd:TIGR01257 1096 SRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-189 |
8.02e-06 |
|
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: 46.87 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 10 RDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARH--PSGTINYAGQDLLTLKEKTI 87
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCS----TLLKALANRTEGNvsVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 88 RHIrgnriamIFqepmTSLNPLHniekqinevlglHKGLTgkvaTQRTLELlelvgilephkRLKALPHE----LSGGQR 163
Cdd:cd03233 83 GEI-------IY----VSEEDVH------------FPTLT----VRETLDF-----------ALRCKGNEfvrgISGGER 124
|
170 180
....*....|....*....|....*.
gi 799207702 164 QRVMIAMALANEPELLIADEPTTALD 189
Cdd:cd03233 125 KRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
237-266 |
8.93e-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: 43.54 E-value: 8.93e-06
10 20 30
....*....|....*....|....*....|
gi 799207702 237 VEQADCETLFQSPQHPYTQELLAAEPSGGP 266
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
426-513 |
9.01e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVE--LLRSLQAKynlTYLFISHDLAVVkALSHQLMVVKHGQV 503
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGK---TRVLVTNQLHFL-PLMDRIILVSEGMI 817
|
90
....*....|
gi 799207702 504 VEQGDAAGIF 513
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-234 |
1.03e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVEFVTgDHHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpYPLARHPSGTINYAGQdllTLKEKTIRHIR 91
Cdd:PRK10982 251 LEVRNLT-SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETL-----FGIREKSAGTITLHGK---KINNHNANEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 92 GNRIAMIFQEPMTS---------LNPL-HNIEKQINEvLGLHKGLTGKVATQRTLELLelvgilephkRLKALPHE---- 157
Cdd:PRK10982 322 NHGFALVTEERRSTgiyayldigFNSLiSNIRNYKNK-VGLLDNSRMKSDTQWVIDSM----------RVKTPGHRtqig 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 158 -LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:PRK10982 391 sLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-238 |
1.03e-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: 48.40 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGdhHQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEKT 86
Cdd:TIGR00957 1285 VEFRNYCLRYRED--LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN-----ESAEGEIIIDGLNIAKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRhirgNRIAMIFQEPM-------TSLNPLHNIEKQinEVLglhkgltgkvatqRTLELLELVGIL--EPHKrlkaLPHE 157
Cdd:TIGR00957 1358 LR----FKITIIPQDPVlfsgslrMNLDPFSQYSDE--EVW-------------WALELAHLKTFVsaLPDK----LDHE 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 -------LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL-----GMALLLISHDLNLVRRIA 225
Cdd:TIGR00957 1415 caeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-------NLIQSTIrtqfeDCTVLTIAHRLNTIMDYT 1487
|
250
....*....|...
gi 799207702 226 hRVCVMQKGCIVE 238
Cdd:TIGR00957 1488 -RVIVLDKGEVAE 1499
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-189 |
1.17e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFvtgdHHQRVVNNVSFDIKRGETIALVGESGSGKSVtahsilrLLPYPLARHPSGTINYagqdlLTL-- 82
Cdd:PRK10938 259 PRIVLNNGVVSY----NDRPILHNLSWQVNPGEHWQIVGPNGAGKST-------LLSLITGDHPQGYSND-----LTLfg 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 83 ----KEKTI----RHIrGNRIAMIFQEPMTSLNPLHNIEKQINEVLGLHKGLTGKvatQRTL--ELLELVGIlepHKRLK 152
Cdd:PRK10938 323 rrrgSGETIwdikKHI-GYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDR---QQKLaqQWLDILGI---DKRTA 395
|
170 180 190
....*....|....*....|....*....|....*...
gi 799207702 153 ALP-HELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:PRK10938 396 DAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
303-470 |
1.37e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.95 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGS-----KGGIRFEGQqldrltqqqvrPLRREMQVVFQDPF----- 372
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSL----LRILAGlarpdAGEVLWQGE-----------PIRRQRDEYHQDLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 ----GSLSPRmcvseivgEGLRI-HKMGTPAEQEAAIIAaLKEVGLdpESRHRYP-HEFSGGQRQRIAIARALVLKPRLI 446
Cdd:PRK13538 83 pgikTELTAL--------ENLRFyQRLHGPGDDEALWEA-LAQVGL--AGFEDVPvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|....
