|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-327 |
0e+00 |
|
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: 547.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgDTGRIKKGEILFLGEDLAKKPEN 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLL--PPPGITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 245 FYDPKHPYTWGLLSSMPDLSTTNDtPLLAIPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPPWFKVSPTHFVKSWLLDA 324
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGR-RLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEE 317
|
...
gi 579304020 325 RAP 327
Cdd:COG0444 318 EAP 320
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-317 |
4.80e-155 |
|
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: 446.05 E-value: 4.80e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqGDTGRIKKGEILFLGEDLAK 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 241 VNEIFYDPKHPYTWGLLSSMPDLsttndTPLLAIPGAPPdLLHppkgdafARrsqyALDIDFKVEPPWFKVSPTHFV 317
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRG-----DPRPVPPDAPP-LLE-------AR----DLKVWFPIKRGLFRRTVGHVK 300
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-307 |
2.40e-137 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 393.71 E-value: 2.40e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtGRIKkGEILFLGEDLAK 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIG-GSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 241 VNEIFYDPKHPYTWGLLSSMPDLSTTNDTpLLAIPGAPPDLLHPPKGDAFARRSQYALDIdFKVEPP 307
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLDAEGES-LLTIPGNPPNLLRLPKGCPFQPRCPHAMEI-CSSAPP 310
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-327 |
8.98e-128 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 369.45 E-value: 8.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITAG-------EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgDTGrikkGEILF 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGlfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-PTS----GEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 74 LGEDLAKKPENELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGL-PNAEKRfka 152
Cdd:COG4608 78 DGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 YPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 233 GQMVETGDVNEIFYDPKHPYTWGLLSSMPDLSTTNDTPLLAIPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPPWFKVS 312
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAVPVPDPERRRERIVLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVG 313
|
330
....*....|....*
gi 579304020 313 PTHFVKSWLLDARAP 327
Cdd:COG4608 314 PGHQVACHLAEEGSG 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-239 |
6.18e-126 |
|
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: 361.05 E-value: 6.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKPEn 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL-----LKPTSGSIIFDGKDLLKLSR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALeILNLVGLPNAEKRFKAYPHQFSGGQRQR 164
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-263 |
9.04e-122 |
|
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: 360.76 E-value: 9.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDI-TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLA 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL-----RPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPENELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSG 159
Cdd:COG1123 331 KLSRRSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|....
gi 579304020 240 DVNEIFYDPKHPYTWGLLSSMPDL 263
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPSL 511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-306 |
7.68e-106 |
|
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: 319.93 E-value: 7.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDitAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqGDTGRIKkGEILFLGEDLAKKPEn 84
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIS-GEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 eliKLRGKDISMIFQDPMTSLNPTmQIGKQVMEPLIKHKnYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQR 164
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLG-LSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 245 FYDPKhpytwgLLSSMPDLSTTNDTPLLAIPGAPPdLL--------HPPKGdafaRRSQYAL-DIDFKVEP 306
Cdd:COG1123 231 LAAPQ------ALAAVPRLGAARGRAAPAAAAAEP-LLevrnlskrYPVRG----KGGVRAVdDVSLTLRR 290
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-263 |
1.46e-105 |
|
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: 319.71 E-value: 1.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDI-------TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikkGEILFLGED 77
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE------GEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 78 LAKKPENELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHK-NYSKAQAKKRALEILNLVGLPnAEKRFKaYPHQ 156
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLD-PAARHR-YPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*..
gi 579304020 237 ETGDVNEIFYDPKHPYTWGLLSSMPDL 263
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAAPLL 532
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-307 |
4.01e-103 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 306.67 E-value: 4.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdTGRIKKGEILFLGEDLAKKPEN 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQR 164
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 245 FYDPKHPYTWGLLSSMPDLStTNDTPLLAIPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPP 307
Cdd:PRK11022 242 FRAPRHPYTQALLRALPEFA-QDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPA 303
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-307 |
5.21e-100 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 298.80 E-value: 5.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITAG------EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITkLFQGDTGrikkGEILFL 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGlfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPTG----GELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 75 GEDLAKKPENElIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGL-PNAEKRfkaY 153
Cdd:PRK11308 76 GQDLLKADPEA-QKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGG 233
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 234 QMVETGDVNEIFYDPKHPYTWGLLSSMPDLSTTNDTPLLAIPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPP 307
Cdd:PRK11308 232 RCVEKGTKEQIFNNPRHPYTQALLSATPRLNPDDRRERIKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQ 305
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-317 |
1.51e-96 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 290.07 E-value: 1.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGE---------VQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLG 75
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 76 EDLAKKPENELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPL-IKHKNYSKAQAKKRALEILNLVGL-PNAEKRfkaY 153
Cdd:PRK15079 83 KDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLlPNLINR---Y 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGG 233
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 234 QMVETGDVNEIFYDPKHPYTWGLLSSM----PDLSTTNDTPLLAipGAPPDLLHPPKGDAFARRSQYALDIDFKVEPPwF 309
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAVpipdPDLERNKTIQLLE--GELPSPINPPSGCVFRTRCPIAGPECAKTRPV-L 315
|
....*...
gi 579304020 310 KVSPTHFV 317
Cdd:PRK15079 316 EGSFRHAV 323
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-271 |
5.60e-96 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 297.92 E-value: 5.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGE----- 76
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 77 DLAKKPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQ 156
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270
....*....|....*....|....*....|....*
gi 579304020 237 ETGDVNEIFYDPKHPYTWGLLSSMPDLSTTNDTPL 271
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDY 283
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-264 |
1.21e-95 |
|
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: 284.77 E-value: 1.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPene 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSG-----EVTFDGRPVTRRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 lIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKnysKAQAKKRALEILNLVGLPnAEKRFKaYPHQFSGGQRQRI 165
Cdd:COG1124 74 -RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLP-PSFLDR-YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*....
gi 579304020 246 YDPKHPYTWGLLSSMPDLS 264
Cdd:COG1124 228 AGPKHPYTRELLAASLAFE 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-272 |
7.56e-92 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 284.68 E-value: 7.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAK 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 579304020 241 VNEIFYDPKHPYTWGLLSSMPDLS----TTNDTPLL 272
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDpvplPEPASPLL 276
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
24-258 |
2.71e-85 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 257.68 E-value: 2.71e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKlFQGDTGRIKKGEILFLGEDLAKkpenelIKLRGKDISMIFQDPMT 103
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILG-LLPPGLTQTSGEILLDGRPLLP------LSIRGRHIATIMQNPRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 SLNPTMQIGKQVMEPLIKHKNYSKaQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:TIGR02770 74 AFNPLFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 184 TTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLLS 258
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-287 |
1.40e-83 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 256.76 E-value: 1.40e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfQGDTGRIKKGEILFLGEDLAKKPEN 84
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTSLNPTMQIGKQVME--PLIKHKNY---SKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSG 159
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEaiPSWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 579304020 240 DVNEIFYDPKHPYTWGLLSSMPDLSTT--NDTPLLAIPGAPPDLLHPPKG 287
Cdd:COG4170 242 PTEQILKSPHHPYTKALLRSMPDFRQPlpHKSRLNTLPGSIPPLQHLPIG 291
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-259 |
1.18e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 244.36 E-value: 1.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAG-----EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFLGED 77
Cdd:COG4167 4 LLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLA-------GIIEptSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 78 LAKKPenelIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFkaYPHQF 157
Cdd:COG4167 77 LEYGD----YKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANF--YPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 579304020 238 TGDVNEIFYDPKHPYTWGLLSS 259
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIES 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-259 |
1.37e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.50 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPEN 84
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV-----LVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRgKDISMIFQDP--MTSlnptmqigKQVME----PLiKHKNYSKAQAKKRALEILNLVGLpnAEKRfKAYPHQFS 158
Cdd:COG1135 76 ELRAAR-RKIGMIFQHFnlLSS--------RTVAEnvalPL-EIAGVPKAEIRKRVAELLELVGL--SDKA-DAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVET 238
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|.
gi 579304020 239 GDVNEIFYDPKHPYTWGLLSS 259
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLPT 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-261 |
2.27e-71 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 233.98 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFDITAG-------EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLG 75
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES-----QGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 76 EDLAKKPENELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGL-PNAEKRfkaYP 154
Cdd:PRK10261 386 QRIDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWR---YP 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
250 260
....*....|....*....|....*..
gi 579304020 235 MVETGDVNEIFYDPKHPYTWGLLSSMP 261
Cdd:PRK10261 542 IVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
1-260 |
1.99e-68 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 215.83 E-value: 1.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTER---ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFLG 75
Cdd:COG4107 1 MTNEeqpLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLY-------FDLAptSGSVYYRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 76 -----EDLAKKPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAekRF 150
Cdd:COG4107 74 rdggpRDLFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHYGDIRARALEWLERVEIPLE--RI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 151 KAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVM 230
Cdd:COG4107 152 DDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVM 231
|
250 260 270
....*....|....*....|....*....|
gi 579304020 231 YGGQMVETGDVNEIFYDPKHPYTWGLLSSM 260
Cdd:COG4107 232 KNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-297 |
2.23e-68 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 217.75 E-value: 2.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgDTGRIKKGEILFLGEDLAKKPEN 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPL----IKHKNYSKAQ-AKKRALEILNLVGLPNAEKRFKAYPHQFSG 159
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtYKGRWWQRFGwRKRRAIELLHRVGIKDHKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 240 DVNEIFYDPKHPYTWGLLSSMPDL--STTNDTPLLAIPGAPPDLLHPPKGDAFARRSQYA 297
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIPDFgsAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYA 301
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-258 |
1.53e-67 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 221.50 E-value: 1.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFDI-------TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgrikKGEILFL 74
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIrkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS------QGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 75 GEDLAKKPENELIKLRGKdISMIFQDPMTSLNPTMQIGKQVMEPL-IKHKNYSKAQAKKRALEILNLVGLpNAEKRFKaY 153
Cdd:PRK15134 346 GQPLHNLNRRQLLPVRHR-IQVVFQDPNSSLNPRLNVLQIIEEGLrVHQPTLSAAQREQQVIAVMEEVGL-DPETRHR-Y 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGG 233
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250 260
....*....|....*....|....*
gi 579304020 234 QMVETGDVNEIFYDPKHPYTWGLLS 258
Cdd:PRK15134 503 EVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-252 |
2.24e-67 |
|
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: 212.15 E-value: 2.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAK 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD-----SGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRgKDISMIFQDP--MTSLNptmqIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFS 158
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGalFDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALD-VTMqAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|....*
gi 579304020 238 TGDVNEIFyDPKHPY 252
Cdd:COG1127 223 EGTPEELL-ASDDPW 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-249 |
1.03e-65 |
|
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: 207.82 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPEN 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT-----SGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRgKDISMIFQ--DPMTSLNptmqIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLpnAEKRfKAYPHQFSGGQR 162
Cdd:cd03258 76 ELRKAR-RRIGMIFQhfNLLSSRT----VFENVALPL-EIAGVPKAEIEERVLELLELVGL--EDKA-DAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 163 QRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVN 242
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 579304020 243 EIFYDPK 249
Cdd:cd03258 227 EVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-237 |
4.13e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.05 E-value: 4.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTErILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSvttkaitklfqgdT-----G---RIKKGEIL 72
Cdd:COG1136 1 MSP-LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-------------TllnilGgldRPTSGEVL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 73 FLGEDLAKKPENELIKLRGKDISMIFQDPmtSLNPTMQIGKQVMEPLIkHKNYSKAQAKKRALEILNLVGLpnaEKRFKA 152
Cdd:COG1136 67 IDGQDISSLSERELARLRRRHIGFVFQFF--NLLPELTALENVALPLL-LAGVSRKERRERARELLERVGL---GDRLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 YPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLgVVANIADRVAVMYG 232
Cdd:COG1136 141 RPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRD 219
|
....*
gi 579304020 233 GQMVE 237
Cdd:COG1136 220 GRIVS 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-251 |
4.79e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 203.69 E-value: 4.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKkPEN 84
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLE-----EPDSGTITVDGEDLTD-SKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRgKDISMIFQdpmtSLN--PTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnAEKRfKAYPHQFSGGQR 162
Cdd:COG1126 71 DINKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL--ADKA-DAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 163 QRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVN 242
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
....*....
gi 579304020 243 EIFYDPKHP 251
Cdd:COG1126 222 EFFENPQHE 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
1.08e-62 |
|
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: 199.25 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgDtgRIKKGEILFLGEDLAKKPENE 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL---D--RPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKDISMIFQDPmtSLNPTMQIGKQVMEPLIKHKNySKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRI 165
Cdd:cd03255 76 LAAFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLgVVANIADRVAVMYGGQ 234
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-259 |
1.05e-61 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 201.18 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKPENEL 86
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQDLTALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 IKLRgKDISMIFQ--DPMTSlnptmqigKQVME----PLiKHKNYSKAQAKKRALEILNLVGLpnAEKRfKAYPHQFSGG 160
Cdd:PRK11153 78 RKAR-RQIGMIFQhfNLLSS--------RTVFDnvalPL-ELAGTPKAEIKARVTELLELVGL--SDKA-DRYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
250
....*....|....*....
gi 579304020 241 VNEIFYDPKHPYTWGLLSS 259
Cdd:PRK11153 225 VSEVFSHPKHPLTREFIQS 243
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-252 |
1.07e-61 |
|
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: 197.34 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-----SGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDP--MTSLNptmqIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQ 163
Cdd:cd03261 72 LYRLR-RRMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNE 243
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 579304020 244 IFyDPKHPY 252
Cdd:cd03261 224 LR-ASDDPL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-259 |
1.28e-61 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 198.00 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkGEILFLGEDLAkkPEneliKLRGKDISMIFQDPMTS 104
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTA-GRVLLDGKPVA--PC----ALRGRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGKQVMEPLikhKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPT 184
Cdd:PRK10418 92 FNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 185 TALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLLSS 259
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-260 |
1.82e-59 |
|
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: 192.71 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDL-----HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLA 79
Cdd:TIGR02769 2 LLEVRDVthtyrTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL-----EKPAQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPENELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkAYPHQFSG 159
Cdd:TIGR02769 77 QLDRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDAD--KLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250 260
....*....|....*....|.
gi 579304020 240 DVNEIFyDPKHPYTWGLLSSM 260
Cdd:TIGR02769 234 DVAQLL-SFKHPAGRNLQSAV 253
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-249 |
4.79e-59 |
|
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: 190.24 E-value: 4.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKpenE 85
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-----SGEVLVDGKDITKK---N 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDPMTSL-NPTmqigkqVME-----PliKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSG 159
Cdd:COG1122 70 LRELR-RKVGLVFQNPDDQLfAPT------VEEdvafgP--ENLGLPREEIRERVEEALELVGLEHLADR---PPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
250
....*....|
gi 579304020 240 DVNEIFYDPK 249
Cdd:COG1122 217 TPREVFSDYE 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
6.70e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 194.16 E-value: 6.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAK 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI-----LLDGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENEliklRgkDISMIFQDPmtSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGG 160
Cdd:COG3842 72 LPPEK----R--NVGMVFQDY--ALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADR---YPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
250
....*....|..
gi 579304020 241 VNEIFYDPKHPY 252
Cdd:COG3842 220 PEEIYERPATRF 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-243 |
7.04e-59 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 191.44 E-value: 7.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENELIKLRg 91
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-----QGNVSWRGEPLAKLNRAQRKAFR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLP--NAEKRfkayPHQFSGGQRQRIVIAT 169
Cdd:PRK10419 89 RDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdsVLDKR----PPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 170 ALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNE 243
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-239 |
7.56e-56 |
|
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: 181.56 E-value: 7.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENE 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSG-----EILIDGRDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liklrgKDISMIFQDPmtSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRI 165
Cdd:cd03259 72 ------RNIGMVFQDY--ALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-234 |
1.05e-54 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 178.88 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKkPENE 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTD-DKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNaekRFKAYPHQFSGGQRQRI 165
Cdd:cd03262 71 INELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD---KADAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGGQ 234
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVV-VTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-259 |
2.15e-54 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 179.60 E-value: 2.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFDITAG-----EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGED 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-----ELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 78 LAKKPenelIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFkaYPHQF 157
Cdd:PRK15112 77 LHFGD----YSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY--YPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 579304020 238 TGDVNEIFYDPKHPYTWGLLSS 259
Cdd:PRK15112 231 RGSTADVLASPLHELTKRLIAG 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
1.10e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 174.89 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTER--ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDL 78
Cdd:COG1116 1 MSAAapALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG-----EVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 79 AKKpeneliklrGKDISMIFQDPmtSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKrfkAYPHQFS 158
Cdd:COG1116 76 TGP---------GPDRGVVFQEP--ALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFED---AYPHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDV----TMQAQILDLMKELQqkidTAIIFITHDLGVVANIADRVAVM 230
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQETG----KTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-234 |
1.58e-52 |
|
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: 173.04 E-value: 1.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFDitAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKPenel 86
Cdd:cd03225 1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKLS---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 IKLRGKDISMIFQDPMTSL-NPTmqIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRI 165
Cdd:cd03225 70 LKELRRKVGLVFQNPDDQFfGPT--VEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
2.23e-52 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 174.34 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRI----KKGEILflge 76
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 77 DLAKKPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPL--IKHKNYSKAQAKkrALEILNLVGLPnaEKRFKAYP 154
Cdd:PRK11701 74 DLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLmaVGARHYGDIRAT--AGDWLERVEID--AARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|....*
gi 579304020 235 MVETGDVNEIFYDPKHPYTWGLLSS 259
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-244 |
2.54e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 170.63 E-value: 2.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPEne 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSG-----EVRVLGEDVARDPA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liKLRgKDISMIFQDPmtSLNPTMQiGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRI 165
Cdd:COG1131 70 --EVR-RRIGYVPQEP--ALYPDLT-VRENLRFFARLYGLPRKEARERIDELLELFGLTDAADR---KVGTLSGGMKQRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-238 |
7.22e-51 |
|
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: 169.54 E-value: 7.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTgrikkGEILFLGEDLAK 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTS-----GTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKDISMIFQDPMtsLNPTMQIGKQVMEPL-IKhknySKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSG 159
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSFQ--LLPTLTALENVMLPLeLA----GRRDARARARALLERVGL---GHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGvVANIADRVAVMYGGQMVET 238
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGRLVED 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-230 |
1.06e-50 |
|
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: 168.42 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKkpene 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG-----EVLVDGEPVTG----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liklRGKDISMIFQDPmtSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRI 165
Cdd:cd03293 71 ----PGPDRGYVFQQD--ALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDV----TMQAQILDLMKELQQkidtAIIFITHDLGVVANIADRVAVM 230
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGK----TVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-252 |
2.48e-50 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 168.25 E-value: 2.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVqAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPEnelIKLRG 91
Cdd:cd03295 5 NVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSG-----EIFIDGEDIREQDP---VELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KdISMIFQDpmTSLNPTMQIGKQVmEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKaYPHQFSGGQRQRIVIATAL 171
Cdd:cd03295 76 K-IGYVIQQ--IGLFPHMTVEENI-ALVPKLLKWPKEKIRERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 172 ACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHP 251
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
.
gi 579304020 252 Y 252
Cdd:cd03295 231 F 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-244 |
6.95e-49 |
|
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: 164.28 E-value: 6.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPENe 85
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKdISMIFQDPmtslNP-TMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfKAYPHQFSGGQRQR 164
Cdd:cd03260 76 VLELRRR-VGMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-237 |
9.12e-49 |
|
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: 163.68 E-value: 9.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENELIKLRGKDISMIFQd 100
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSG-----EVLFNGQSLSKLSSNERAKLRNKKLGFIYQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 101 pMTSLNPTMQIGKQVMEP-LIKHKnySKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLI 179
Cdd:TIGR02211 91 -FHHLLPDFTALENVAMPlLIGKK--SVKEAKERAYEMLEKVGL---EHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIaDRVAVMYGGQMVE 237
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-252 |
2.90e-48 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 163.97 E-value: 2.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 19 AGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPENELIKLRGKDISMIF 98
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE-----PTSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVL 178
Cdd:cd03294 109 QS--FALLPHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHK---YPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPY 252
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-257 |
1.08e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 164.55 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAkkpene 85
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-----VLNGRDLF------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 lIKLRGKD--ISMIFQDPMtsLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQ 163
Cdd:COG1118 68 -TNLPPRErrVGFVFQHYA--LFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNE 243
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
250
....*....|....
gi 579304020 244 IFYDPKHPYTWGLL 257
Cdd:COG1118 221 VYDRPATPFVARFL 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-256 |
1.45e-47 |
|
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: 162.24 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 18 TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSvttkaiTkLFQGDTGRIK--KGEILFLGEDLAKKPENELIKLRgKDIS 95
Cdd:TIGR04521 14 TPFEKKALDDVSLTIEDGEFVAIIGHTGSGKS------T-LIQHLNGLLKptSGTVTIDGRDITAKKKKKLKDLR-KKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 96 MIFQdpmtslNPTMQ-----IGKQVM-EPlikhKNY--SKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSGGQRQRIVI 167
Cdd:TIGR04521 86 LVFQ------FPEHQlfeetVYKDIAfGP----KNLglSEEEAEERVKEALELVGLD--EEYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 168 ATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYD 247
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
....*....
gi 579304020 248 PKHPYTWGL 256
Cdd:TIGR04521 234 VDELEKIGL 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
2.54e-47 |
|
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: 158.50 E-value: 2.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKkpENE 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDLTD--LED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKDISMIFQDPmtSLNPTMQIGKQVMEPLikhknyskaqakkraleilnlvglpnaekrfkayphqfSGGQRQRI 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-237 |
6.97e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 158.68 E-value: 6.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPENELIKLRgKDISMIFQ 99
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE-----RPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DpmTSLNPTMQIGKQVMEPLIKHKnYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLI 179
Cdd:COG2884 87 D--FRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL---SDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-260 |
1.97e-46 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 158.84 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPEN 84
Cdd:TIGR02323 3 LLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPL--IKHKNYSKAQAKkrALEILNLVGLPNAekRFKAYPHQFSGGQR 162
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLmaIGARHYGNIRAT--AQDWLEEVEIDPT--RIDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 163 QRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVN 242
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
250
....*....|....*...
gi 579304020 243 EIFYDPKHPYTWGLLSSM 260
Cdd:TIGR02323 235 QVLDDPQHPYTQLLVSSI 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-245 |
1.42e-45 |
|
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: 156.36 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSvtT--KAITKLFqgdtgRIKKGEILFLGEDLAKKP 82
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKS--TllRALAGLL-----KPSSGEVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLrgkdISMIFQDPMTSLNPTmqigkqVME-------PLIKH-KNYSKA--QAKKRALEILNLVGLpnAEKRFka 152
Cdd:COG1120 70 RRELARR----IAYVPQEPPAPFGLT------VRElvalgryPHLGLfGRPSAEdrEAVEEALERTGLEHL--ADRPV-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 ypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:COG1120 136 --DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
250
....*....|...
gi 579304020 233 GQMVETGDVNEIF 245
Cdd:COG1120 214 GRIVAQGPPEEVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-249 |
1.32e-44 |
|
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: 153.36 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-----SGSVLFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKlRGkdISMIFQDP-----MTSLNpTMQIGKQVMEP---LIKHKNYSKAQAKKRALEILNLVGLpnAEKRFKAyPHQF 157
Cdd:cd03219 72 IAR-LG--IGRTFQIPrlfpeLTVLE-NVMVAAQARTGsglLLARARREEREARERAEELLERVGL--ADLADRP-AGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|..
gi 579304020 238 TGDVNEIFYDPK 249
Cdd:cd03219 224 EGTPDEVRNNPR 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-249 |
4.30e-44 |
|
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: 152.01 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKlFQGDTgrikKGEILFLGEDLAKKPENEliklrgKDISMIFQ 99
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-FETPT----SGEILLDGKDITNLPPHK------RPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLI 179
Cdd:cd03300 80 N--YALFPHLTVFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPK 249
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
9.84e-44 |
|
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: 148.18 E-value: 9.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPenelIKLRGKDISMIFQDPmtS 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDDE----RKSLRKEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGKQVMEPLIkHKNYSKAQAKKRALEILNLVGLPNAEKRF-KAYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:pfam00005 70 LFPRLTVRENLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 579304020 184 TT 185
Cdd:pfam00005 149 TA 150
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-258 |
1.98e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.67 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 23 QAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPENELIKLRgKDISMIFQDpm 102
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLR-QHVGFVFQN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 103 TSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKrfkAYPHQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:PRK11264 94 FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 183 PTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLLS 258
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
2.09e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSvtT--KAITKLFqgdtgRIKKGEILFLGEDL 78
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS--TllKAILGLL-----PPTSGTVRLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 79 AKKpeneliklrGKDISMIFQdpMTSLNPTMQI-GKQ-VMEPLIKHKN----YSKAQaKKRALEILNLVGLPN-AEKRFk 151
Cdd:COG1121 71 RRA---------RRRIGYVPQ--RAEVDWDFPItVRDvVLMGRYGRRGlfrrPSRAD-REAVDEALERVGLEDlADRPI- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 152 aypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMy 231
Cdd:COG1121 138 ---GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL- 212
|
250
....*....|....
gi 579304020 232 GGQMVETGDVNEIF 245
Cdd:COG1121 213 NRGLVAHGPPEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-239 |
4.16e-43 |
|
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: 147.58 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPenel 86
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL-----KPSSGEILLDGKDLASLS---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 IKLRGKDISMIFQdpmtslnptmqigkqvmeplikhknyskaqakkrALEILNLVGLpnAEKRFkaypHQFSGGQRQRIV 166
Cdd:cd03214 68 PKELARKIAYVPQ----------------------------------ALELLGLAHL--ADRPF----NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 167 IATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-259 |
5.09e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.53 E-value: 5.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTEriLEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAK 80
Cdd:COG3839 1 MAS--LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE-----DPTSGEILIGGRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENEliklRgkDISMIFQDPMtsLNPTMQigkqVME----PLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQ 156
Cdd:COG3839 70 LPPKD----R--NIAMVFQSYA--LYPHMT----VYEniafPL-KLRKVPKAEIDRRVREAAELLGLEDLLDR---KPKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALD----VTMQAQIldlmKELQQKIDTAIIFITHDLgVVAN-IADRVAVMY 231
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEI----KRLHRRLGTTTIYVTHDQ-VEAMtLADRIAVMN 208
|
250 260
....*....|....*....|....*...
gi 579304020 232 GGQMVETGDVNEIFYDPKHPYTWGLLSS 259
Cdd:COG3839 209 DGRIQQVGTPEELYDRPANLFVAGFIGS 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-230 |
6.02e-43 |
|
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: 148.74 E-value: 6.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTErILEVNDLHVSFDI-TAG--EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRI----KKGEIlf 73
Cdd:COG4778 1 MTT-LLEVENLSKTFTLhLQGgkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhDGGWV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 74 lgeDLAKKPENELIKLRGKDISMIFQdpmtSLN-----PTMQIgkqVMEPLIkHKNYSKAQAKKRALEILNLVGLPnaEK 148
Cdd:COG4778 78 ---DLAQASPREILALRRRTIGYVSQ----FLRviprvSALDV---VAEPLL-ERGVDREEARARARELLARLNLP--ER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 149 RFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVA 228
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVV 223
|
..
gi 579304020 229 VM 230
Cdd:COG4778 224 DV 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-244 |
8.60e-43 |
|
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: 148.87 E-value: 8.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDPmtSLNPTMQIGKQVMEPLIKHKN--------YSKAQaKKRALEILNLVGL-PNAEKRFKayphQ 156
Cdd:cd03256 73 LRQLR-RQIGMIFQQF--NLIERLSVLENVLSGRLGRRStwrslfglFPKEE-KQRALAALERVGLlDKAYQRAD----Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
....*...
gi 579304020 237 ETGDVNEI 244
Cdd:cd03256 225 FDGPPAEL 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-251 |
8.79e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 149.18 E-value: 8.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPEN- 84
Cdd:COG4598 9 LEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPD-----SGEIRVGGEEIRLKPDRd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ---------ELIKLRGKdISMIFQdpmtSLN--PTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnAEKRfKAY 153
Cdd:COG4598 80 gelvpadrrQLQRIRTR-LGMVFQ----SFNlwSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGL--ADKR-DAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGG 233
Cdd:COG4598 152 PAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFARDVSSHVVFLHQG 230
|
250
....*....|....*...
gi 579304020 234 QMVETGDVNEIFYDPKHP 251
Cdd:COG4598 231 RIEEQGPPAEVFGNPKSE 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-253 |
9.39e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 149.03 E-value: 9.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTG-RIKkGEILFLGEDLAK 80
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGaRVE-GEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 kPENELIKLRgKDISMIFQDPmtslNP-TMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEK-RFKAYPHQFS 158
Cdd:COG1117 83 -PDVDVVELR-RRVGMVFQKP----NPfPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKdRLKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIdtAIIFITHDLGVVANIADRVAVMYGGQMVET 238
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEF 234
|
250
....*....|....*
gi 579304020 239 GDVNEIFYDPKHPYT 253
Cdd:COG1117 235 GPTEQIFTNPKDKRT 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-236 |
2.28e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.90 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPEN 84
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSG-----EILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGkDISMIFQDPmtSLNPTMQigkqVME----------PLIKH--KNYSKAQaKKRALEILNLVGLpnAEKRFK- 151
Cdd:COG3638 74 ALRRLRR-RIGMIFQQF--NLVPRLS----VLTnvlagrlgrtSTWRSllGLFPPED-RERALEALERVGL--ADKAYQr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 152 AypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMY 231
Cdd:COG3638 144 A--DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLR 221
|
....*
gi 579304020 232 GGQMV 236
Cdd:COG3638 222 DGRVV 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-257 |
2.42e-42 |
|
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: 147.49 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPenelikLRGKDISMIFQ 99
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-----LFGGEDATDVP------VQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DpmTSLNPTMQIGKQVMEPL-IKHKNY--SKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPK 176
Cdd:cd03296 82 H--YALFRHMTVFDNVAFGLrVKPRSErpPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 177 VLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGL 256
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
.
gi 579304020 257 L 257
Cdd:cd03296 237 L 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-249 |
2.60e-42 |
|
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: 147.48 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAK-KPENEliklrgkDISMIFQDpmT 103
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-----LLNGKDITNlPPEKR-------DISYVPQN--Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 SLNPTMQIGKQVmEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:cd03299 81 ALFPHMTVYKNI-AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR---KPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 184 TTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPK 249
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-292 |
6.84e-42 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 149.42 E-value: 6.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITagevQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLAKKPENE 85
Cdd:TIGR03265 5 LSIDNIRKRFGAF----TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQG-----GRDITRLPPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liklrgKDISMIFQDpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRI 165
Cdd:TIGR03265 76 ------RDYGIVFQS--YALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERK---YPGQLSGGQQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:TIGR03265 144 ALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 579304020 246 YDPKHPYTWGLLSSMPDLSTTNDTPLLAIPG------APPDLLHPPKGDAFAR 292
Cdd:TIGR03265 224 RHPATPFVADFVGEVNWLPGTRGGGSRARVGgltlacAPGLAQPGASVRLAVR 276
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-252 |
1.64e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 147.16 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 19 AGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPeneLIKLRgKDISMIF 98
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRI-----LIDGEDIRDLD---PVELR-RRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDpmTSLNPTMQIGKQVMepLI-KHKNYSKAQAKKRALEILNLVGLPNAEKRfKAYPHQFSGGQRQRIVIATALACEPKV 177
Cdd:COG1125 83 QQ--IGLFPHMTVAENIA--TVpRLLGWDKERIRARVDELLELVGLDPEEYR-DRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 178 LIADEPTTALD-VTmQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPY 252
Cdd:COG1125 158 LLMDEPFGALDpIT-REQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-249 |
2.03e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 145.16 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFlgeDLAKKP-ENELIKLRgKDISMIF 98
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF---DFSKTPsDKAIRELR-RNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQRQRIVIATALACEPKVL 178
Cdd:PRK11124 89 QQ--YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRF---PLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGGQMVETGDvNEIFYDPK 249
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-244 |
5.81e-41 |
|
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: 143.98 E-value: 5.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPEN 84
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV-----EPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKdISMIFQDpmTSLNPTMQIGKQVMEPLIKHKN--------YSKAQaKKRALEILNLVGLPN-AEKRFKayph 155
Cdd:TIGR02315 73 KLRKLRRR-IGMIFQH--YNLIERLTVLENVLHGRLGYKPtwrsllgrFSEED-KERALSALERVGLADkAYQRAD---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:TIGR02315 145 QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
....*....
gi 579304020 236 VETGDVNEI 244
Cdd:TIGR02315 225 VFDGAPSEL 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-235 |
6.19e-41 |
|
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: 141.77 E-value: 6.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPEne 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDIKKEPE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liKLRGKdISMIFQDPmtSLNPTMqigkqvmeplikhknyskaqakkRALEILNLvglpnaekrfkayphqfSGGQRQRI 165
Cdd:cd03230 70 --EVKRR-IGYLPEEP--SLYENL-----------------------TVRENLKL-----------------SGGMKQRL 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-230 |
9.51e-41 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 142.29 E-value: 9.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFLGEDLAKKPen 84
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL-------GLLKptSGSIRVFGKPLEKER-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 eliklrgKDISMIFQdpMTSLNPTMQI-GKQ-VMEPLIKHKN----YSKAQaKKRALEILNLVGLPN-AEKRFKayphQF 157
Cdd:cd03235 68 -------KRIGYVPQ--RRSIDRDFPIsVRDvVLMGLYGHKGlfrrLSKAD-KAKVDEALERVGLSElADRQIG----EL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVM 230
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
2.08e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 142.74 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPene 85
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDPmtSLNPTMQIGKQV-MEPLIKHKNYSKAQAKKRALEILNLVGLPNAEK-RFKAYPHQFSGGQRQ 163
Cdd:PRK14247 77 VIELR-RRVQMVFQIP--NPIPNLSIFENVaLGLKLNRLVKSKKELQERVRWALEKAQLWDEVKdRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqqKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNE 243
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
250
....*....|
gi 579304020 244 IFYDPKHPYT 253
Cdd:PRK14247 232 VFTNPRHELT 241
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-257 |
5.13e-40 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 141.48 E-value: 5.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKkpene 85
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRI-----RLNGQDATR----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 lIKLRGKDISMIFQDpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRI 165
Cdd:TIGR00968 67 -VHARDRKIGFVFQH--YALFKHLTVRDNIAFGL-EIRKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:TIGR00968 140 ALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVY 219
|
250
....*....|..