gi 799207702 447 LLDEPTSALDrtvqRQVVELLRSL 470
Cdd:PRK13538 152 ILDEPFTAID----KQGVARLEAL 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
158-247 |
1.40e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIAHRVCVMQKGCIV 237
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
90
....*....|....*
gi 799207702 238 -----EQADCETLFQ 247
Cdd:PRK11288 476 gelarEQATERQALS 490
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
426-503 |
1.45e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 1.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDrtvqRQVVELLRSLQAKYNLTYLFISHDLAVVKALSHQLMVVKHGQV 503
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
286-508 |
1.52e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 286 PIKKGFLRTtvdyVKAVDGinFSLPqGQTLGIVGESGSGKSTLgLAIL--RLIGS--KGGIRF-EGQQLD----RLT--- 353
Cdd:TIGR00956 770 KIKKEKRVI----LNNVDG--WVKP-GTLTALMGASGAGKTTL-LNVLaeRVTTGviTGGDRLvNGRPLDssfqRSIgyv 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 354 QQQ--------VRP-------LRREMQVvfqdpfgSLSPRMcvsEIVGEGLRIHKM--------GTPAEqeaaiiaalke 410
Cdd:TIGR00956 842 QQQdlhlptstVREslrfsayLRQPKSV-------SKSEKM---EYVEEVIKLLEMesyadavvGVPGE----------- 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 411 vGLDPEsrhryphefsggQRQRIAIARALVLKPRLIL-LDEPTSALDRTVQRQVVELLRSLqAKYNLTYLFISHDLAVV- 488
Cdd:TIGR00956 901 -GLNVE------------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSAIl 966
|
250 260
....*....|....*....|.
gi 799207702 489 -KALSHQLMVVKHGQVVEQGD 508
Cdd:TIGR00956 967 fEEFDRLLLLQKGGQTVYFGD 987
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
425-507 |
1.79e-05 |
|
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: 45.72 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 425 FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNLTyLFISHDLAVVKALS--HQLMVVKHGQ 502
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTT-TFVSLYQASDEIYDlfDKVLVLYEGR 197
|
....*
gi 799207702 503 VVEQG 507
Cdd:cd03233 198 QIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-191 |
2.16e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSIlrllpyplarhpSGTI---NYAGQDLLTLKEKTIRHIRgnRIAMIFQE 101
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL------------AGRIqgnNFTGTILANNRKPTKQILK--RTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 102 PMtsLNPLHNIEKQI--NEVLGLHKGLTGKVATQRTLELLELVGILEPHKRL--KALPHELSGGQRQRVMIAMALANEPE 177
Cdd:PLN03211 149 DI--LYPHLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170
....*....|....
gi 799207702 178 LLIADEPTTALDVT 191
Cdd:PLN03211 227 LLILDEPTSGLDAT 240
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-60 |
2.22e-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: 46.39 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 799207702 7 IEIRDLSVEFVTGDHhqRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLL 60
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL 54
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
408-513 |
2.52e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 408 LKEVGLDPESRHRYPHEFSGGQRQRIAIARAL--VLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISHDL 485
Cdd:cd03270 121 LVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDE 199
|
90 100
....*....|....*....|....*...
gi 799207702 486 AVVKALSHqlmvvkhgqVVEQGDAAGIF 513
Cdd:cd03270 200 DTIRAADH---------VIDIGPGAGVH 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
426-456 |
2.91e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 2.91e-05
10 20 30
....*....|....*....|....*....|.