gi 579304020 246 YDPKHPYTWGLL 257
Cdd:TIGR00968 220 DHPANPFVMSFL 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-249 |
8.42e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.92 E-value: 8.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFlgeDLAKKP-ENELIKLRGKdISMIF 98
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF---DFSQKPsEKAIRLLRQK-VGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQRQRIVIATALACEPKVL 178
Cdd:COG4161 89 QQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF---PLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGGQMVETGDVnEIFYDPK 249
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-239 |
2.62e-39 |
|
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: 138.54 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPENEliklrgKDISMIFQ 99
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE-----PTSGRIYIGGRDVTDLPPKD------RDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLI 179
Cdd:cd03301 80 N--YALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-244 |
4.27e-39 |
|
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: 139.22 E-value: 4.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPene 85
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL-----KPDSGSILIDGEDVRKEP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 lIKLRgKDISMIFQDPMTSLNPTmqiGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfKAypHQFSGGQRQRI 165
Cdd:COG4555 70 -REAR-RQIGVLPDERGLYDRLT---VRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDR-RV--GELSTGMKKKV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-258 |
5.62e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 139.33 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGEILFLGED-- 77
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvNGQTINLVRDkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 78 ----LAKKPENELIKLRgkdISMIFQDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnAEKRFKAY 153
Cdd:PRK10619 77 gqlkVADKNQLRLLRTR---LTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI--DERAQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGG 233
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQG 228
|
250 260
....*....|....*....|....*
gi 579304020 234 QMVETGDVNEIFYDPKHPYTWGLLS 258
Cdd:PRK10619 229 KIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-236 |
5.83e-39 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 138.23 E-value: 5.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAItklfqGDTGRIKKGEILFLGEDLAKKPEN 84
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLI-----GGLRSVQEGSLKVLGQELHGASKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRgKDISMIFQDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQR 164
Cdd:TIGR02982 76 QLVQLR-RRIGYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGL---GDHLNYYPHNLSGGQKQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDlGVVANIADRVAVMYGGQMV 236
Cdd:TIGR02982 150 VAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-234 |
1.33e-38 |
|
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: 135.59 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENELIKLrg 91
Cdd:cd03228 5 NVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDLRDLDLESLRKN-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 kdISMIFQDP----MTslnptmqigkqVMEplikhknyskaqakkraleilNLvglpnaekrfkayphqFSGGQRQRIVI 167
Cdd:cd03228 78 --IAYVPQDPflfsGT-----------IRE---------------------NI----------------LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 168 ATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAVMYGGQ 234
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-251 |
2.14e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.15 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGED-LAKKPENELIKLrgkDISMIF 98
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE-----ITSGDLIVDGLKvNDPKVDERLIRQ---EAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVL 178
Cdd:PRK09493 84 QQ--FYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHP 251
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-234 |
5.32e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.52 E-value: 5.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPeneL 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL-----KPTSGEILIDGKDIAKLP---L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 IKLRgKDISMIFQdpmtslnptmqigkqvmeplikhknyskaqakkraleilnlvglpnaekrfkayphqFSGGQRQRIV 166
Cdd:cd00267 69 EELR-RRIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 167 IATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-237 |
6.90e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 135.68 E-value: 6.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNdlHVSFDITAGEVQ--AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLA 79
Cdd:PRK10584 3 AENIVEVH--HLKKSVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSG-----EVSLVGQPLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPENELIKLRGKDISMIFQDPMtsLNPTMQIGKQVMEPLIKhKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSG 159
Cdd:PRK10584 76 QMDEEARAKLRAKHVGFVFQSFM--LIPTLNALENVELPALL-RGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVE 237
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-244 |
1.39e-37 |
|
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: 134.42 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeILFlGEDLAKKPenelIKLRgKDISMIFQ 99
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA----TVA-GHDVVREP----REVR-RRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPmtSLNPTMQiGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYphqFSGGQRQRIVIATALACEPKVLI 179
Cdd:cd03265 81 DL--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-247 |
1.69e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.89 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAKkpENeLIKLRG 91
Cdd:PRK13632 12 NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP-----QSGEIKIDGITISK--EN-LKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KdISMIFQdpmtslNPTMQ-IGKQVMEPL---IKHKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVI 167
Cdd:PRK13632 84 K-IGIIFQ------NPDNQfIGATVEDDIafgLENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 168 ATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVETGDVNEIFYD 247
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-235 |
3.18e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.02 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGevqaVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPene 85
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG-----EIYLDGKPLSAMP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDP----MTslnptmqIGKQVMEPL-IKHKNYSKAqakkRALEILNLVGLPNA--EKRFkaypHQFS 158
Cdd:COG4619 69 PPEWR-RQVAYVPQEPalwgGT-------VRDNLPFPFqLRERKFDRE----RALELLERLGLPPDilDKPV----ERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-244 |
4.05e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.77 E-value: 4.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTgrikkGEILFLGEDLAKKPEN 84
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS-----GEILLDGEPVRFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRgkdISMIFQDPmtSLNPTMqigkQVME------PLIKHKNYSKAQAKKRALEILNLVGLP-NAEKRFKAYphqf 157
Cdd:COG1129 75 DAQAAG---IAIIHQEL--NLVPNL----SVAEniflgrEPRRGGLIDWRAMRRRARELLARLGLDiDPDTPVGDL---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
....*..
gi 579304020 238 TGDVNEI 244
Cdd:COG1129 221 TGPVAEL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-245 |
4.57e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNdlHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGE---D 77
Cdd:PRK13635 1 MKEEIIRVE--HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 78 LAKKpeneliklrgkdISMIFQdpmtslNPTMQ-IGKQVMEPL---IKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaY 153
Cdd:PRK13635 79 VRRQ------------VGMVFQ------NPDNQfVGATVQDDVafgLENIGVPREEMVERVDQALRQVGMEDFLNR---E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGG 233
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
250
....*....|..
gi 579304020 234 QMVETGDVNEIF 245
Cdd:PRK13635 217 EILEEGTPEEIF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-253 |
1.93e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 132.48 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFDITAgevqAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGEILFLGEDLAKK 81
Cdd:PRK14246 8 EDVFNISRLYLYINDKA----ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 penELIKLRgKDISMIFQDPmtSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGL-PNAEKRFKAYPHQFSGG 160
Cdd:PRK14246 84 ---DAIKLR-KEVGMVFQQP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIdtAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
250
....*....|...
gi 579304020 241 VNEIFYDPKHPYT 253
Cdd:PRK14246 236 SNEIFTSPKNELT 248
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
5-227 |
2.94e-36 |
|
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: 130.97 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSF---DITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeILFLGE--DLA 79
Cdd:TIGR02324 1 LLEVEDLSKTFtlhQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRIL---VRHEGAwvDLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPENELIKLRGKDISMIFQdpMTSLNPTMQIGKQVMEPLIKhKNYSKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSG 159
Cdd:TIGR02324 78 QASPREVLEVRRKTIGYVSQ--FLRVIPRVSALEVVAEPLLE-RGVPREAARARARELLARLNIP--ERLWHLPPATFSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRV 227
Cdd:TIGR02324 153 GEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRV 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
6.36e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.74 E-value: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQGDTGRIK--KGEILFLGEDLaKKP 82
Cdd:PRK13639 1 ILETRDLKYSYP---DGTEALKGINFKAEKGEMVALLGPNGAGKST-------LFLHFNGILKptSGEVLIKGEPI-KYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLRgKDISMIFQDPmtslnptmqiGKQVMEPLIKHK--------NYSKAQAKKRALEILNLVGLPNAEKRfkaYP 154
Cdd:PRK13639 70 KKSLLEVR-KTVGIVFQNP----------DDQLFAPTVEEDvafgplnlGLSKEEVEKRVKEALKAVGMEGFENK---PP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:PRK13639 136 HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGK 214
|
250
....*....|....*
gi 579304020 235 MVETGDVNEIFYDPK 249
Cdd:PRK13639 215 IIKEGTPKEVFSDIE 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-238 |
1.91e-35 |
|
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: 126.77 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-----SGEILVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgkdISMIfqdpmtslnptmqigkqvmeplikhknyskaqakkraleilnlvglpnaekrfkaypHQFSGGQRQRI 165
Cdd:cd03216 72 ARRAG---IAMV---------------------------------------------------------YQLSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVET 238
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-267 |
2.56e-35 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 131.46 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 40 IVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPENelikLRGkdISMIFQDpmTSLNPTMQIGKQVMEPL 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI-----MLDGEDVTNVPPH----LRH--INMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 120 iKHKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLM 199
Cdd:TIGR01187 68 -KMRKVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 200 KELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLLSSMPDLSTTN 267
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATV 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-253 |
1.25e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 127.58 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAK 80
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 kPENELIKLRgKDISMIFQDPmtslNP-TMQIGKQVMEPL----IKHKNYSKAQAKK--RALEILNLVglpnaEKRFKAY 153
Cdd:PRK14239 77 -PRTDTVDLR-KEIGMVFQQP----NPfPMSIYENVVYGLrlkgIKDKQVLDEAVEKslKGASIWDEV-----KDRLHDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIADRVAVMYGG 233
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|
gi 579304020 234 QMVETGDVNEIFYDPKHPYT 253
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKET 243
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-244 |
1.76e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.30 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKK--- 81
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG-----EVLWDGEPLDPEdrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 -----PEnEliklRGkdismifqdpmtsLNPTMQIGKQVMEpLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfKAypHQ 156
Cdd:COG4152 72 rigylPE-E----RG-------------LYPKMKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANK-KV--EE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
....*...
gi 579304020 237 ETGDVNEI 244
Cdd:COG4152 209 LSGSVDEI 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-227 |
1.11e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.54 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgDTGriKKGEILFLGEDLAKKPENELIKLRGKDISMIFQdpMTS 104
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTP--TSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGKQVMEPL-IKHKNysKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:PRK11629 98 LLPDFTALENVAMPLlIGKKK--PAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579304020 184 TTALDVTMQAQILDLMKELQQKIDTAIIFITHDLgvvaNIADRV 227
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-245 |
1.17e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.61 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFDiTAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAkk 81
Cdd:PRK13650 1 MSNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-----QIIIDGDLLT-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 pENELIKLRGKdISMIFQdpmtslNPTMQ-IGKQVMEPL---IKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQF 157
Cdd:PRK13650 73 -EENVWDIRHK-IGMVFQ------NPDNQfVGATVEDDVafgLENKGIPHEEMKERVNEALELVGMQDFKER---EPARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVAnIADRVAVMYGGQMVE 237
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVES 220
|
....*...
gi 579304020 238 TGDVNEIF 245
Cdd:PRK13650 221 TSTPRELF 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-256 |
1.18e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.90 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilfLGEDL--AKKPENELIKLRgKDISMIF 98
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT------IGERVitAGKKNKKLKPLR-KKVGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QdpmtslNPTMQIGKQVMEPLIKH--KNY--SKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSGGQRQRIVIATALACE 174
Cdd:PRK13634 92 Q------FPEHQLFEETVEKDICFgpMNFgvSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 175 PKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTW 254
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
..
gi 579304020 255 GL 256
Cdd:PRK13634 244 GL 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-289 |
1.32e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.03 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDitaGEvQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKlFQGDTgrikKGEILFLGEDLAKKPEN 84
Cdd:PRK11607 19 LLEIRNLTKSFD---GQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPT----AGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 EliklrgKDISMIFQDpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQR 164
Cdd:PRK11607 90 Q------RPINMMFQS--YALFPHMTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVT----MQAQILDLMkelqQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 579304020 241 VNEIFYDPKHPYTWGLLSSMPDLSTT-----NDTPLLAIPGappdLLHPPKGDA 289
Cdd:PRK11607 234 PEEIYEHPTTRYSAEFIGSVNVFEGVlkerqEDGLVIDSPG----LVHPLKVDA 283
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-239 |
2.44e-33 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 130.72 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAkkpENELIKLRg 91
Cdd:COG2274 478 NVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI-----LIDGIDLR---QIDPASLR- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDP------------MTSLNPTMQigkQVMEplikhknyskaqakkrALEILNL----VGLPN------AEKR 149
Cdd:COG2274 549 RQIGVVLQDVflfsgtirenitLGDPDATDE---EIIE----------------AARLAGLhdfiEALPMgydtvvGEGG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 150 fkaypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIdtAIIFITHDLGVVANiADRVAV 229
Cdd:COG2274 610 -----SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIV 681
|
250
....*....|
gi 579304020 230 MYGGQMVETG 239
Cdd:COG2274 682 LDKGRIVEDG 691
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-245 |
4.56e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 4.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQGDTGRIK--KGEILFLGEDLAKKPENeLIKL 89
Cdd:PRK13637 10 HIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKST-------LIQHLNGLLKptSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 90 RgKDISMIFQdpmtslNPTMQIGKQVMEPLI----KHKNYSKAQAKKRALEILNLVGLPNAEKRFKAyPHQFSGGQRQRI 165
Cdd:PRK13637 82 R-KKVGLVFQ------YPEYQLFEETIEKDIafgpINLGLSEEEIENRVKRAMNIVGLDYEDYKDKS-PFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
8.27e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 122.64 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKkPENE 85
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYS-PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDPmtSLNPTMQIGKQV-----MEPLIKhknySKAQAKKRALEILNLVGLPNAEK-RFKAYPHQFSG 159
Cdd:PRK14267 80 PIEVR-REVGMVFQYP--NPFPHLTIYDNVaigvkLNGLVK----SKKELDERVEWALKKAALWDEVKdRLNDYPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqqKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
250
....*....|....
gi 579304020 240 DVNEIFYDPKHPYT 253
Cdd:PRK14267 231 PTRKVFENPEHELT 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-236 |
9.88e-33 |
|
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: 121.21 E-value: 9.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKPenel 86
Cdd:cd03226 1 RIENISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL-----IKESSGSILLNGKPIKAKE---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 iklRGKDISMIFQDPMTSLnptmqIGKQVMEPL-IKHKNYSKAQAKKRA-LEILNLVGLpnAEKrfkaYPHQFSGGQRQR 164
Cdd:cd03226 69 ---RRKSIGYVMQDVDYQL-----FTDSVREELlLGLKELDAGNEQAETvLKDLDLYAL--KER----HPLSLSGGQKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqQKIDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:cd03226 135 LAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-252 |
2.55e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.76 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAKKPENELIKLRGKDISMIFQDpmT 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP-----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--F 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 SLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKrfkAYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:PRK10070 116 ALMPHMTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 184 TTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPY 252
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
3.15e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.04 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFD-ITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEIL----FLGEDLA 79
Cdd:PRK13631 21 ILRVKNLYCVFDeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdkKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPENELIK----LRgKDISMIFQDPMTSLNPTMqIGKQVMEPLIKHKnYSKAQAKKRALEILNLVGLpnAEKRFKAYPH 155
Cdd:PRK13631 101 TNPYSKKIKnfkeLR-RRVSMVFQFPEYQLFKDT-IEKDIMFGPVALG-VKKSEAKKLAKFYLNKMGL--DDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLEVADEVIVMDKGKI 254
|
250
....*....|...
gi 579304020 236 VETGDVNEIFYDP 248
Cdd:PRK13631 255 LKTGTPYEIFTDQ 267
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-248 |
3.33e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.51 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilfLGEDLAKKPene 85
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT------LDGVPVTGP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liklrGKDISMIFQDpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQRQRI 165
Cdd:COG4525 75 -----GADRGVVFQK--DALLPWLNVLDNVAFGL-RLRGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDV----TMQAQILDLMKELQQkidtAIIFITHD------LG---VV-----ANIADRV 227
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQRTGK----GVFLITHSveealfLAtrlVVmspgpGRIVERL 219
|
250 260
....*....|....*....|.
gi 579304020 228 AVMYGGQMVETGDVNEIFYDP 248
Cdd:COG4525 220 ELDFSRRFLAGEDARAIKSDP 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-245 |
3.82e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPENEliklRGkdISMIFQDpmTSLNPT 108
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRI-----LWNGQDLTALPPAE----RP--VSMLFQE--NNLFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 109 MQIGKQV---MEPLIKhknYSKAQaKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADEPTT 185
Cdd:COG3840 86 LTVAQNIglgLRPGLK---LTAEQ-RAQVEQALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 186 ALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-244 |
5.10e-32 |
|
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: 119.85 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPENE 85
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL-----PPRSGSIRFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKlRGkdISMIFQDPMtsLNPTMQigkqVMEPL-IKHKNYSKAQAKKRALEILNLvgLPNAEKRFKAYPHQFSGGQRQR 164
Cdd:cd03224 72 RAR-AG--IGYVPEGRR--IFPELT----VEENLlLGAYARRRAKRKARLERVYEL--FPRLKERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-263 |
5.95e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 121.43 E-value: 5.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 18 TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEIlflgeDLAKKPENELIKLRGKDISMI 97
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDI-----TITHKTKDKYIRPVRKRIGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 98 FQDPMTslnptmQIGKQVMEPLI----KHKNYSKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSGGQRQRIVIATALAC 173
Cdd:PRK13646 91 FQFPES------QLFEDTVEREIifgpKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 174 EPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYT 253
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLAD 242
|
250
....*....|
gi 579304020 254 WGLlsSMPDL 263
Cdd:PRK13646 243 WHI--GLPEI 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-239 |
2.29e-31 |
|
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: 117.77 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTgrikkGEILFLGEDLAKKPENE 85
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS-----GEVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKL---RGkdismifqdpmtsLNPTMQIGKQVMEpLIKHKNYSKAQAKKRALEILNLVGL-PNAEKRFKayphQFSGGQ 161
Cdd:cd03269 72 IGYLpeeRG-------------LYPKMKVIDQLVY-LAQLKGLKKEEARRRIDEWLERLELsEYANKRVE----ELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-244 |
3.45e-31 |
|
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: 117.61 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTgRIKKGEILFLGEDLAKKPeneliKLRGKDISMIFQ 99
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLT----GEL-RPTSGTAYINGYSIRTDR-----KAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPMTSLNPTmqigkqVMEPLIKH---KNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQRQRIVIATALACEPK 176
Cdd:cd03263 83 FDALFDELT------VREHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 177 VLIADEPTTALDVTMQAQILDLMKELQQKidTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-248 |
3.55e-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: 120.98 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 10 DLHVSFDITAGEVqavrgvdfylnkgetLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGEILFlgeDLAKK----PEn 84
Cdd:COG4148 15 TLDVDFTLPGRGV---------------TALFGPSGSGKTTLLRAIAGLERPDSGRIRlGGEVLQ---DSARGiflpPH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 elikLRGkdISMIFQDPmtSLNPTMQIGKQVmepLIKHKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQR 164
Cdd:COG4148 76 ----RRR--IGYVFQEA--RLFPHLSVRGNL---LYGRKRAPRAERRISFDEVVELLGI---GHLLDRRPATLSGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
....
gi 579304020 245 FYDP 248
Cdd:COG4148 222 LSRP 225
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
35-313 |
3.72e-31 |
|
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: 120.87 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 35 GETLAIVGESGSGKSVTTKAITKLFQGDTgriKKGEILFLGEDLAKKPENEliklrgKDISMIFQDpmTSLNPTMQIGKQ 114
Cdd:TIGR03258 31 GELLALIGKSGCGKTTLLRAIAGFVKAAG---LTGRIAIADRDLTHAPPHK------RGLALLFQN--YALFPHLKVEDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 115 VMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQ 194
Cdd:TIGR03258 100 VAFGL-RAQKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 195 ILDLMKELQQKI-DTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLLSSmPDLSTTNDTPLLA 273
Cdd:TIGR03258 176 MREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGA-ANILPAIALGITE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 579304020 274 IPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPPWFKVSP 313
Cdd:TIGR03258 255 APGLVDVSCGGAVIFAFGDGRHDGRDKLACIRPEHLALTP 294
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-239 |
7.29e-31 |
|
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: 116.63 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLN-----KGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGEILFLGEDLAKKPENEliklrgKDISMIFQDpm 102
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlNGTVLFDSRKKINLPPQQ------RKIGLVFQQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 103 TSLNPTMQIGKQVMEPLIKHKNyskAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:cd03297 84 YALFPHLNVRENLAFGLKRKRN---REDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 183 PTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-243 |
1.10e-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: 122.56 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLAKKPENE 85
Cdd:COG4988 337 IELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-----GVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LiklrGKDISMIFQDPMTsLNPTmqigkqVMEPL-IKHKNYSKAQAKkRALEilnLVGLpnaeKRF-KAYPHQF------ 157
Cdd:COG4988 409 W----RRQIAWVPQNPYL-FAGT------IRENLrLGRPDASDEELE-AALE---AAGL----DEFvAALPDGLdtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 -----SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAVMYG 232
Cdd:COG4988 470 ggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDD 546
|
250
....*....|.