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALD 456
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-193 |
3.77e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLArhPSgtinyagqdlltlkEKTIRHirGNRIAMIFQEPMT 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKS----SLLMMIMGELE--PS--------------EGKIKH--SGRISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SLNPLHNiekqiNEVLGLHKGLTGKVATQRTLELLELVGILePHKRLKALPH---ELSGGQRQRVMIAMALANEPELLIA 181
Cdd:TIGR01271 499 MPGTIKD-----NIIFGLSYDEYRYTSVIKACQLEEDIALF-PEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLL 572
|
170
....*....|..
gi 799207702 182 DEPTTALDVTVQ 193
Cdd:TIGR01271 573 DSPFTHLDVVTE 584
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
301-484 |
3.78e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.50 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 301 AVDGINFSLPQGQTLGIVGESGSGKSTlgLAILrLIG----SKGGIRFEGQQLDRLTQQQVRPLrreMQVVFQD------ 370
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKST--LAML-LTGlyqpQSGEILLDGKPVTAEQPEDYRKL---FSAVFTDfhlfdq 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 371 ---PFGSLSPrmcvSEIVGEGLRIHKMGTPAEQEAAIIAALKevgldpesrhrypheFSGGQRQRIAIARALVLKPRLIL 447
Cdd:PRK10522 412 llgPEGKPAN----PALVEKWLERLKMAHKLELEDGRISNLK---------------LSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 799207702 448 LDEptSALDRTVQ-RQVV--ELLRSLQAKyNLTYLFISHD 484
Cdd:PRK10522 473 LDE--WAADQDPHfRREFyqVLLPLLQEM-GKTIFAISHD 509
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-189 |
5.27e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 5 NLIEIRDLSVEFVTGDHHQRVVNNVSFDIKRGETIALVGESGSGKS--------------VTAHSIL---RLLPYPLARh 67
Cdd:TIGR00956 758 DIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTtllnvlaervttgvITGGDRLvngRPLDSSFQR- 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 68 psgTINYAGQDLLTLKEKTIRHirgnriAMIFQEPMTSLNPLHNIEKQ--INEVLglhkgltgkvatqrtlELLELVGIL 145
Cdd:TIGR00956 837 ---SIGYVQQQDLHLPTSTVRE------SLRFSAYLRQPKSVSKSEKMeyVEEVI----------------KLLEMESYA 891
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 799207702 146 EPhkrLKALPHE-LSGGQRQRVMIAMALANEPELLI-ADEPTTALD 189
Cdd:TIGR00956 892 DA---VVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
158-456 |
5.63e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQRVMIAMALANEPELLIADEPTTALD-----------VTVQlkilellkelQARLGMALLLISHDLNLVRRIAH 226
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfweliDRIR----------AERPGMSVLVATAYMEEAERFDW 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 227 RVcVMQKGCIV---------EQADCETLFQSpqhpYTQeLLAAEPSGGPATNVIgPPLLEVDDLKVwfPIK-KGFLRTTV 296
Cdd:NF033858 207 LV-AMDAGRVLatgtpaellARTGADTLEAA----FIA-LLPEEKRRGHQPVVI-PPRPADDDDEP--AIEaRGLTMRFG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 297 DYVkAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGQQL---DRLTQQQVR------PLRR 362
Cdd:NF033858 278 DFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTmkmltGL----LPASEGEAWLFGQPVdagDIATRRRVGymsqafSLYG 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 363 EMQV---------VFQDPFGSLSPRmcvseivgeglrIHKMgtpaeqeaaiiaaLKEVGLDPESRHRyPHEFSGGQRQRI 433
Cdd:NF033858 353 ELTVrqnlelharLFHLPAAEIAAR------------VAEM-------------LERFDLADVADAL-PDSLPLGIRQRL 406
|
330 340
....*....|....*....|...
gi 799207702 434 AIARALVLKPRLILLDEPTSALD 456
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVD 429
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
305-370 |
6.29e-05 |
|
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: 45.56 E-value: 6.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799207702 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGQQLDRLTQQQVRPLrreMQVVFQD 370
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyRPESGEILLDGQPVTADNREAYRQL---FSAVFSD 414
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-190 |
7.58e-05 |
|
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: 44.24 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplaRHPSGTINYAGQDLLTLKEKTIRHIRGNRIAMIFQEPMts 105
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 lnpLHNIEKQINEVLG------LHKGLTGKVATQRTLELLELVGILEPHKRlkalPHELSGGQRQRVMIAMALANEPELL 179
Cdd:cd03290 90 ---LLNATVEENITFGspfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNIV 162
|
170
....*....|.