gi 579304020 233 GQMVETGDVNE 243
Cdd:COG4988 547 GRIVEQGTHEE 557
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-236 |
1.31e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.13 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKPENELIKLRgKDISMIFQ 99
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPMTSLNPTmqIGKQVMEPLIKhKNYSKAQAKKRALEILNLVGLPNaekRFKAYPHQFSGGQRQRIVIATALACEPKVLI 179
Cdd:PRK10908 87 DHHLLMDRT--VYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELqQKIDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-249 |
1.32e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 118.26 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDI-TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRI----------KKGEIL-- 72
Cdd:PRK13651 3 IKVKNIVKIFNKkLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 73 FLGEDLAKKPENELIK----LRgKDISMIFQdpmtslNPTMQIGKQVMEPLI----KHKNYSKAQAKKRALEILNLVGLP 144
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKkikeIR-RRVGVVFQ------FAEYQLFEQTIEKDIifgpVSMGVSKEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 145 naEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIA 224
Cdd:PRK13651 156 --ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWT 232
|
250 260
....*....|....*....|....*
gi 579304020 225 DRVAVMYGGQMVETGDVNEIFYDPK 249
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-240 |
1.55e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 122.18 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:COG4987 334 LELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LiklRGKdISMIFQDP---MTSLNPTMQIGKQvmeplikhknyskaQAKKRAL-EILNLVGLpnaEKRFKAYPH------ 155
Cdd:COG4987 407 L---RRR-IAVVPQRPhlfDTTLRENLRLARP--------------DATDEELwAALERVGL---GDWLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 -----QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLgVVANIADRVAVM 230
Cdd:COG4987 466 geggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVL 542
|
250
....*....|
gi 579304020 231 YGGQMVETGD 240
Cdd:COG4987 543 EDGRIVEQGT 552
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-253 |
2.19e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.28 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDITagevQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAK 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG-----RIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENEliklrgKDISMIFQDpmTSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPN-AEKRfkayPHQFSG 159
Cdd:PRK09452 81 VPAEN------RHVNTVFQS--YALFPHMTVFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEfAQRK----PHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
250
....*....|....
gi 579304020 240 DVNEIFYDPKHPYT 253
Cdd:PRK09452 228 TPREIYEEPKNLFV 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-235 |
2.80e-30 |
|
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: 114.81 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKPENELIKLRGKdISMIFQ 99
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DpmTSLNPTMQIGKQVMEPL--IKHKnysKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKV 177
Cdd:cd03292 86 D--FRLLPDRNVYENVAFALevTGVP---PREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 178 LIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-239 |
4.54e-30 |
|
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: 114.39 E-value: 4.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPEN 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQDPMTslnptmqiGKQVMEPLIKHKNYSKAQAKKRALEILNLVGL-PNAEKRFKAyphqFSGGQRQ 163
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLT--------ARENLEYFAGLYGLKGDELTARLEELADRLGMeELLDRRVGG----FSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-239 |
5.27e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.65 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPENE 85
Cdd:COG1132 340 IEFENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY-----DPTSGRILIDGVDIRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLrgkdISMIFQDPM---TSL--NptMQIGKqvmeplikhKNYSKAQAKkRALEILNlvglpnAEKRFKAYPHQF--- 157
Cdd:COG1132 412 LRRQ----IGVVPQDTFlfsGTIreN--IRYGR---------PDATDEEVE-EAAKAAQ------AHEFIEALPDGYdtv 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 --------SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAV 229
Cdd:COG1132 470 vgergvnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILV 546
|
250
....*....|
gi 579304020 230 MYGGQMVETG 239
Cdd:COG1132 547 LDDGRIVEQG 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-243 |
6.73e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLA- 79
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD-----SGEILIDGKPVRi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPeNELIKLRgkdISMIFQDPMtsLNPTM------QIGkqvMEPLiKHKNYSKAQAKKRALEILNLVGL---PNAekrf 150
Cdd:COG3845 72 RSP-RDAIALG---IGMVHQHFM--LVPNLtvaeniVLG---LEPT-KGGRLDRKAARARIRELSERYGLdvdPDA---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 151 kaYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALdvTMQ--AQILDLMKELQQKiDTAIIFITHDLGVVANIADRVA 228
Cdd:COG3845 138 --KVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVT 212
|
250
....*....|....*
gi 579304020 229 VMYGGQMVETGDVNE 243
Cdd:COG3845 213 VLRRGKVVGTVDTAE 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-249 |
7.43e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 114.31 E-value: 7.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLAKKP 82
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL-----LPPRSGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKlRGkdISM------IFQDpMTslnptmqigkqVMEPLI--KHKNYSKAQAKKRALEILNLvgLPNAEKRFKAYP 154
Cdd:COG0410 72 PHRIAR-LG--IGYvpegrrIFPS-LT-----------VEENLLlgAYARRDRAEVRADLERVYEL--FPRLKERRRQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:COG0410 135 GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGR 213
|
250
....*....|....*
gi 579304020 235 MVETGDVNEIFYDPK 249
Cdd:COG0410 214 IVLEGTAAELLADPE 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-248 |
1.15e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.72 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilFLGEDLAKkpene 85
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIR-----FHGTDVSR----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 lIKLRGKDISMIFQD-----PMTSLNpTMQIGKQVmepLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGG 160
Cdd:PRK10851 69 -LHARDRKVGFVFQHyalfrHMTVFD-NIAFGLTV---LPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
....*...
gi 579304020 241 VNEIFYDP 248
Cdd:PRK10851 221 PDQVWREP 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-247 |
1.19e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.33 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQGDTGRIK--KGEILFLGE-- 76
Cdd:PRK13636 1 MEDYILKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKST-------LFQNLNGILKpsSGRILFDGKpi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 77 DLAKKpenELIKLRgKDISMIFQDPMTSLNPTMQIGKQVMEPLikHKNYSKAQAKKRALEILNLVGLpnaeKRFKAYP-H 155
Cdd:PRK13636 71 DYSRK---GLMKLR-ESVGMVFQDPDNQLFSASVYQDVSFGAV--NLKLPEDEVRKRVDNALKRTGI----EHLKDKPtH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:PRK13636 141 CLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
250
....*....|..
gi 579304020 236 VETGDVNEIFYD 247
Cdd:PRK13636 221 ILQGNPKEVFAE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-248 |
4.98e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNdlHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGriKKGEILFLGEDLAK 80
Cdd:PRK13640 1 MKDNIVEFK--HVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDN--PNSKITVDGITLTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KpenELIKLRGKdISMIFQdpmtslNPTMQ-IGKQVMEPL---IKHKNYSKAQAKKRALEILNLVGLPNAEKrfkAYPHQ 156
Cdd:PRK13640 77 K---TVWDIREK-VGIVFQ------NPDNQfVGATVGDDVafgLENRAVPRPEMIKIVRDVLADVGMLDYID---SEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGvVANIADRVAVMYGGQMV 236
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLL 222
|
250
....*....|..
gi 579304020 237 ETGDVNEIFYDP 248
Cdd:PRK13640 223 AQGSPVEIFSKV 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-236 |
5.15e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.87 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDI-TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPE 83
Cdd:COG1101 1 MLELKNLSKTFNPgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI-----LIDGKDVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 84 NEliklRGKDISMIFQDPMTSLNPTMQIGkqvmEPLI------KHKNYSKAQAKKR------ALEILNLvGLpnaEKRFK 151
Cdd:COG1101 76 YK----RAKYIGRVFQDPMMGTAPSMTIE----ENLAlayrrgKRRGLRRGLTKKRrelfreLLATLGL-GL---ENRLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 152 AYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKEL--QQKIDTaiIFITHDLGVVANIADRVAV 229
Cdd:COG1101 144 TKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTT--LMVTHNMEQALDYGNRLIM 221
|
....*..
gi 579304020 230 MYGGQMV 236
Cdd:COG1101 222 MHEGRII 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
5.55e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQGDTGRIK--KGEILFLGEDLAKKP 82
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKST-------LFRHFNGILKptSGSVLIRGEPITKEN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLRGkdisMIFQdpmtslNPTMQIGKQVMEPLIK----HKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFS 158
Cdd:PRK13652 73 IREVRKFVG----LVFQ------NPDDQIFSPTVEQDIAfgpiNLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVET 238
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
250
....*....|
gi 579304020 239 GDVNEIFYDP 248
Cdd:PRK13652 220 GTVEEIFLQP 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-249 |
6.10e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 6.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFYLNKGETLAIVGESGSGKsvTTkaITKLFQGdtgrIKK---GEILFLGEDLAKKpeneliKLRGKDISMIFQDpmTS 104
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGK--TT--VLRLVAG----LEKpteGQIFIDGEDVTHR------SIQQRDICMVFQS--YA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADEPT 184
Cdd:PRK11432 89 LFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 185 TALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPK 249
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-235 |
1.07e-28 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 109.83 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSfditagevQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKP 82
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR-----PPASGEITLDGKPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLRgkdISMIFQDPM-TSLNPTMQIGKqvmeplikhknyskaqakkraleilNLVGlpnaekrfkayPHQFSGGQ 161
Cdd:cd03215 69 PRDAIRAG---IAYVPEDRKrEGLVLDLSVAE-------------------------NIAL-----------SSLLSGGN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-247 |
1.46e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.15 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 13 VSFDITAG---EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDlakkpENELIKL 89
Cdd:PRK13649 8 VSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-----KNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 90 RGKDISMIFQDPMTSLNPTMQIGKQVMEPlikhKNY--SKAQAKKRALEILNLVGLpnAEKRFKAYPHQFSGGQRQRIVI 167
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEETVLKDVAFGP----QNFgvSQEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 168 ATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYD 247
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-256 |
1.68e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.77 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNdlHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaITKLFQGdTGRIKKGEILFlgEDLAK 80
Cdd:PRK13648 3 DKNSIIVFK--NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKST----IAKLMIG-IEKVKSGEIFY--NNQAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENeLIKLRgKDISMIFQDPMTSLNPTMqIGKQVMEPLIKHK-NYSKAQAK-KRALEILNLVGLPNAEkrfkayPHQFS 158
Cdd:PRK13648 74 TDDN-FEKLR-KHIGIVFQNPDNQFVGSI-VKYDVAFGLENHAvPYDEMHRRvSEALKQVDMLERADYE------PNALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVET 238
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKE 223
|
250
....*....|....*...
gi 579304020 239 GDVNEIFYDPKHPYTWGL 256
Cdd:PRK13648 224 GTPTEIFDHAEELTRIGL 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-267 |
3.52e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.96 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 39 AIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKpeNELIKLRgKDISMIFQDPmtslNP-TMQIGKQVME 117
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNY--RDVLEFR-RRVGMLFQRP----NPfPMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 118 PLIKHKNYSKAQAKKRALEILNLVGLPNAEK-RFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQIL 196
Cdd:PRK14271 124 GVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 197 DLMKELQQKIdtAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHP----YTWGLLSSMPDLSTTN 267
Cdd:PRK14271 204 EFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSGDVKDAKRGN 276
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-245 |
5.42e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 4 RILEVNDLHVSFDiTAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilFLGEDLAKKpe 83
Cdd:PRK13642 3 KILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK-----IDGELLTAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 84 nELIKLRGKdISMIFQDPMTSLnptmqIGKQVMEPL---IKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGG 160
Cdd:PRK13642 75 -NVWNLRRK-IGMVFQNPDNQF-----VGATVEDDVafgMENQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVETGD 240
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA 223
|
....*
gi 579304020 241 VNEIF 245
Cdd:PRK13642 224 PSELF 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-245 |
6.76e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 6.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeilfLGEDLAKKPENELIKLRGKdISMIFQdpmt 103
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-------YVDGLDTSDEENLWDIRNK-AGMVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 slNPTMQIGKQVMEPLI----KHKNYSKAQAKKRALEILNLVGLpnaeKRFKAY-PHQFSGGQRQRIVIATALACEPKVL 178
Cdd:PRK13633 93 --NPDNQIVATIVEEDVafgpENLGIPPEEIRERVDESLKKVGM----YEYRRHaPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVETGDVNEIF 245
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-243 |
7.21e-28 |
|
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: 109.17 E-value: 7.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFD-ITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAkkpENELIKLR 90
Cdd:cd03249 5 NVSFRyPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYD-----PTSGEILLDGVDIR---DLNLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 91 GKdISMIFQDPM---TSL--NPTMQIGKQVMEPLIkhknyskaQAKKRAlEILNLV-GLPNA-EKRFKAYPHQFSGGQRQ 163
Cdd:cd03249 77 SQ-IGLVSQEPVlfdGTIaeNIRYGKPDATDEEVE--------EAAKKA-NIHDFImSLPDGyDTLVGERGSQLSGGQKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQIldlmkelQQKIDTAI-----IFITHDLGVVANiADRVAVMYGGQMVET 238
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLV-------QEALDRAMkgrttIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
....*
gi 579304020 239 GDVNE 243
Cdd:cd03249 219 GTHDE 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-245 |
9.27e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 9.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSfditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTgRIKKGEILFLGEDLAKKPENE 85
Cdd:COG4559 2 LEAENLSVR----LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT----GEL-TPSSGEVRLNGRPLAAWSPWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGkdisMIFQDpmTSLN---PTMQIgkqVMEPLIKHKNySKAQAKKRALEILNLVGLPNAEKRFkaYPhQFSGGQR 162
Cdd:COG4559 73 LARRRA----VLPQH--SSLAfpfTVEEV---VALGRAPHGS-SAAQDRQIVREALALVGLAHLAGRS--YQ-TLSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 163 QRIVIATALA-------CEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
250
....*....|
gi 579304020 236 VETGDVNEIF 245
Cdd:COG4559 219 VAQGTPEEVL 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-239 |
2.31e-27 |
|
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: 106.89 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGeTLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPEne 85
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-----SGTIRIDGQDVLKQPQ-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liKLRGKdISMIFQDPMTSLNPTmqigkqVMEPLiKH----KNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQ 161
Cdd:cd03264 69 --KLRRR-IGYLPQEFGVYPNFT------VREFL-DYiawlKGIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-236 |
3.16e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.90 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLAKKPEN 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-----GQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLRGKDISMIFQdpMTSLNPTMQIGKQVMEPLIkHKNYSKAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQRQR 164
Cdd:PRK10535 79 ALAQLRREHFGFIFQ--RYHLLSHLTAAQNVEVPAV-YAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDlGVVANIADRVAVMYGGQMV 236
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-244 |
4.23e-27 |
|
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: 106.84 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPENE 85
Cdd:TIGR03410 1 LEVSNLNVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP-----VKSGSIRLDGEDITKLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKL------RGKdisMIFqdPMTSLNPTMQIGkqvMEPLikhknysKAQAKKRALEILNLvglpnaekrfkaYP--HQF 157
Cdd:TIGR03410 72 RARAgiayvpQGR---EIF--PRLTVEENLLTG---LAAL-------PRRSRKIPDEIYEL------------FPvlKEM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 --------SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAV 229
Cdd:TIGR03410 125 lgrrggdlSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYV 204
|
250
....*....|....*
gi 579304020 230 MYGGQMVETGDVNEI 244
Cdd:TIGR03410 205 MERGRVVASGAGDEL 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-240 |
4.29e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 107.08 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitagEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTG-RIKKGEILFLGEDLAKKPEN 84
Cdd:COG0396 1 LEIKNLHVSVE----GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM----GHPKyEVTSGSILLDGEDILELSPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLrGkdISMIFQDPM------------TSLNptmqigkQVMEPLIkhknySKAQAKKRALEILNLVGLPnaekrfKA 152
Cdd:COG0396 73 ERARA-G--IFLAFQYPVeipgvsvsnflrTALN-------ARRGEEL-----SAREFLKLLKEKMKELGLD------ED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 YPHQ-----FSGGQRQRIVIATALACEPKVLIADEPTTALDV-TMQAqILDLMKELQQKiDTAIIFITHDLGVVANI-AD 225
Cdd:COG0396 132 FLDRyvnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPD 209
|
250
....*....|....*
gi 579304020 226 RVAVMYGGQMVETGD 240
Cdd:COG0396 210 FVHVLVDGRIVKSGG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-249 |
9.19e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.61 E-value: 9.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 18 TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQGDTGRIK--KGEILFLGEDLAKKPENELIKLRGKDIS 95
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKST-------LMQHFNALLKpsSGTITIAGYHITPETGNKNLKKLRKKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 96 MIFQDPMTSLNPTMQIGKQVMEPliKHKNYSKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSGGQRQRIVIATALACEP 175
Cdd:PRK13641 89 LVFQFPEAQLFENTVLKDVEFGP--KNFGFSEDEAKEKALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 176 KVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPK 249
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-247 |
1.56e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 23 QAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKpenelIKLRGKDISMIFQDPM 102
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKE-----IKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 103 TSLNPTMQIGKQVMEPliKHKNYSKAQAKKRALEILNLVGLpnAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:PRK13643 95 SQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGL--ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 183 PTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYD 247
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-239 |
1.94e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTgRIKKGEILFLGEDLAKKPENE 85
Cdd:PRK13548 3 LEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS----GEL-SPDSGEVRLNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRG---KDISMIFqdPMTslnptmqigkqVME----PLIKHKNySKAQAKKRALEILNLVGLPNAEKRFkaYPhQFS 158
Cdd:PRK13548 74 LARRRAvlpQHSSLSF--PFT-----------VEEvvamGRAPHGL-SRAEDDALVAAALAQVDLAHLAGRD--YP-QLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALA------CEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
....*..