gi 799207702 180 IADEPTTALDV 190
Cdd:cd03290 163 FLDDPFSALDI 173
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
426-507 |
8.45e-05 |
|
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: 45.39 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLK---PRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISHDLAVVKALSHQLMV----- 497
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|
gi 799207702 498 VKHGQVVEQG 507
Cdd:TIGR00630 910 DGGGTVVASG 919
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-225 |
8.97e-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: 42.75 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 35 RGETIALVGESGSGKSVTAHSILRLLPYPlarhpsgtinyagqdlltlkektirhirgnriamifqepmtslnplhniek 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP--------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 115 qinevlglhkglTGKVATQRTLELLELVGILEPHKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQ- 193
Cdd:smart00382 30 ------------GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEa 97
|
170 180 190
....*....|....*....|....*....|....*.
gi 799207702 194 ----LKILELLKELQARLGMALLLISHDLNLVRRIA 225
Cdd:smart00382 98 llllLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
426-504 |
1.00e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALDrtvqrqvVELLRSLQA---KYNLTYLFISHDLAVVKALSHQLMVVKHGQ 502
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMaleKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
..
gi 799207702 503 VV 504
Cdd:PRK15064 513 VV 514
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-222 |
1.38e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 12 LSVEFVTGDHHQRVV-NNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLARHpSGTINYA-GQDLLTLKEKTIRH 89
Cdd:PRK10636 313 LKMEKVSAGYGDRIIlDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLLAGELAPV-SGEIGLAkGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 90 IRGNRIAMifqEPMTSLNPlHNIEKQINEVLGLHkGLTGKVATQRTlellelvgilephkrlkalpHELSGGQRQRVMIA 169
Cdd:PRK10636 388 LRADESPL---QHLARLAP-QELEQKLRDYLGGF-GFQGDKVTEET--------------------RRFSGGEKARLVLA 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 799207702 170 MALANEPELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVR 222
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLR 491
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-183 |
1.46e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDHHqrvVNNVSFDIKRGETIALVGESGSGKSVTAhsilRLLPyPLARHPSGTINYAGQdllTLKEKT 86
Cdd:PRK10522 323 LELRNVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTLA----MLLT-GLYQPQSGEILLDGK---PVTAEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRgNRIAMIFQEpmtslnpLHNIEKqineVLGLHKGLTGKVATQRTLELLELVGILEpHKRLKALPHELSGGQRQRV 166
Cdd:PRK10522 392 PEDYR-KLFSAVFTD-------FHLFDQ----LLGPEGKPANPALVEKWLERLKMAHKLE-LEDGRISNLKLSKGQKKRL 458
|
170
....*....|....*..
gi 799207702 167 MIAMALANEPELLIADE 183
Cdd:PRK10522 459 ALLLALAEERDILLLDE 475
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
97-495 |
1.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 97 MIFQEPMTSLNPLHNIEKQINEVLglhKGLTGKVATQRTLELlelvGILEPHKRLKALphelSGGQRQRVMIAMALANEP 176
Cdd:PRK00635 427 MSLQELFIFLSQLPSKSLSIEEVL---QGLKSRLSILIDLGL----PYLTPERALATL----SGGEQERTALAKHLGAEL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 177 E--LLIADEPTTALDV--TVQLKILELLKELQarlGMALLLISHDLNLVRrIAHRVCVMQKGCIVEQAdcETLFQ-SPQh 251
Cdd:PRK00635 496 IgiTYILDEPSIGLHPqdTHKLINVIKKLRDQ---GNTVLLVEHDEQMIS-LADRIIDIGPGAGIFGG--EVLFNgSPR- 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 252 pytqELLAAEPSggpatnvIGPPLLEvDDLKVWFPIKKGFLRTTVDYVKA----VDGINFSLPQGQTLGIVGESGSGKS- 326
Cdd:PRK00635 569 ----EFLAKSDS-------LTAKYLR-QELTIPIPEKRTNSLGTLTLSKAtkhnLKDLTISLPLGRLTVVTGVSGSGKSs 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 327 ----TLGLAILRLI--GSKGGIRFEGQQLDRLTQ-----------------------------QQVRPLRREM---QVVF 368
Cdd:PRK00635 637 lindTLVPAVEEFIeqGFCSNLSIQWGAISRLVHitrdlpgrsqrsipltyikafddlrelfaEQPRSKRLGLtksHFSF 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 369 QDPFGSLS---------------PRMC-----------VSEIVGEGLRIHK-------------MGTPAEQEAAIIaaLK 409
Cdd:PRK00635 717 NTPLGACAecqglgsitttdnrtSIPCpsclgkrflpqVLEVRYKGKNIADilemtayeaekffLDEPSIHEKIHA--LC 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 410 EVGLDPESRHRYPHEFSGGQRQRIAIARAL---VLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISHDLA 486
Cdd:PRK00635 795 SLGLDYLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMH 873
|
....*....