gi 579304020 233 GQMVETG 239
Cdd:PRK13548 217 GRLVADG 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-216 |
2.60e-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: 104.10 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKsvTT--KAITKLFQGDtgrikKGEILFLGEDLAKKPE 83
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGK--TTllRILAGLLPPS-----AGEVLWNGEPIRDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 84 NeliklRGKDISMIFQDPMtsLNPTMQigkqVMEPL-IKHKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQR 162
Cdd:COG4133 72 D-----YRRRLAYLGHADG--LKPELT----VRENLrFWAALYGLRADREAIDEALEAVGLAGLADLP---VRQLSAGQK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579304020 163 QRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHD 216
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-239 |
2.72e-26 |
|
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: 104.61 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENEL 86
Cdd:cd03254 4 EFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-----KGQILIDGIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 IKLrgkdISMIFQDPmTSLNPTmqigkqVMEPLIKHKNYSKAQAKKRALEILNLVGLpnAEKRFKAYPHQ-------FSG 159
Cdd:cd03254 76 RSM----IGVVLQDT-FLFSGT------IMENIRLGRPNATDEEVIEAAKEAGAHDF--IMKLPNGYDTVlgenggnLSQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIfITHDLGVVANiADRVAVMYGGQMVETG 239
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKG-RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-244 |
5.70e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 108.74 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSF-DITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeiLFLGE---DL 78
Cdd:TIGR03269 277 EPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN----VRVGDewvDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 79 AKKPENEliklRG---KDISMIFQD----PMTSL--NPTMQIGKQVMEPLikhknyskaqAKKRALEILNLVGLPN--AE 147
Cdd:TIGR03269 353 TKPGPDG----RGrakRYIGILHQEydlyPHRTVldNLTEAIGLELPDEL----------ARMKAVITLKMVGFDEekAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 148 KRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALD----VTMQAQILDLMKELQQkidTAIIfITHDLGVVANI 223
Cdd:TIGR03269 419 EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ---TFII-VSHDMDFVLDV 494
|
250 260
....*....|....*....|.
gi 579304020 224 ADRVAVMYGGQMVETGDVNEI 244
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-241 |
6.15e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 102.99 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSfditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTG-RIKKGEILFLGEDLAKKPEN 84
Cdd:cd03217 1 LEIKDLHVS----VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM----GHPKyEVTEGEILFKGEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLrgkDISMIFQDPmtslnptMQIgkqvmePLIKHKNYskaqakkraLEILNlVGlpnaekrfkayphqFSGGQRQR 164
Cdd:cd03217 73 ERARL---GIFLAFQYP-------PEI------PGVKNADF---------LRYVN-EG--------------FSGGEKKR 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHdLGVVAN--IADRVAVMYGGQMVETGDV 241
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITH-YQRLLDyiKPDRVHVLYDGRIVKSGDK 189
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-245 |
6.49e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 6.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 18 TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEIlflgedlaKKPEN-----ELIKLRgK 92
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDY--------AIPANlkkikEVKRLR-K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 93 DISMIFQdpmtslNPTMQIGKQVMEPLIK----HKNYSKAQAKKRALEILNLVGLPnaEKRFKAYPHQFSGGQRQRIVIA 168
Cdd:PRK13645 91 EIGLVFQ------FPEYQLFQETIEKDIAfgpvNLGENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 169 TALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-244 |
6.84e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.51 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDItAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilFLGEDLAKkpenelIKLRG 91
Cdd:PRK13657 339 DVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL-----IDGTDIRT------VTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 --KDISMIFQDPM---TSLNPTMQIGKQVMEPLIKHKNYSKAQA----KKRALEILNLVGlpnaEKrfkayPHQFSGGQR 162
Cdd:PRK13657 407 lrRNIAVVFQDAGlfnRSIEDNIRVGRPDATDEEMRAAAERAQAhdfiERKPDGYDTVVG----ER-----GRQLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 163 QRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIifITHDLGVVANiADRVAVMYGGQMVETGDVN 242
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNGRVVESGSFD 554
|
..
gi 579304020 243 EI 244
Cdd:PRK13657 555 EL 556
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-244 |
7.41e-26 |
|
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: 103.72 E-value: 7.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPENELIKLRG 91
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDI--SMIF----QDPMTSLNPTMQigkqvMEPLIKHKNYSKAQAKKRAL-----EIL--NLVGLpnaekrfkayphqfS 158
Cdd:cd03252 80 VVLqeNVLFnrsiRDNIALADPGMS-----MERVIEAAKLAGAHDFISELpegydTIVgeQGAGL--------------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqQKIDTAIIfITHDLGVVANiADRVAVMYGGQMVET 238
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVII-IAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
....*.
gi 579304020 239 GDVNEI 244
Cdd:cd03252 218 GSHDEL 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-239 |
2.59e-25 |
|
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: 101.52 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDlAKKPENE 85
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG-----EITFDGKS-YQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LiklrgKDISMIFQDPmtSLNPTMQigkqVMEPLIKHKNYsKAQAKKRALEILNLVGLPNAEKRfKAypHQFSGGQRQRI 165
Cdd:cd03268 71 L-----RRIGALIEAP--GFYPNLT----ARENLRLLARL-LGIRKKRIDEVLDVVGLKDSAKK-KV--KGFSLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGIT-VLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-216 |
2.78e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.40 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLhvsfDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqG--DTGRIKKGEILFLGEDLAKKPe 83
Cdd:COG4136 2 LSLENL----TITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA----GtlSPAFSASGEVLLNGRRLTALP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 84 nelIKLRGkdISMIFQDPMtsLNPTMQIGKQVMEPLikHKNYSKAQAKKRALEILNLVGLPNaekRFKAYPHQFSGGQRQ 163
Cdd:COG4136 73 ---AEQRR--IGILFQDDL--LFPHLSVGENLAFAL--PPTIGRAQRRARVEQALEEAGLAG---FADRDPATLSGGQRA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHD 216
Cdd:COG4136 141 RVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-239 |
4.60e-25 |
|
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: 101.03 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPeneliklrgkdISMIFQDpmTSLNPT 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-----------VSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 109 MQIGKQV---MEPLIKhknySKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQRQRIVIATALACEPKVLIADEPTT 185
Cdd:cd03298 85 LTVEQNVglgLSPGLK----LTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579304020 186 ALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-252 |
6.61e-25 |
|
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: 103.65 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGEILFlgeDLAKKPENELIKLRgkdISMIFQDpmTSLN 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlNGRTLF---DSRKGIFLPPEKRR---IGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 107 PTMQigkqVMEPLIKhkNYSKAQAKKRAL---EILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:TIGR02142 88 PHLS----VRGNLRY--GMKRARPSERRIsfeRVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 184 TTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPY 252
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-239 |
6.74e-25 |
|
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: 101.25 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGE-----------------VQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKK 68
Cdd:cd03267 1 IEVSNLSKSYRVYSKEpgligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 69 GEILflgedlakkPENELIKLRgKDISMIFQD---------PMTSLNptmqigkqvmepLIKH-KNYSKAQAKKRALEIL 138
Cdd:cd03267 81 AGLV---------PWKRRKKFL-RRIGVVFGQktqlwwdlpVIDSFY------------LLAAiYDLPPARFKKRLDELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 139 NLVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLG 218
Cdd:cd03267 139 ELLDL---EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
250 260
....*....|....*....|.
gi 579304020 219 VVANIADRVAVMYGGQMVETG 239
Cdd:cd03267 216 DIEALARRVLVIDKGRLLYDG 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-244 |
8.95e-25 |
|
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: 105.18 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAkkpENELIKLRg 91
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-----SGQILLDGHDLA---DYTLASLR- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDPMTsLNPTM--QIGKQVMEplikhkNYSKAQAKkRALEILNLV----GLPNA------EKRFKayphqFSG 159
Cdd:TIGR02203 406 RQVALVSQDVVL-FNDTIanNIAYGRTE------QADRAEIE-RALAAAYAQdfvdKLPLGldtpigENGVL-----LSG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaiIFITHDLGVVANiADRVAVMYGGQMVETG 239
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
....*
gi 579304020 240 DVNEI 244
Cdd:TIGR02203 550 THNEL 554
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-239 |
1.37e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENE 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAG-----TVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LiklrGKDISMIFQDPMTSLNPTmqiGKQVMEpLIKHKNYSK----AQAKKRALE-ILNLVGLpnaeKRFKAYP-HQFSG 159
Cdd:PRK09536 75 A----SRRVASVPQDTSLSFEFD---VRQVVE-MGRTPHRSRfdtwTETDRAAVErAMERTGV----AQFADRPvTSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFItHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-245 |
1.39e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAKKPEN 84
Cdd:PRK11231 2 TLRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-----QSGTVFLGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELiklrGKDISMIFQDPMTSLNPTMQ----IGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnAEKRFKAyphqFSGG 160
Cdd:PRK11231 73 QL----ARRLALLPQHHLTPEGITVRelvaYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHL--ADRRLTD----LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
....*
gi 579304020 241 VNEIF 245
Cdd:PRK11231 222 PEEVM 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-244 |
1.54e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtG--RIKKGEILFLGEDLAK 80
Cdd:COG3845 255 EVVLEVENLSVRDD---RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALA-------GlrPPASGSIRLDGEDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRgkdISMIFQDPM-TSLNPTMQI------GKQVMEPLIKHKNYSKAQAKKRALEILNL--VGLPNAEKRFK 151
Cdd:COG3845 325 LSPRERRRLG---VAYIPEDRLgRGLVPDMSVaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEfdVRTPGPDTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 152 AyphqFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMY 231
Cdd:COG3845 402 S----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMY 476
|
250
....*....|...
gi 579304020 232 GGQMVETGDVNEI 244
Cdd:COG3845 477 EGRIVGEVPAAEA 489
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-248 |
1.76e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.50 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITagevQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPENe 85
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDP----------------MTSLNPTMQIgKQVMEPLIKHKNY---SKAQAKKRALEIlnlvglpna 146
Cdd:PRK14258 83 LNRLR-RQVSMVHPKPnlfpmsvydnvaygvkIVGWRPKLEI-DDIVESALKDADLwdeIKHKIHKSALDL--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 147 ekrfkayphqfSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADR 226
Cdd:PRK14258 152 -----------SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
250 260
....*....|....*....|....*..
gi 579304020 227 VAVMYG-----GQMVETGDVNEIFYDP 248
Cdd:PRK14258 221 TAFFKGnenriGQLVEFGLTKKIFNSP 247
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-243 |
3.19e-24 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 99.23 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAkkpENELIKLRg 91
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-----LIDGHDVR---DYTLASLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDPMTsLNPTmqigkqVMEPLIkhknYSKAQAKKRALEilnlvglpNAEKrfKAYPHQF-------------- 157
Cdd:cd03251 76 RQIGLVSQDVFL-FNDT------VAENIA----YGRPGATREEVE--------EAAR--AANAHEFimelpegydtvige 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 -----SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIfITHDLGVVANiADRVAVMYG 232
Cdd:cd03251 135 rgvklSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTIEN-ADRIVVLED 211
|
250
....*....|.
gi 579304020 233 GQMVETGDVNE 243
Cdd:cd03251 212 GKIVERGTHEE 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-248 |
3.55e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.46 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 19 AGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLfqgdtGRIKKGEILFLGEDLakkpeNELiKLRGKDISMIF 98
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-----ERITSGEIWIGGRVV-----NEL-EPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDpmTSLNPTMQIgKQVMEPLIKHKNYSKAQAKKRALE---ILNLvglpnaEKRFKAYPHQFSGGQRQRIVIATALACEP 175
Cdd:PRK11650 83 QN--YALYPHMSV-RENMAYGLKIRGMPKAEIEERVAEaarILEL------EPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 176 KVLIADEPTTALD----VTMQAQIldlmKELQQKIDTAIIFITHDlGVVA-NIADRVAVMYGGQMVETGDVNEIFYDP 248
Cdd:PRK11650 154 AVFLFDEPLSNLDaklrVQMRLEI----QRLHRRLKTTSLYVTHD-QVEAmTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-244 |
5.06e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.00 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERIlEVNDLHVSFDI------------------TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGD 62
Cdd:COG1134 1 MSSMI-EVENVSKSYRLyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 63 TGRIK-KGEILFL------------GEdlakkpENelIKLRGkdismifqdpmtslnptmqigkQVMeplikhkNYSKAQ 129
Cdd:COG1134 80 SGRVEvNGRVSALlelgagfhpeltGR------EN--IYLNG----------------------RLL-------GLSRKE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 130 AKKRALEILNLVGLPNAEKR-FKAYphqfSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDT 208
Cdd:COG1134 123 IDEKFDEIVEFAELGDFIDQpVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT 198
|
250 260 270
....*....|....*....|....*....|....*.
gi 579304020 209 aIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG1134 199 -VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-248 |
9.69e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgDTGrikkGEILFLGEDLAK 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYK-PTG----GTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKlrgKDISMIFQD-----PMTSLNPTM-----QIGKQVMEPLIKHKNYSKAQAKK--RA---LEILNLVGLPN 145
Cdd:PRK11300 72 LPGHQIAR---MGVVRTFQHvrlfrEMTVIENLLvaqhqQLKTGLFSGLLKTPAFRRAESEAldRAatwLERVGLLEHAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 146 AEKRFKAYphqfsgGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIAD 225
Cdd:PRK11300 149 RQAGNLAY------GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISD 222
|
250 260
....*....|....*....|...
gi 579304020 226 RVAVMYGGQMVETGDVNEIFYDP 248
Cdd:PRK11300 223 RIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-259 |
9.70e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.49 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPENEliklRGkdISMIFQ 99
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED-----ITSGDLFIGEKRMNDVPPAE----RG--VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 D----PMTSLNPTMQIGkqvmeplIKHKNYSKAQAKKR---ALEILNLVGLpnAEKRFKAyphqFSGGQRQRIVIATALA 172
Cdd:PRK11000 83 SyalyPHLSVAENMSFG-------LKLAGAKKEEINQRvnqVAEVLQLAHL--LDRKPKA----LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 173 CEPKVLIADEPTTALD----VTMQAQIldlmKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDP 248
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDaalrVQMRIEI----SRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
250
....*....|.
gi 579304020 249 KHPYTWGLLSS 259
Cdd:PRK11000 226 ANRFVAGFIGS 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-239 |
1.13e-23 |
|
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: 97.69 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAkkpENE 85
Cdd:cd03253 1 IEFENVTFAYD---PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-----LIDGQDIR---EVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRgKDISMIFQDpmTSL-NPTmqIGKQvmeplIKHKN--------YSKAQAKKRALEILNL-------VGlpnaEKR 149
Cdd:cd03253 70 LDSLR-RAIGVVPQD--TVLfNDT--IGYN-----IRYGRpdatdeevIEAAKAAQIHDKIMRFpdgydtiVG----ERG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 150 FKayphqFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaiIFITHDLGVVANiADRVAV 229
Cdd:cd03253 136 LK-----LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVN-ADKIIV 207
|
250
....*....|
gi 579304020 230 MYGGQMVETG 239
Cdd:cd03253 208 LKDGRIVERG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-238 |
1.22e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.54 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLF-QGDTgrikKGEILFLGEDLA 79
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYpHGTY----EGEIIFEGEELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KK--PENEliklrGKDISMIFQDPMtsLNPTMQIGKQVM---EPLIKHK-NYSKAQAkkRALEILNLVGLP-NAEKRFKA 152
Cdd:PRK13549 73 ASniRDTE-----RAGIAIIHQELA--LVKELSVLENIFlgnEITPGGImDYDAMYL--RAQKLLAQLKLDiNPATPVGN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 YphqfSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:PRK13549 144 L----GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRD 218
|
....*.
gi 579304020 233 GQMVET 238
Cdd:PRK13549 219 GRHIGT 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-244 |
1.78e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.01 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFLGEDlakkPENELIKLRgKDISMIF 98
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-------GILVptSGEVRVLGYV----PFKRRKEFA-RRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 -Q------D--PMTSLNptmqigkqvmepLIKHKnY--SKAQAKKRA---LEILNLVGLPNAEKRfkayphQFSGGQRQR 164
Cdd:COG4586 102 gQrsqlwwDlpAIDSFR------------LLKAI-YriPDAEYKKRLdelVELLDLGELLDTPVR------QLSLGQRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-249 |
2.24e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.88 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSF-DITagevQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilFLGEDLAKK 81
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGT----KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVK-----VMGREVNAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 PENELiklRGKdISMIFQDP-----MTSLNPTMQIGKQVMEplikhknYSKAQAKKRALEILNLVGLpnAEKRFKAyPHQ 156
Cdd:PRK13647 73 NEKWV---RSK-VGLVFQDPddqvfSSTVWDDVAFGPVNMG-------LDKDEVERRVEEALKAVRM--WDFRDKP-PYH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
250
....*....|...
gi 579304020 237 ETGDvNEIFYDPK 249
Cdd:PRK13647 218 AEGD-KSLLTDED 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-275 |
4.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAkkpenELIKLRG--KDISMIFQDP 101
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL-----RPQKGKVLVSGIDTG-----DFSKLQGirKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 102 MTSLnptmqIGKQVMEPLIkhknYSKAQAKKRALEILNLVGLPNAEKRFKAY----PHQFSGGQRQRIVIATALACEPKV 177
Cdd:PRK13644 87 ETQF-----VGRTVEEDLA----FGPENLCLPPIEIRKRVDRALAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 178 LIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVaNIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLL 257
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTP 235
|
250
....*....|....*...
gi 579304020 258 SSMPDLSTTNDTPLLAIP 275
Cdd:PRK13644 236 PSLIELAENLKMHGVVIP 253
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
234-321 |
7.47e-23 |
|
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: 90.88 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 234 QMVETGDVNEIFYDPKHPYTWGLLSSMPDLSTTnDTPLLAIPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPPWFKVSP 313
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKR-DRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAE 79
|
....*...
gi 579304020 314 THFVKSWL 321
Cdd:TIGR01727 80 GHRVACHL 87
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-217 |
9.05e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 9.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditAGEvQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedLAKKPen 84
Cdd:PRK11248 1 MLQISHLYADY---GGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT----------LDGKP-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 elIKLRGKDISMIFQD----PMTSLNPTMQIGKQVmeplikhKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGG 160
Cdd:PRK11248 65 --VEGPGAERGVVFQNegllPWRNVQDNVAFGLQL-------AGVEKMQRLEIAHQMLKKVGLEGAEKRY---IWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDL 217
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-239 |
1.19e-22 |
|
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: 94.52 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedlakkpenelikLRGKDISMIfq 99
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT---------------------VRGRVSSLL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPMTSLNPTMQiGKQ--VMEPLIKhkNYSKAQAKKRALEILNLVGLPNA-EKRFKAYphqfSGGQRQRIVIATALACEPK 176
Cdd:cd03220 90 GLGGGFNPELT-GREniYLNGRLL--GLSRKEIDEKIDEIIEFSELGDFiDLPVKTY----SSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 177 VLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-230 |
5.27e-22 |
|
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: 96.97 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLAKKPEne 85
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-----GVPLADADA-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liKLRGKDISMIFQdpmtslNPTMQIGkQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNA-----EKRFKAYPHQFSGG 160
Cdd:TIGR02857 392 --DSWRDQIAWVPQ------HPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAAlpqglDTPIGEGGAGLSGG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAVM 230
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-250 |
5.51e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 92.91 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkGEILflgedlakkpENELIKLRGKDISMIFQDpmTS 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG----GVIL----------EGKQITEPGPDRMVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIgKQVMEPLIKHKNYSKAQAKKRAL--EILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:TIGR01184 65 LLPWLTV-RENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 183 PTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI-FYDPKH 250
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-245 |
6.63e-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: 93.23 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITK-LFQGDTGRIKkgeilFLGEDLAKkpE 83
Cdd:COG1119 3 LLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVR-----LFGERRGG--E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 84 NeLIKLRGK------DISMIFQDPMTSLN-------PTMQIgkqvmeplikHKNYSKAQaKKRALEILNLVGLPN-AEKR 149
Cdd:COG1119 72 D-VWELRKRiglvspALQLRFPRDETVLDvvlsgffDSIGL----------YREPTDEQ-RERARELLELLGLAHlADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 150 FkaypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLG-VVANIaDRVA 228
Cdd:COG1119 140 F----GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVL 214
|
250
....*....|....*..
gi 579304020 229 VMYGGQMVETGDVNEIF 245
Cdd:COG1119 215 LLKDGRVVAAGPKEEVL 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-239 |
8.16e-22 |
|
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: 91.22 E-value: 8.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAkkpenE 85
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-----QGEITLDGVPVS-----D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKDISMIFQDPMTsLNPTmqigkqvmeplikhknyskaqakkraleILNLVGLpnaekrfkayphQFSGGQRQRI 165
Cdd:cd03247 69 LEKALSSLISVLNQRPYL-FDTT----------------------------LRNNLGR------------RFSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMkeLQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVETG 239
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-244 |
2.24e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENEliklrgKDISMIFQDpmTSLNPT 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-----SGSLTLNGQDHTTTPPSR------RPVSMLFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 109 MQIGKQV---MEPLIKHKNYSKAQAKkralEILNLVGLPNAEKRFkayPHQFSGGQRQRIVIATALACEPKVLIADEPTT 185
Cdd:PRK10771 86 LTVAQNIglgLNPGLKLNAAQREKLH----AIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 186 ALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-239 |
3.98e-21 |
|
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: 90.16 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGEVqaVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilFLGEDLAKKPene 85
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE-----IDGIDISTIP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKdISMIFQDPmTSLNPTMqigKQVMEPlikHKNYSKAQAKKrALEI----LNLvglpnaekrfkayphqfSGGQ 161
Cdd:cd03369 77 LEDLRSS-LTIIPQDP-TLFSGTI---RSNLDP---FDEYSDEEIYG-ALRVseggLNL-----------------SQGQ 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIaDRVAVMYGGQMVETG 239
Cdd:cd03369 131 RQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-277 |
4.26e-21 |
|
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: 90.30 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 30 FYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedLAKKPENEliklRGKDISMIFQ------DPMT 103
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVK----------VAGASPGK----GWRHIGYVPQrhefawDFPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 SLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKrfkaypHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:TIGR03771 67 SVAHTVMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPV------GELSGGQRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 184 TTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVaVMYGGQMVETGDVNEIfydpKHPYTWgllssMPDL 263
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL----QDPAPW-----MTTF 209
|
250
....*....|....
gi 579304020 264 STTNDTPLLAIPGA 277
Cdd:TIGR03771 210 GVSDSSPLLRIVGA 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-235 |
4.34e-21 |
|
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: 88.81 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDlhVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLAKKPENE 85
Cdd:cd03246 1 LEVEN--VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-----GADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LiklrGKDISMIFQDpmtslnpTMQIGKQVMEplikhknyskaqakkraleilNLvglpnaekrfkayphqFSGGQRQRI 165
Cdd:cd03246 74 L----GDHVGYLPQD-------DELFSGSIAE---------------------NI----------------LSGGQRQRL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVAnIADRVAVMYGGQM 235
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-244 |
4.96e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.10 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitagEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAI--TKLFQGDTGRI--------KKGEI---L 72
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalceKCGYVerpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 73 FLGEDLAK-------------KPENELIKLRGKDISMIFQDPMtSLNPTMQIGKQVMEPLiKHKNYSKAQAKKRALEILN 139
Cdd:TIGR03269 77 KVGEPCPVcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEAL-EEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 140 LVGLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGV 219
Cdd:TIGR03269 155 MVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*
gi 579304020 220 VANIADRVAVMYGGQMVETGDVNEI 244
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-248 |
1.39e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDI-TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLakkPENELIKLR 90
Cdd:TIGR00958 483 DVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG-----QVLLDGVPL---VQYDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 91 GKdISMIFQDPmtslnptmqigkQVMEPLIKHkNYSKAQAKKRALEILNLVGLPNAEKRFKAYPH-----------QFSG 159
Cdd:TIGR00958 555 RQ-VALVGQEP------------VLFSGSVRE-NIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDvtmqAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVMYGGQMVETG 239
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
....*....
gi 579304020 240 DVNEIFYDP 248
Cdd:TIGR00958 696 THKQLMEDQ 704
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-239 |
1.47e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.80 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 13 VSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPENELiklRgK 92
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-----LLDGTDIRQLDPADL---R-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 93 DISMIFQDPMT---SLNPTMQIGKQVMEplikhknyskaqaKKRALEILNLVGLPNAEKRfkaYPHQF-----------S 158
Cdd:cd03245 79 NIGYVPQDVTLfygTLRDNITLGAPLAD-------------DERILRAAELAGVTDFVNK---HPNGLdlqigergrglS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqqKIDTAIIFITHDLGVVAnIADRVAVMYGGQMVET 238
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVAD 219
|
.
gi 579304020 239 G 239
Cdd:cd03245 220 G 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-240 |
1.53e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 92.58 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 18 TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTgriKKGEILFLGEDLAKKPENELiklRGKDISMI 97
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT---WDGEIYWSGSPLKASNIRDT---ERAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 98 FQDPMtsLNPTMQIGKQV-MEPLIKHKNYSKAQAK--KRALEILNLVGLPNAEKRFKAypHQFSGGQRQRIVIATALACE 174
Cdd:TIGR02633 84 HQELT--LVPELSVAENIfLGNEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPV--GDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 175 PKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-234 |
1.77e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPEne 85
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-----ELLAGTAPLAEARE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liklrgkDISMIFQDpmTSLNPTmqigKQVMEplikhkNYS---KAQAKKRALEILNLVGLpnaEKRFKAYPHQFSGGQR 162
Cdd:PRK11247 82 -------DTRLMFQD--ARLLPW----KKVID------NVGlglKGQWRDAALQALAAVGL---ADRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304020 163 QRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-245 |
2.70e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 23 QAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQGDTG--RIKKGEILFLGE--DLAKKpenELIKLRgKDISMIF 98
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKST-------LFMNLSGllRPQKGAVLWQGKplDYSKR---GLLALR-QQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDPMTSLNPTmQIGKQVMEPLiKHKNYSKAQAKKRALEILNLVGlpnaEKRFKAYPHQ-FSGGQRQRIVIATALACEPKV 177
Cdd:PRK13638 84 QDPEQQIFYT-DIDSDIAFSL-RNLGVPEAEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 178 LIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYGGQMVETGDVNEIF 245
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-243 |
3.37e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSfditagevQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAItklFqGDTgRIKKGEILFLGEDLAKKP 82
Cdd:COG1129 254 EVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL---F-GAD-PADSGEIRLDGKPVRIRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLRgkdISMIFQDPMTS-LNPTMQIGK----QVMEPLIKHKNYSKAQAKKRALEILNLVGL--PNAEKRFKayph 155
Cdd:COG1129 321 PRDAIRAG---IAYVPEDRKGEgLVLDLSIREnitlASLDRLSRGGLLDRRRERALAEEYIKRLRIktPSPEQPVG---- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
250
....*....|.
gi 579304020 236 V---ETGDVNE 243
Cdd:COG1129 473 VgelDREEATE 483
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-240 |
4.96e-20 |
|
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: 87.22 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPeneliklrgkdISMIFQDpmTSLNPT 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP-----------VSMLFQE--NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 109 MQIGKQV---MEPLIKhknySKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQRQRIVIATALACEPKVLIADEPTT 185
Cdd:TIGR01277 85 LTVRQNIglgLHPGLK----LNAEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 186 ALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGD 240
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-254 |
5.17e-20 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 88.16 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFDitagEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTG-RIKKGEILFLGEDLA 79
Cdd:CHL00131 3 KNKPILEIKNLHASVN----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA----GHPAyKILEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKPENELIKLrgkDISMIFQDP------------MTSLNPTM-QIGKQVMEPL-----IKhknyskaqakkralEILNLV 141
Cdd:CHL00131 75 DLEPEERAHL---GIFLAFQYPieipgvsnadflRLAYNSKRkFQGLPELDPLefleiIN--------------EKLKLV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 142 GLpnaEKRF--KAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGV 219
Cdd:CHL00131 138 GM---DPSFlsRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRL 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 579304020 220 VANIA-DRVAVMYGGQMVETGDVNEIFYDPKHPYTW 254
Cdd:CHL00131 214 LDYIKpDYVHVMQNGKIIKTGDAELAKELEKKGYDW 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-248 |
6.46e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 39 AIVGESGSGKSVTTKAITKLFQGDTGRIKKGE-ILFlgeDLAKK----PEneliKLRgkdISMIFQDpmTSLNPTMQIgk 113
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLF---DAEKGiclpPE----KRR---IGYVFQD--ARLFPHYKV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 114 qvmeplikHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQA 193
Cdd:PRK11144 94 --------RGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 194 QILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDP 248
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-249 |
6.48e-20 |
|
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: 87.21 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLrgkDISMIFQDPmtSLNPTMQIGKQVMEPLIKHKnYSKAQAKKRALEILNLVGLPNAEKRfKAYphQFSGGQRQRI 165
Cdd:cd03218 72 RARL---GIGYLPQEA--SIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKS-KAS--SLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKidtAI-IFIT-HDLGVVANIADRVAVMYGGQMVETGDVNE 243
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR---GIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
....*.
gi 579304020 244 IFYDPK 249
Cdd:cd03218 220 IAANEL 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
35-244 |
1.07e-19 |
|
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: 90.57 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 35 GETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPENELiklrGKDISMIFQDpmtslnpTMQIGKQ 114
Cdd:TIGR01846 483 GEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV-----LVDGVDLAIADPAWL----RRQMGVVLQE-------NVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 115 VMEplikhkNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQF-----------SGGQRQRIVIATALACEPKVLIADEP 183
Cdd:TIGR01846 547 IRD------NIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 184 TTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAVMYGGQMVETGDVNEI 244
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
12-239 |
1.11e-19 |
|
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: 90.40 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVttkaitkLFQgdtgrikkgeiLFLGEDlakKPENELIKLRG 91
Cdd:TIGR03797 456 RVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST-------LLR-----------LLLGFE---TPESGSVFYDG 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDPMTS-LNPTMQIGK----QVMEPLIKHKNYSKaqakKRALEILNLVGLpnaEKRFKAYP---H-------- 155
Cdd:TIGR03797 515 QDLAGLDVQAVRRqLGVVLQNGRlmsgSIFENIAGGAPLTL----DEAWEAARMAGL---AEDIRAMPmgmHtviseggg 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkidTAIIfITHDLGVVANiADRVAVMYGGQM 235
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV---TRIV-IAHRLSTIRN-ADRIYVLDAGRV 662
|
....
gi 579304020 236 VETG 239
Cdd:TIGR03797 663 VQQG 666
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-217 |
1.31e-19 |
|
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: 89.73 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDitaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENE 85
Cdd:TIGR02868 335 LELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLrgkdISMIFQDPM---TSLNPTMQIGKqvmeplikhKNYSKAQAkkraLEILNLVGLpnaEKRFKAYPH------- 155
Cdd:TIGR02868 407 VRRR----VSVCAQDAHlfdTTVRENLRLAR---------PDATDEEL----WAALERVGL---ADWLRALPDgldtvlg 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 156 ----QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQIL-DLMKELQQKidtAIIFITHDL 217
Cdd:TIGR02868 467 eggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSGR---TVVLITHHL 530
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-245 |
1.68e-19 |
|
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: 89.76 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVndLHVSFDITA------------GEVQ---------------AVRGVDFYLNKGETLAIVGESGSGKSVTTKA 54
Cdd:TIGR02204 308 AERLIEL--LQAEPDIKApahpktlpvplrGEIEfeqvnfayparpdqpALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 55 ITKLFQGDTGRIkkgeiLFLGEDLAKKPENELiklRGKdISMIFQDPM---TSLNPTMQIGKqvmePLIKHKNYSKAQAK 131
Cdd:TIGR02204 386 LLRFYDPQSGRI-----LLDGVDLRQLDPAEL---RAR-MALVPQDPVlfaASVMENIRYGR----PDATDEEVEAAARA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 132 KRALEILNlvGLPNAekrFKAYPHQ----FSGGQRQRIVIATALACEPKVLIADEPTTALDV---TMQAQILD-LMKElq 203
Cdd:TIGR02204 453 AHAHEFIS--ALPEG---YDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAeseQLVQQALEtLMKG-- 525
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 579304020 204 qkiDTAIIfITHDLGVVANiADRVAVMYGGQMVETGDVNEIF 245
Cdd:TIGR02204 526 ---RTTLI-IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELI 562
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
13-239 |
1.84e-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: 89.62 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 13 VSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENEL---IKL 89
Cdd:TIGR03796 483 ITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSG-----EILFDGIPREEIPREVLansVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 90 RGKDISMiFQ----DPMTSLNPTMQIGKQVmeplikhknyskaQAKKRAlEILNLVGlpnaeKRFKAYPHQ-------FS 158
Cdd:TIGR03796 558 VDQDIFL-FEgtvrDNLTLWDPTIPDADLV-------------RACKDA-AIHDVIT-----SRPGGYDAElaegganLS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 159 GGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDlmkELQQKIDTAIIfITHDLGVVANiADRVAVMYGGQMVET 238
Cdd:TIGR03796 618 GGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDD---NLRRRGCTCII-VAHRLSTIRD-CDEIIVLERGKVVQR 692
|
.
gi 579304020 239 G 239
Cdd:TIGR03796 693 G 693
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-244 |
2.66e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.92 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAkkpENELIKLRg 91
Cdd:PRK11176 346 NVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD-----IDEGEILLDGHDLR---DYTLASLR- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDpMTSLNPTmqIGKQVMEPliKHKNYSKAQAKKRAleilnlvGLPNAEKRFKAYPHQF-----------SGG 160
Cdd:PRK11176 417 NQVALVSQN-VHLFNDT--IANNIAYA--RTEQYSREQIEEAA-------RMAYAMDFINKMDNGLdtvigengvllSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 161 QRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAVMYGGQMVETGD 240
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
....
gi 579304020 241 VNEI 244
Cdd:PRK11176 562 HAEL 565
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-239 |
3.82e-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: 84.85 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPeneLIKLRGKdISMIFQ 99
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE-----LSSGSILIDGVDISKIG---LHDLRSR-ISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPMT-------SLNPtmqigkqvmeplikHKNYSKAQAkkraLEILNLVGLpnaEKRFKAYPHQ-----------FSGGQ 161
Cdd:cd03244 86 DPVLfsgtirsNLDP--------------FGEYSDEEL----WQALERVGL---KEFVESLPGGldtvveeggenLSVGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQIldlmkelQQKIDTA-----IIFITHDLGVVANiADRVAVMYGGQMV 236
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALI-------QKTIREAfkdctVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
...
gi 579304020 237 ETG 239
Cdd:cd03244 217 EFD 219
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-239 |
6.08e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 88.26 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDL---HVSFDITAGEvQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGED 77
Cdd:TIGR01193 464 RTELNNLNGDIvinDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQA-----RSGEILLNGFS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 78 LAKKPENELIKLrgkdISMIFQDPMTslnptmqIGKQVMEPLIKHKNYSKAQAK-KRALEILNLvglpnaEKRFKAYPHQ 156
Cdd:TIGR01193 538 LKDIDRHTLRQF----INYLPQEPYI-------FSGSILENLLLGAKENVSQDEiWAACEIAEI------KDDIENMPLG 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 F-----------SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKidtAIIFITHDLGvVANIAD 225
Cdd:TIGR01193 601 YqtelseegssiSGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSD 676
|
250
....*....|....
gi 579304020 226 RVAVMYGGQMVETG 239
Cdd:TIGR01193 677 KIIVLDHGKIIEQG 690
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-243 |
6.95e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVsFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKsvtTKAITKLFQGDTGRiKKGEILFLGEDLAKKP 82
Cdd:PRK13549 257 EVILEVRNLTA-WDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGR---TELVQCLFGAYPGR-WEGEIFIDGKPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLrgkDISMIFQD-PMTSLNPTMQIGKQVMepLIKHKNYSKAQAKKRALEilnLVGLPNAEKRFK---AYPHQ-- 156
Cdd:PRK13549 332 PQQAIAQ---GIAMVPEDrKRDGIVPVMGVGKNIT--LAALDRFTGGSRIDDAAE---LKTILESIQRLKvktASPELai 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 --FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKEL-QQKIdtAIIFITHDLGVVANIADRVAVMYGG 233
Cdd:PRK13549 404 arLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGV--AIIVISSELPEVLGLSDRVLVMHEG 481
|
250
....*....|.
gi 579304020 234 QMveTGD-VNE 243
Cdd:PRK13549 482 KL--KGDlINH 490
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-230 |
1.30e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilfLGEDLAKKPENeliklrgkdISMIFQ 99
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA----GGARVAYVPQR---------SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPMTSLNpTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnAEKRFKAyphqFSGGQRQRIVIATALACEPKVLI 179
Cdd:NF040873 70 LPLTVRD-LVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADL--AGRQLGE----LSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 579304020 180 ADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANiADRVAVM 230
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-253 |
1.39e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLaKK 81
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNL-YA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 PENELIKLRgKDISMIFQDPM---TSLNPTMQIGKQV------MEPLIKhKNYSKAQAKKRALEILNLVGLpnaekrfka 152
Cdd:PRK14243 82 PDVDPVEVR-RRIGMVFQKPNpfpKSIYDNIAYGARIngykgdMDELVE-RSLRQAALWDEVKDKLKQSGL--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 yphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:PRK14243 151 ---SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTAFFNV 225
|
250 260 270
....*....|....*....|....*....|
gi 579304020 233 ---------GQMVETGDVNEIFYDPKHPYT 253
Cdd:PRK14243 226 eltegggryGYLVEFDRTEKIFNSPQQQAT 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-244 |
1.59e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAK 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-----TKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLrgkDISMIFQ-----DPMTSLNpTMQIG----KQVME-PLIKHKnyskaQAKKRALEILNLVGLPNAEKRF 150
Cdd:PRK09700 72 LDHKLAAQL---GIGIIYQelsviDELTVLE-NLYIGrhltKKVCGvNIIDWR-----EMRVRAAMMLLRVGLKVDLDEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 151 KAyphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqQKIDTAIIFITHDLGVVANIADRVAVM 230
Cdd:PRK09700 143 VA---NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVM 218
|
250
....*....|....