gi 799207702 487 VVKALSHQL 495
Cdd:PRK00635 874 VVKVADYVL 882
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
425-501 |
2.13e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 425 FSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQ----VVELLRSLQAkynltYLFISHDLAVVKALSHQLMVVKH 500
Cdd:TIGR01257 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIREGRA-----VVLTSHSMEECEALCTRLAIMVK 2145
|
.
gi 799207702 501 G 501
Cdd:TIGR01257 2146 G 2146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-234 |
2.61e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTahsiLRLLPYPLARhPSGTINYAGQDLLTlkekTIRHIRGNriaMIFQEPMTS 105
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTV-TSGDATVAGKSILT----NISDVHQN---MGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 LNPLHNIEkqinEVLGLHKGLTGKVATQrtLELLELVGILEPHKRLKA--LPHELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:TIGR01257 2023 IDDLLTGR----EHLYLYARLRGVPAEE--IEKVANWSIQSLGLSLYAdrLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 799207702 184 PTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVRRIAHRVCVMQKG 234
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-192 |
2.96e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFDIKRGETIALVGESGSGKSVTAHSILRLLPyPLARHP---SGTINYAGQDLLTLKEKtirhIRGNriaMIFQEPMT 104
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP-PRSDASvviRGTVAYVPQVSWIFNAT----VRDN---ILFGSPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 SlnplHNIEKQInEVLGLhkgltgkvatQRTLELLELVGILEPHKRlkalPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:PLN03130 707 P----ERYERAI-DVTAL----------QHDLDLLPGGDLTEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
....*...
gi 799207702 185 TTALDVTV 192
Cdd:PLN03130 768 LSALDAHV 775
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
157-225 |
3.13e-04 |
|
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: 43.39 E-value: 3.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDV-TVQlkilellKELQARLGMA--LLLISHDLNLVRRIA 225
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLR-------ALEEALLNFAgcAVVISHDRWFLDRIA 507
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
125-232 |
3.50e-04 |
|
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: 41.79 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 125 GLTGKVATQRTLELLELVGILEPHKRLKALPH----------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQL 194
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGitpvykpqyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRL 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 799207702 195 KILELLKELQARLGMALLLISHDLNLVRRIAHRVCVMQ 232
Cdd:cd03222 109 NAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
299-340 |
4.49e-04 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 41.57 E-value: 4.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 799207702 299 VKAVDGInFSLPQGQTLGIVGESGSGKSTLGLAILR----------LIGSKG 340
Cdd:pfam00006 2 IRAIDGL-LPIGRGQRIGIFGGSGVGKTVLAGMIARqasadvvvyaLIGERG 52
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-248 |
5.23e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYplarhpsgtinyagqdlltlKEKTIRHIRGNrIAMIFQEPMts 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH--------------------AETSSVVIRGS-VAYVPQVSW-- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 lnpLHNIEKQINEVLG--LHKGLTGK----VATQRTLELLELVGILEPHKRlkalPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PLN03232 690 ---IFNATVRENILFGsdFESERYWRaidvTALQHDLDLLPGRDLTEIGER----GVNISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 799207702 180 IADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVRRIaHRVCVMQKGCIVEQADCETLFQS 248
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-221 |
6.53e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLaRHPSGTINYAGQdlltlkektirhirgNRIAMIFQEPMTSL- 106
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKS----TILKLISGEL-QPSSGTVFRSAK---------------VRMAVFSQHHVDGLd 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 107 ---NPLHNI--------EKQINEVLGlHKGLTGKVATQRTlellelvgilephkrlkalpHELSGGQRQRVMIAMALANE 175
Cdd:PLN03073 587 lssNPLLYMmrcfpgvpEQKLRAHLG-SFGVTGNLALQPM--------------------YTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 799207702 176 PELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLV 221
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLI 687
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
158-230 |
6.75e-04 |
|
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: 41.05 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 158 LSGGQRQ------RVMIAMALANEPELLIADEPTTALD---VTVQLKILELLKELQArlGMALLLISHDLNLVRRIAHRV 228
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenIEESLAEIIEERKSQK--NFQLIVITHDEELVDAADHIY 193
|
..