gi 579304020 231 YGGQMVETGDVNEI 244
Cdd:PRK09700 219 KDGSSVCSGMVSDV 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-247 |
2.30e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.52 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFDitagEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgRIKKGEILFLGEDL--AK 80
Cdd:PRK09984 2 QTIIRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD--KSAGSHIELLGRTVqrEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKdISMIFQ-----DPMTSLNPTMqIGKQVMEPLIKH--KNYSKAQaKKRALEILNLVGLPNaekrfkaY 153
Cdd:PRK09984 76 RLARDIRKSRAN-TGYIFQqfnlvNRLSVLENVL-IGALGSTPFWRTcfSWFTREQ-KQRALQALTRVGMVH-------F 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQ----FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAV 229
Cdd:PRK09984 146 AHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVA 225
|
250
....*....|....*...
gi 579304020 230 MYGGQmvetgdvneIFYD 247
Cdd:PRK09984 226 LRQGH---------VFYD 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-243 |
3.74e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.23 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTgriKKGEILFLGEdlakkpen 84
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGS---YEGEILFDGE-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 eliKLRGKDIS--------MIFQDpmTSLNPTMQIGKQVM---EPLiKHKNYSKAQAKKRALEILNLVGLP-NAEKRFKa 152
Cdd:NF040905 66 ---VCRFKDIRdsealgivIIHQE--LALIPYLSIAENIFlgnERA-KRGVIDWNETNRRARELLAKVGLDeSPDTLVT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 yphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADRVAVMYG 232
Cdd:NF040905 139 ---DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRD 214
|
250
....*....|....*.
gi 579304020 233 GQMVET-----GDVNE 243
Cdd:NF040905 215 GRTIETldcraDEVTE 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-237 |
5.62e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDlhvsfdITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAItklFQGDtgRIKKGEILFLGEDLakK 81
Cdd:PRK09700 262 HETVFEVRN------VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL---FGVD--KRAGGEIRLNGKDI--S 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 PENELIKLRgKDISMIFQD-------PMTSLNPTMQIGKQVMEP-------LIKHKNYSKAQAKKRALEILNLVGLpnaE 147
Cdd:PRK09700 329 PRSPLDAVK-KGMAYITESrrdngffPNFSIAQNMAISRSLKDGgykgamgLFHEVDEQRTAENQRELLALKCHSV---N 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 148 KRFKayphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRV 227
Cdd:PRK09700 405 QNIT----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRI 479
|
250
....*....|
gi 579304020 228 AVMYGGQMVE 237
Cdd:PRK09700 480 AVFCEGRLTQ 489
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-244 |
6.28e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.51 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDlhVSFdiTAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKK 81
Cdd:PRK11831 4 VANLVDMRG--VSF--TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-----HGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 PENELIKLRgKDISMIFQDpmTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFkayPHQFSGGQ 161
Cdd:PRK11831 75 SRSRLYTVR-KRMSMLFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDV 241
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
...
gi 579304020 242 NEI 244
Cdd:PRK11831 229 QAL 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-240 |
7.40e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDlhVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENE 85
Cdd:PRK11160 339 LTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG-----EILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLrgkdISMIFQDP---MTSLNPTMQIGKqvmeplikhknyskAQAKKRAL-EILNLVGLPN---AEKRFKAY----P 154
Cdd:PRK11160 412 LRQA----ISVVSQRVhlfSATLRDNLLLAA--------------PNASDEALiEVLQQVGLEKlleDDKGLNAWlgegG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIaDRVAVMYGGQ 234
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
....*.
gi 579304020 235 MVETGD 240
Cdd:PRK11160 551 IIEQGT 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-251 |
1.82e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklFQGDTGRIKKGEILFLGEdlakK 81
Cdd:TIGR00955 18 GSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA--FRSPKGVKGSGSVLLNGM----P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 82 PENELIKLRGkdiSMIFQDPMtsLNPTMQIGKQ--VMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQ--- 156
Cdd:TIGR00955 92 IDAKEMRAIS---AYVQQDDL--FIPTLTVREHlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
250
....*....|....*...
gi 579304020 237 ETGDVNE---IFYDPKHP 251
Cdd:TIGR00955 247 YLGSPDQavpFFSDLGHP 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-235 |
2.33e-17 |
|
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: 82.95 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLhVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKsvtTKAITKLFQGDTGRIKkGEILFLGEDLAKKP 82
Cdd:TIGR02633 255 DVILEARNL-TCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGR---TELVQALFGAYPGKFE-GNVFINGKPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKlrgKDISMIFQD-PMTSLNPTMQIGKQVMepLIKHKNYSKAQAKKRALEilnLVGLPNAEKRFK---AYPH--- 155
Cdd:TIGR02633 330 PAQAIR---AGIAMVPEDrKRHGIVPILGVGKNIT--LSVLKSFCFKMRIDAAAE---LQIIGSAIQRLKvktASPFlpi 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 -QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:TIGR02633 402 gRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
.
gi 579304020 235 M 235
Cdd:TIGR02633 481 L 481
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-245 |
2.41e-17 |
|
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: 83.38 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 13 VSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDtgrikKGEILFLGEDLAKKPENELiklRgK 92
Cdd:TIGR03375 469 VSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT-----EGSVLLDGVDIRQIDPADL---R-R 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 93 DISMIFQDPMT---SL--NPTM---QIGKQVMeplikhknyskaqakkraLEILNLVGLPN-AEKRFKAYPHQ------- 156
Cdd:TIGR03375 540 NIGYVPQDPRLfygTLrdNIALgapYADDEEI------------------LRAAELAGVTEfVRRHPDGLDMQigergrs 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVaNIADRVAVMYGGQMV 236
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
....*....
gi 579304020 237 ETGDVNEIF 245
Cdd:TIGR03375 679 ADGPKDQVL 687
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-239 |
3.24e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 79.62 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtGRIKKGEILFLGEDLAKKpenelikLRGKDISMIFQD 100
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG--GGTTSGQILFNGQPRKPD-------QFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 101 PMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKR-ALEILNLVGL-PNAEKRFKayphQFSGGQRQRIVIATALACEPKVL 178
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLPRKSSDAIRKKRvEDVLLRDLALtRIGGNLVK----GISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-244 |
4.43e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 7 EVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENEL 86
Cdd:COG4604 3 EIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSG-----EVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 87 iklrGKDISMIFQDPMTSLNPTmqigkqVME-------PlikhknYSKAQAKK-------RALEILNLVGLpnaEKRfka 152
Cdd:COG4604 74 ----AKRLAILRQENHINSRLT------VRElvafgrfP------YSKGRLTAedreiidEAIAYLDLEDL---ADR--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 YPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:COG4604 132 YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKD 211
|
250
....*....|..
gi 579304020 233 GQMVETGDVNEI 244
Cdd:COG4604 212 GRVVAQGTPEEI 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-244 |
5.68e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLHVSFditAGeVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLA-K 80
Cdd:PRK10762 1 MQALLQLKGIDKAF---PG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAG-----SILYLGKEVTfN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPeneliklrgKD-----ISMIFQDpmtsLN--PTMQI------GKQVMEPL--IKHKN-YSKAQAkkraleILNLVGLP 144
Cdd:PRK10762 72 GP---------KSsqeagIGIIHQE----LNliPQLTIaeniflGREFVNRFgrIDWKKmYAEADK------LLARLNLR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 145 NAEKRFKAyphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIA 224
Cdd:PRK10762 133 FSSDKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEIC 208
|
250 260
....*....|....*....|
gi 579304020 225 DRVAVMYGGQMVETGDVNEI 244
Cdd:PRK10762 209 DDVTVFRDGQFIAEREVADL 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-238 |
7.90e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTER--ILEVNDLHVSfditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDL 78
Cdd:PRK10247 1 MQENspLLQLQNVGYL----AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG-----TLLFEGEDI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 79 AK-KPEneliKLRgKDISMIFQDPMTslnptmqIGKQVMEPLI-KHKNYSKAQAKKRALEILNLVGLPNA--EKRFKAyp 154
Cdd:PRK10247 72 STlKPE----IYR-QQVSYCAQTPTL-------FGDTVYDNLIfPWQIRNQQPDPAIFLDDLERFALPDTilTKNIAE-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 hqFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAVM--YG 232
Cdd:PRK10247 138 --LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHA 214
|
....*.
gi 579304020 233 GQMVET 238
Cdd:PRK10247 215 GEMQEA 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-235 |
9.18e-17 |
|
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: 78.28 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLakkPENELIKLRGKdISMIFQD 100
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ-----PQGGQVLLDGKPI---SQYEHKYLHSK-VSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 101 PMT---SLNPTMQIGKQVMEPLIKHKNYSKAQA----KKRALEILNLVGLPNAekrfkayphQFSGGQRQRIVIATALAC 173
Cdd:cd03248 97 PVLfarSLQDNIAYGLQSCSFECVKEAAQKAHAhsfiSELASGYDTEVGEKGS---------QLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304020 174 EPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANiADRVAVMYGGQM 235
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
158-235 |
1.02e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.25 E-value: 1.02e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-215 |
1.16e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.01 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRI---KKGEILFLgedlakkPeneliklrgkdismifQDP 101
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIarpAGARVLFL-------P----------------QRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 102 MtslnptMQIGK---QVMEPLIkHKNYSKAQAKkralEILNLVGLPNAEKRF---KAYPHQFSGGQRQRIVIATALACEP 175
Cdd:COG4178 436 Y------LPLGTlreALLYPAT-AEAFSDAELR----EALEAVGLGHLAERLdeeADWDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579304020 176 KVLIADEPTTALDVTMQAQILDLMKElqQKIDTAIIFITH 215
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-239 |
1.85e-16 |
|
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: 80.63 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 12 HVSFDITAgEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeiLFLGEDLAKKPENELiklRg 91
Cdd:COG5265 362 NVSFGYDP-ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI-----LIDGQDIRDVTQASL---R- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDpmTSL-NPTMQ--IGkqvmeplikhknYSKAQAKK-------RALEILNLV-GLPNA------EKRFKayp 154
Cdd:COG5265 432 AAIGIVPQD--TVLfNDTIAynIA------------YGRPDASEeeveaaaRAAQIHDFIeSLPDGydtrvgERGLK--- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 hqFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIfITHDLGVVANiADRVAVMYGGQ 234
Cdd:COG5265 495 --LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLV-IAHRLSTIVD-ADEILVLEAGR 569
|
....*
gi 579304020 235 MVETG 239
Cdd:COG5265 570 IVERG 574
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
35-244 |
3.11e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 35 GETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAKKPENELiklrGKDISMIFQDPMTSLNPTMQ---- 110
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTP-----AHGHVWLDGEHIQHYASKEV----ARRIGLLAQNATTPGDITVQelva 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 111 IGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKrfkaypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVT 190
Cdd:PRK10253 104 RGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSV------DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579304020 191 MQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-300 |
3.70e-16 |
|
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: 72.05 E-value: 3.70e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 236 VETGDVNEIFYDPKHPYTWGLLSSMPDLsTTNDTPLLAIPGAPPDLLHPPKGDAFARRSQYALDI 300
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRL-DPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEE 64
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-245 |
7.22e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFdiTAGEVqAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEdlak 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTW--RNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-----RLASGKISILGQ---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 kPENEliKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNY-SKAQAKKRALEILNLVGLPNAEKRFKAYpHQFSG 159
Cdd:PRK15056 70 -PTRQ--ALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWlRRAKKRDRQIVTAALARVDMVEFRHRQI-GELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANIADrVAVMYGGQMVETG 239
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCD-YTVMVKGTVLASG 223
|
....*.
gi 579304020 240 DVNEIF 245
Cdd:PRK15056 224 PTETTF 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-237 |
7.34e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 2 TERILEVNDLhvsFDITAGEVQ--AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIKKgeilflgedla 79
Cdd:COG2401 24 SERVAIVLEA---FGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALKG----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 kKPENELIKLrgkdismifqdpmtslnPTMQIGKQVmePLIKHknYSKAQAKKRALEILNLVGLPNAEKrFKAYPHQFSG 159
Cdd:COG2401 83 -TPVAGCVDV-----------------PDNQFGREA--SLIDA--IGRKGDFKDAVELLNAVGLSDAVL-WLRRFKELST 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMqAQILDL-MKELQQKIDTAIIFITHDLGVVANIADRVAVM--YGGQMV 236
Cdd:COG2401 140 GQKFRFRLALLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPE 218
|
.
gi 579304020 237 E 237
Cdd:COG2401 219 E 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-236 |
1.74e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.12 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDI--TAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGR----IKKGEILFLGEDLA 79
Cdd:cd03213 4 LSFRNLTVTVKSspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRrtglGVSGEVLINGRPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 80 KKpeneliKLRGKdISMIFQDPMtsLNPTMQIGKQVMeplikhknYSkaqAKKRALeilnlvglpnaekrfkayphqfSG 159
Cdd:cd03213 77 KR------SFRKI-IGYVPQDDI--LHPTLTVRETLM--------FA---AKLRGL----------------------SG 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDL-GVVANIADRVAVMYGGQMV 236
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRT-IICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-245 |
3.51e-15 |
|
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: 76.71 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 13 VSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtG--RIKKGEILFLGEDLAKKPENELiklr 90
Cdd:COG4618 336 LTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV-------GvwPPTAGSVRLDGADLSQWDREEL---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 91 GKDISMIFQDP-------------MTSLNPTMQIgkqvmeplikhknyskaQAKKRA----LeILnlvGLPNA-EKRFKA 152
Cdd:COG4618 405 GRHIGYLPQDVelfdgtiaeniarFGDADPEKVV-----------------AAAKLAgvheM-IL---RLPDGyDTRIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 153 YPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVAnIADRVAVMYG 232
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRD 541
|
250
....*....|...
gi 579304020 233 GQMVETGDVNEIF 245
Cdd:COG4618 542 GRVQAFGPRDEVL 554
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-244 |
3.54e-15 |
|
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: 76.62 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilFLGEDLAKKPENELiklrGKDISMIFQDpmts 104
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR-----LDGADLKQWDRETF----GKHIGYLPQD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 lnptmqigKQVMEPLIKhKNYSK----AQAKK-----RALEILNLV-GLPNA-EKRFKAYPHQFSGGQRQRIVIATALAC 173
Cdd:TIGR01842 401 --------VELFPGTVA-ENIARfgenADPEKiieaaKLAGVHELIlRLPDGyDTVIGPGGATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 174 EPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAiIFITHDLGVVaNIADRVAVMYGGQMVETGDVNEI 244
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERDEV 540
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-245 |
4.64e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.72 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVsfditAGEVQAVRGVdfyLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgrikKGEILFLGEDLAKKPENE 85
Cdd:COG4138 1 LQLNDVAV-----AGRLGPISAQ---VNAGELIHLIGPNGAGKSTLLARMAGLLPG------QGEILLNGRPLSDWSAAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGkdisMIFQDpmTSLNPTMQIGkQVMEpLIKHKNYSKAQAKKRALEILNLVGLpnAEKrfkaYP---HQFSGGQR 162
Cdd:COG4138 67 LARHRA----YLSQQ--QSPPFAMPVF-QYLA-LHQPAGASSEAVEQLLAQLAEALGL--EDK----LSrplTQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 163 QRIVIATAL-----ACEP--KVLIADEPTTALDVTMQAQILDLMKEL-QQKIdtAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:COG4138 133 QRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDVAQQAALDRLLRELcQQGI--TVVMSSHDLNHTLRHADRVWLLKQGK 210
|
250
....*....|.
gi 579304020 235 MVETGDVNEIF 245
Cdd:COG4138 211 LVASGETAEVM 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-249 |
7.64e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFLGEDLAKKP 82
Cdd:COG1137 3 TLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIV-------GLVKpdSGRIFLDGEDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 enelIKLRGK--------DISmIFQDpMTslnptmqigkqVMEPL---IKHKNYSKAQAKKRA---LEILNLVGLpnaeK 148
Cdd:COG1137 72 ----MHKRARlgigylpqEAS-IFRK-LT-----------VEDNIlavLELRKLSKKEREERLeelLEEFGITHL----R 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 149 RFKAYphQFSGGQRQRIVIATALACEPKVLIADEPTTALD---VtmqAQILDLMKELQQKidtAI-IFIT-HD----LGV 219
Cdd:COG1137 131 KSKAY--SLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaV---ADIQKIIRHLKER---GIgVLITdHNvretLGI 202
|
250 260 270
....*....|....*....|....*....|
gi 579304020 220 VaniaDRVAVMYGGQMVETGDVNEIFYDPK 249
Cdd:COG1137 203 C----DRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-220 |
8.36e-15 |
|
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: 72.01 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSfditAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeilflgeDLAKKPENE 85
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV----------RWNGTPLAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKDISMIFQDPmtSLNPTMQigkqVMEPL-IKHKNYSKAQakKRALEILNLVGLPNAEKRfkayP-HQFSGGQRQ 163
Cdd:TIGR01189 67 QRDEPHENILYLGHLP--GLKPELS----ALENLhFWAAIHGGAQ--RTIEDALAAVGLTGFEDL----PaAQLSAGQQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVV 220
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-244 |
1.79e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLAKKPEN 84
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-----GNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 ELIKLrgkDISMIFQDPMtsLNPTMQIGKQVMEPLIKH-KNYSKAQAKKRALEI-LNLvglpnaekrfkaypHQFSG--- 159
Cdd:PRK15439 82 KAHQL---GIYLVPQEPL--LFPNLSVKENILFGLPKRqASMQKMKQLLAALGCqLDL--------------DSSAGsle 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 -GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVET 238
Cdd:PRK15439 143 vADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
|
....*.
gi 579304020 239 GDVNEI 244
Cdd:PRK15439 222 GKTADL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
128-244 |
1.95e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 128 AQAKKRALEILNLVGL-PNAEKRFKAyphqFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKI 206
Cdd:PRK10575 122 AADREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQER 197
|
90 100 110
....*....|....*....|....*....|....*...