gi 799207702 229 CV 230
Cdd:cd03240 194 RV 195
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
426-463 |
1.05e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 799207702 426 SGGQRQRIAIARALVLKPRLILLDEPTSALD--------RTVQRQV 463
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDaraaaivmRTVRNTV 1066
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
408-513 |
1.11e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 408 LKEVGLDPESRHRYPHEFSGGQRQRIAIARAL--VLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKYNlTYLFISHDL 485
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDE 550
|
90 100
....*....|....*....|....*...
gi 799207702 486 AVVKALSHqlmvvkhgqVVEQGDAAGIF 513
Cdd:TIGR00630 551 DTIRAADY---------VIDIGPGAGEH 569
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
408-484 |
1.14e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 408 LKEVGLdPESRHRYP-HEFSGGQRQRIAIARALVLKPRLILLDEPTSALDRTVQRQVVELLRslqaKYNLTYLFISHD 484
Cdd:PRK15064 139 LLGVGI-PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN----ERNSTMIIISHD 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-193 |
1.29e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.82 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 7 IEIRDLSVEFVTGDhhQRVVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLpyplarHPSGTINYAGQDLLTLKEKT 86
Cdd:TIGR01271 1218 MDVQGLTAKYTEAG--RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL------STEGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 87 IRHIRGNRIAMIFQEPMTSLNPLHNIEKQINEVLglhkgltGKVAtqrtlELLELVGILE--PHK---RLKALPHELSGG 161
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEI-------WKVA-----EEVGLKSVIEqfPDKldfVLVDGGYVLSNG 1357
|
170 180 190
....*....|....*....|....*....|...
gi 799207702 162 QRQRVMIAMALANEPELLIADEPTTALD-VTVQ 193
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-293 |
1.39e-03 |
|
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: 41.47 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 26 VNNVSFDIKRGETIALVGESGSGKSvtahSILRLLPYPLAR-----HPSGTINYAGQDLLtLKEKTIRHirgnriAMIFQ 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKS----SLLSALLAEMDKveghvHMKGSVAYVPQQAW-IQNDSLRE------NILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 101 EPmtsLNPlhNIEKQINEVLGLHKGLTGKVATQRTlELLElVGIlephkrlkalphELSGGQRQRVMIAMALANEPELLI 180
Cdd:TIGR00957 723 KA---LNE--KYYQQVLEACALLPDLEILPSGDRT-EIGE-KGV------------NLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 181 ADEPTTALDVTVQLKILELLKELQARL-GMALLLISHDLNLVRRIaHRVCVMQKGCIVEQADCETLFQSP--------QH 251
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDgafaeflrTY 862
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 799207702 252 PYTQELLAAEPSGGPATNVIGPPLLEVDD-LKVWFPIKKGFLR 293
Cdd:TIGR00957 863 APDEQQGHLEDSWTALVSGEGKEAKLIENgMLVTDVVGKQLQR 905
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
424-468 |
1.82e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 799207702 424 EFSGGQRQR---IAIARALV----------LKPRLILLDEPTSALDRTVQRQVVELLR 468
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLR 89
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
157-190 |
2.80e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.80e-03
10 20 30
....*....|....*....|....*....|....
gi 799207702 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-188 |
3.16e-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: 39.16 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 28 NVSFDIKRGETIALVGESGSGKSVTAHSILrllpYPLA--RHPSGTINYAGQDLLTLKEKTIRHIRGNRIAMIFQEPMTS 105
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAFDTI----YAEGqrRYVESLSAYARQFLGQMDKPDVDSIEGLSPAIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 106 LNPlHNIEKQINEVLGLHKGLTGKVATQRTLELLELVGIlePHKRLKALPHELSGGQRQRVMIAMALANEPE--LLIADE 183
Cdd:cd03270 89 RNP-RSTVGTVTEIYDYLRLLFARVGIRERLGFLVDVGL--GYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDE 165
|
....*
gi 799207702 184 PTTAL 188
Cdd:cd03270 166 PSIGL 170
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
504-527 |
3.88e-03 |
|
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: 35.84 E-value: 3.88e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
422-499 |
4.28e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 422 PHEFSGGQRQ------RIAIARALVLK-------PRLILlDEPTSALDRTVQRQVVELLRSLQAKYNLTYLFISHDLAVV 488
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELV 857
|
90
....*....|.
gi 799207702 489 KALSHQLMVVK 499
Cdd:PRK02224 858 GAADDLVRVEK 868
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
128-190 |
4.47e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 4.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 799207702 128 GKVATQRTLELLELVGI-LEPHKRLKAlphELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:PRK15064 128 GYTAEARAGELLLGVGIpEEQHYGLMS---EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
299-472 |
5.17e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-GSK----GGIR-FEGQQLDRLTQQQVRPlrremQVVFQdPF 372
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIaGARkiqqGRVEvLGGDMADARHRRAVCP-----RIAYM-PQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 373 G---SLSPRMCVSEIV-------GEG-----LRIHKMgtpaeqeaaiiaaLKEVGLDPeSRHRYPHEFSGGQRQRIAIAR 437
Cdd:NF033858 84 GlgkNLYPTLSVFENLdffgrlfGQDaaerrRRIDEL-------------LRATGLAP-FADRPAGKLSGGMKQKLGLCC 149
|
170 180 190
....*....|....*....|....*....|....*
gi 799207702 438 ALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQA 472
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRA 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-263 |
5.87e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 25 VVNNVSFDIKRGETIALVGESGSGKSVTAHSILRLLPYPlarhpSGTINYAGQDLLTLKEKTIRHIrgnrIAMIFQEPMT 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 105 -------SLNPL--HNiEKQINEvlGLHKGLTGKVATQRTLELlelvgilepHKRLKALPHELSGGQRQRVMIAMALANE 175
Cdd:PLN03232 1322 fsgtvrfNIDPFseHN-DADLWE--ALERAHIKDVIDRNPFGL---------DAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 176 PELLIADEPTTALDVTVQLKILELLKELQARLGMalLLISHDLNLVRRiAHRVCVMQKGCIVEqadcetlFQSPqhpytQ 255
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLE-------YDSP-----Q 1454
|
....*...
gi 799207702 256 ELLAAEPS 263
Cdd:PLN03232 1455 ELLSRDTS 1462
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
292-520 |
7.79e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.23 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 292 LRTTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAilrLIGSK------GGIRFEGQQLDRLTqqqvrPLRREMQ 365
Cdd:PRK09580 7 LHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREdyevtgGTVEFKGKDLLELS-----PEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 366 VVF---QDP--FGSLSPRMCVSEIVGEgLRIHKMGTPAEQ---EAAIIAALKEVGLDPESRHRYPHE-FSGGQRQRIAIA 436
Cdd:PRK09580 79 GIFmafQYPveIPGVSNQFFLQTALNA-VRSYRGQEPLDRfdfQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799207702 437 RALVLKPRLILLDEPTSALDRTVQRQVVELLRSLQAKyNLTYLFISHDLAVVKALSHQLM-VVKHGQVVEQGDAAGIFAA 515
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGDFTLVKQL 236
|
....*
gi 799207702 516 PQHGY 520
Cdd:PRK09580 237 EEQGY 241
|
|
| |