gi 579304020 207 DTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK10575 198 GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-233 |
2.17e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 8 VNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeilflgedlakkpenelI 87
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------------------S 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 88 KLRGKDISMIFQDP------------MTSLNPTMQIGKQVMEPLIKH-------KNYSKAQAKK----------RALEIL 138
Cdd:COG0488 57 IPKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLaepdedlERLAELQEEFealggweaeaRAEEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 139 NLVGLPNAEkrFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMqaqILDLMKELQQKiDTAIIFITHD-- 216
Cdd:COG0488 137 SGLGFPEED--LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNY-PGTVLVVSHDry 210
|
250 260
....*....|....*....|..
gi 579304020 217 -LGVVAN----IADRVAVMYGG 233
Cdd:COG0488 211 fLDRVATrileLDRGKLTLYPG 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-230 |
2.17e-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: 69.40 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflgedlakkpene 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 liklrgkdismifqdpmtslnPTMQIGkqvmeplikhknyskaqakkraleilnlvglpnaekrfkaYPHQFSGGQRQRI 165
Cdd:cd03221 61 ---------------------STVKIG----------------------------------------YFEQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkidtAIIFITHDLGVVANIADRVAVM 230
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIEL 140
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-227 |
3.20e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKkpen 84
Cdd:PRK09544 4 LVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 85 eliklrgkdismifqdpmTSLNPTMqigkqvmePLIKHKNYSKAQAKKRAlEILNLVGLPNAEKRFKAYPHQFSGGQRQR 164
Cdd:PRK09544 76 ------------------LYLDTTL--------PLTVNRFLRLRPGTKKE-DILPALKRVQAGHLIDAPMQKLSGGETQR 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 165 IVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRV 227
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-244 |
4.42e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedLAK 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIS----------LCG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKDISMIFQdpMTSLNPTMQigkqVMEPLIKHKNY---SKAQAKKRALEILNLVGLpnaEKRFKAYPHQF 157
Cdd:PRK13537 69 EPVPSRARHARQRVGVVPQ--FDNLDPDFT----VRENLLVFGRYfglSAAAARALVPPLLEFAKL---ENKADAKVGEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVE 237
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIA 218
|
....*..
gi 579304020 238 TGDVNEI 244
Cdd:PRK13537 219 EGAPHAL 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-240 |
7.00e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITklfqGDTgRIKKGEILFLGEDLAKKPENELIKlrgKDISMIFQ 99
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLC----GDP-RATSGRIVFDGKDITDWQTAKIMR---EAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 dpmtslnptmqiGKQVMEPLIKHKNYS-------KAQAKKRALEILNLvgLPNAEKRFKAYPHQFSGGQRQRIVIATALA 172
Cdd:PRK11614 88 ------------GRRVFSRMTVEENLAmggffaeRDQFQERIKWVYEL--FPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 173 CEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMV--ETGD 240
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGHVVleDTGD 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-243 |
7.06e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSvtT--KAITKLFQGDTGRIKKGEILFLG------E 76
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS--TllKLLAGELEPDSGTVKLGETVKIGyfdqhqE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 77 DLakKPENELIklrgkdismifqDPMTSLNPTMQIGK--QVMEPLikhkNYSKAQAKKRAleilnlvglpnaekrfkayp 154
Cdd:COG0488 389 EL--DPDKTVL------------DELRDGAPGGTEQEvrGYLGRF----LFSGDDAFKPV-------------------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMqaqiLDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG 506
|
250
....*....|
gi 579304020 235 MVE-TGDVNE 243
Cdd:COG0488 507 VREyPGGYDD 516
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-239 |
8.15e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.40 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEdlakkPENELIKLRGKDISMIFQdpMTS 104
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-----KITVLGV-----PVPARARLARARIGVVPQ--FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQigkqVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPT 184
Cdd:PRK13536 125 LDLEFT----VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 185 TALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-247 |
1.88e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 23 QAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEilflgEDLAKKPENELIKlRGkdISMIFQDPm 102
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-----EDISLLPLHARAR-RG--IGYLPQEA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 103 tSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKaypHQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:PRK10895 88 -SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 183 PTTALDvtmQAQILDLMKELQQKIDTAI-IFIT-HDLGVVANIADRVAVMYGGQMVETGDVNEIFYD 247
Cdd:PRK10895 164 PFAGVD---PISVIDIKRIIEHLRDSGLgVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-239 |
3.77e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 30 FYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgrikKGEILFLGEDLAKKPENELIKLRGkdiSMIFQDPMTSLNPTM 109
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPG------SGSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 110 QigkqvMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkaYPHQFSGGQRQRIVIATA-LACEP------KVLIADE 182
Cdd:PRK03695 88 Q-----YLTLHQPDKTRTEAVASALNEVAEALGLDDKLGR---SVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 183 PTTALDVTMQAqILD-LMKEL-QQKIdtAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:PRK03695 160 PMNSLDVAQQA-ALDrLLSELcQQGI--AVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-238 |
4.64e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 22 VQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedlakkpenelikLRGKdiSMIFQDP 101
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---------------------IDGQ--EMRFAST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 102 MTSLNPTMQIGKQ---------VMEPLI------KHKNYSKAQAKKRALEILNLVGL---PNAEKRFkayphqFSGGQRQ 163
Cdd:PRK11288 74 TAALAAGVAIIYQelhlvpemtVAENLYlgqlphKGGIVNRRLLNYEAREQLEHLGVdidPDTPLKY------LSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 164 RIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVET 238
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-227 |
5.13e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK------------------KGEIL-FLGEDLAKkpENELIKl 89
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarlqqdpprnvEGTVYdFVAEGIEE--QAEYLK- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 90 RGKDIS-MIFQDPMTSLNPTMQigkQVMEPLiKHKNysKAQAKKRALEILNLVGLpNAEKRFKAyphqFSGGQRQRIVIA 168
Cdd:PRK11147 100 RYHDIShLVETDPSEKNLNELA---KLQEQL-DHHN--LWQLENRINEVLAQLGL-DPDAALSS----LSGGWLRKAALG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 169 TALACEPKVLIADEPTTALDVTMQAQILDLMKELQqkidTAIIFITHDLGVVANIADRV 227
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ----GSIIFISHDRSFIRNMATRI 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-235 |
8.90e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEvnDLHVSFDITAGEVQ---------AVRGVDFYLNKGETLAIVGESGSGKSvttkAITKLFQGDTGRiKKGEI 71
Cdd:PRK10762 237 MVGRKLE--DQYPRLDKAPGEVRlkvdnlsgpGVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALPR-TSGYV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 72 LFLGEDL-AKKPENELI----------KLRGKDISMIFQDPM--TSLNPTMQIGKQvmeplIKHKnySKAQAKKRALEIL 138
Cdd:PRK10762 310 TLDGHEVvTRSPQDGLAngivyisedrKRDGLVLGMSVKENMslTALRYFSRAGGS-----LKHA--DEQQAVSDFIRLF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 139 NlVGLPNAEKRFKayphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLG 218
Cdd:PRK10762 383 N-IKTPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMP 456
|
250
....*....|....*..
gi 579304020 219 VVANIADRVAVMYGGQM 235
Cdd:PRK10762 457 EVLGMSDRILVMHEGRI 473
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-229 |
1.14e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFdITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLF--------------QGDTGRIKK--- 68
Cdd:PTZ00265 1166 IEIMDVNFRY-ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehTNDMTNEQDyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 69 --------------------------------GEILFLGEDLAKKPENELIKLrgkdISMIFQDPM---TSLNPTMQIGK 113
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNL----FSIVSQEPMlfnMSIYENIKFGK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 114 Q--VMEPLikhKNYSKAQAKKRALEilnlvGLPNA-EKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVT 190
Cdd:PTZ00265 1321 EdaTREDV---KRACKFAAIDEFIE-----SLPNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270
....*....|....*....|....*....|....*....
gi 579304020 191 MQAQILDLMKELQQKIDTAIIFITHDLGVVANiADRVAV 229
Cdd:PTZ00265 1393 SEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-240 |
2.00e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFDitagEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAitkLFQGDTGRIKKGEILFLGEDLAK-KPE 83
Cdd:PRK09580 1 MLSIKDLHVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFKGKDLLElSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 84 NEliklRGKDISMIFQDPM------------TSLNPTMQIGKQvmEPLIKHKNYSKAQAKkraleiLNLVGLPnAEKRFK 151
Cdd:PRK09580 74 DR----AGEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLDRFDFQDLMEEK------IALLKMP-EDLLTR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 152 AYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVtmqaqilDLMKELQQKIDT------AIIFITHDLGVVANIA- 224
Cdd:PRK09580 141 SVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDI-------DALKIVADGVNSlrdgkrSFIIVTHYQRILDYIKp 213
|
250
....*....|....*.
gi 579304020 225 DRVAVMYGGQMVETGD 240
Cdd:PRK09580 214 DYVHVLYQGRIVKSGD 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-245 |
4.39e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKkpeNELIKLRgKDISMIFQDPMTs 104
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVE-----LEKGRIMIDDCDVAK---FGLTDLR-RVLSIIPQSPVL- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGkqvMEPLIKHKNYSKAQAKKRAlEILNLV-----GLpnaEKRFKAYPHQFSGGQRQRIVIATALACEPKVLI 179
Cdd:PLN03232 1322 FSGTVRFN---IDPFSEHNDADLWEALERA-HIKDVIdrnpfGL---DAEVSEGGENFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 180 ADEPTTALDVTMQAQILDLMKElQQKIDTAIIfITHDLGVVANiADRVAVMYGGQMVETGDVNEIF 245
Cdd:PLN03232 1395 LDEATASVDVRTDSLIQRTIRE-EFKSCTMLV-IAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-244 |
7.13e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLhvsfdiTAGEVQAVRGVDFYLNKGETLAIVGESGSGKsvtTKAITKLFqGDTGRiKKGEILFLGEDLAKKP 82
Cdd:PRK10982 248 EVILEVRNL------TSLRQPSIRDVSFDLHKGEILGIAGLVGAKR---TDIVETLF-GIREK-SAGTITLHGKKINNHN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIK---------LRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALeilnlvglpnaekRFKAY 153
Cdd:PRK10982 317 ANEAINhgfalvteeRRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSM-------------RVKTP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 154 PHQ-----FSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVA 228
Cdd:PRK10982 384 GHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRIL 462
|
250 260
....*....|....*....|.
gi 579304020 229 VMYGGQ---MVETGDV--NEI 244
Cdd:PRK10982 463 VMSNGLvagIVDTKTTtqNEI 483
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-244 |
1.25e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFYLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK-KGEILFLGEDLAkkpENELIKLRgKDISMIFQDPmtsln 106
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALL-------GFLPyQGSLKINGIELR---ELDPESWR-KHLSWVGQNP----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 107 ptmqigkQVMEPLIK------HKNYSKAQAKKrALEilnlvglpnaekrfKAYPHQF-------------------SGGQ 161
Cdd:PRK11174 433 -------QLPHGTLRdnvllgNPDASDEQLQQ-ALE--------------NAWVSEFlpllpqgldtpigdqaaglSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 162 RQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIaDRVAVMYGGQMVETGDV 241
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDY 567
|
...
gi 579304020 242 NEI 244
Cdd:PRK11174 568 AEL 570
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-234 |
1.65e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 27 GVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTgrikkgeilFLGEDLA--KKPENELIKLRGkdisMIFQDPMts 104
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---------FTGTILAnnRKPTKQILKRTG----FVTQDDI-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGKQ-VMEPLIKHKNYSKAQAKKRALE-ILNLVGLPNAEKRF--KAYPHQFSGGQRQRIVIATALACEPKVLIA 180
Cdd:PLN03211 151 LYPHLTVRETlVFCSLLRLPKSLTKQEKILVAEsVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579304020 181 DEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQ 234
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-215 |
1.80e-11 |
|
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: 61.79 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeilflgedlakkpenelIKLRGKDISMIFQDP-MT 103
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------------GMPEGEDLLFLPQRPyLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 SLNPTMQIgkqvmeplikhknyskaqakkraleilnlvglpnaekrfkAYP--HQFSGGQRQRIVIATALACEPKVLIAD 181
Cdd:cd03223 77 LGTLREQL----------------------------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....
gi 579304020 182 EPTTALDVTMQAQILDLMKELQqkidTAIIFITH 215
Cdd:cd03223 117 EATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-227 |
3.47e-11 |
|
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: 61.74 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 27 GVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedLAKKPENELIKLRGKDISMI-FQDPMtsl 105
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL----------LNGGPLDFQRDSIARGLLYLgHAPGI--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 106 nptmqigKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRfkayP-HQFSGGQRQRIVIATALACEPKVLIADEPT 184
Cdd:cd03231 85 -------KTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDR----PvAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 579304020 185 TALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRV 227
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-236 |
3.99e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.51 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdTGRIKkGEILFLGEDL---AKKPENELIKLRGKDISMifqdp 101
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEG-NVSVE-GDIHYNGIPYkefAEKYPGEIIYVSEEDVHF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 102 mtslnPTMQIgKQVMEPLIKHKNyskaqakkraleilnlvglpnaekrfKAYPHQFSGGQRQRIVIATALACEPKVLIAD 181
Cdd:cd03233 96 -----PTLTV-RETLDFALRCKG--------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 182 EPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVA-NIADRVAVMYGGQMV 236
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
158-236 |
4.73e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKEL-QQKIdtAIIFITHDLGVVANIADRVAVMYGGQMV 236
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGV--AVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-219 |
4.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVsfdiTAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKKPENE 85
Cdd:PRK13539 3 LEGEDLAC----VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL-----PPAAGTIKLDGGDIDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKdismifQDPMtslNPTMQigkqVMEPLIKHKNYsKAQAKKRALEILNLVGLPNAEKRFKAYphqFSGGQRQRI 165
Cdd:PRK13539 74 ACHYLGH------RNAM---KPALT----VAENLEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQILDLMKE-LQQkiDTAIIFITH-DLGV 219
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQ--GGIVIAATHiPLGL 190
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-247 |
5.06e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 22 VQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPENELIKlrgKDISMIFQDp 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSG-----SILFQGKEIDFKSSKEALE---NGISMVHQE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 102 mtsLNPTMQigKQVME-----------PLIKH-KNYSKAQAKKRALEIlnlvglpNAEKRFKAypHQFSGGQRQRIVIAT 169
Cdd:PRK10982 82 ---LNLVLQ--RSVMDnmwlgryptkgMFVDQdKMYRDTKAIFDELDI-------DIDPRAKV--ATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 170 ALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYD 247
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-250 |
1.24e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDT---GRIKKGEILFLGEDLAKKPENELIKLRGkdismifqdp 101
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprGARVTGDVTLNGEPLAAIDAPRLARLRA---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 102 mtslnptmqigkqVMeplikhknyskAQAKKRAL-----EILNLVGLPNAeKRFKAYPHQ-------------------- 156
Cdd:PRK13547 87 -------------VL-----------PQAAQPAFafsarEIVLLGRYPHA-RRAGALTHRdgeiawqalalagatalvgr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 157 ----FSGGQRQRIVIATALA---------CEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANI 223
Cdd:PRK13547 142 dvttLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARH 221
|
250 260
....*....|....*....|....*..
gi 579304020 224 ADRVAVMYGGQMVETGDVNEIFyDPKH 250
Cdd:PRK13547 222 ADRIAMLADGAIVAHGAPADVL-TPAH 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-248 |
1.66e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDiTAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeilfLGEDLAKKPENE 85
Cdd:PTZ00265 383 IQFKNVRFHYD-TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-------IINDSHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKdISMIFQDPM---TSLNPTMQIGKQVMEPLIKHKNY-------------SKAQAKKRALEILNLV-------G 142
Cdd:PTZ00265 455 LKWWRSK-IGVVSQDPLlfsNSIKNNIKYSLYSLKDLEALSNYynedgndsqenknKRNSCRAKCAGDLNDMsnttdsnE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 143 LPNAEKRF-------------KAYPHQF-------------------SGGQRQRIVIATALACEPKVLIADEPTTALDVT 190
Cdd:PTZ00265 534 LIEMRKNYqtikdsevvdvskKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 191 MQAQILDLMKELQQKIDTAIIFITHDLGVVaNIADRVAVMYGGQMVETGDVNEIFYDP 248
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-237 |
2.19e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 27 GVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKpenELIKLRgKDISMIFQDPMTsLN 106
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVE-----LERGRILIDGCDISKF---GLMDLR-KVLGIIPQAPVL-FS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 107 PTMQIGkqvMEPLIKHKNYSKAQAKKRA-LEIL---NLVGLpNAEkrFKAYPHQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:PLN03130 1327 GTVRFN---LDPFNEHNDADLWESLERAhLKDVirrNSLGL-DAE--VSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 183 PTTALDVTMQAQILDLMKElQQKIDTAIIfITHDLGVVANiADRVAVMYGGQMVE 237
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIRE-EFKSCTMLI-IAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-232 |
2.50e-10 |
|
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: 60.07 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 35 GETLAIVGESGSGKSVTTKAITKLFQGDTGRIKK----GEIL--FLGEDLakkpENELIKLRGKDISMIFQDPMTSLNPT 108
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdwDEILdeFRGSEL----QNYFTKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 109 MQIGKqvMEPLIKHKNysKAQAKKRALEILNLVGLPNAEKrfkaypHQFSGGQRQRIVIATALACEPKVLIADEPTTALD 188
Cdd:cd03236 102 AVKGK--VGELLKKKD--ERGKLDELVDQLELRHVLDRNI------DQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 579304020 189 VTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:cd03236 172 IKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-244 |
3.81e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 20 GEVQAVRGVDFYLNKGETLAIVGESGSGKSvttkaitklfqgdtgrikKGEI--LFLGEDLAKKP---ENELIKLRGKDI 94
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**------------------RGALpaHV*GPDAGRRPwrf*TWCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 95 SMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAyphQFSGGQRQRIVIATALACE 174
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 175 PKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-253 |
8.94e-10 |
|
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: 58.77 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 6 LEVNDLHVSFDITAGEVqaVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPene 85
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD-----IFDGKIVIDGIDISKLP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKdISMIFQDPMTsLNPTMQIGkqvMEPlikhknySKAQAKKRALEILNLVGLPNAekrFKAYP----------- 154
Cdd:cd03288 90 LHTLRSR-LSIILQDPIL-FSGSIRFN---LDP-------ECKCTDDRLWEALEIAQLKNM---VKSLPggldavvtegg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQaQILdlmkelqQKI------DTAIIFITHDLGVVANiADRVA 228
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NIL-------QKVvmtafaDRTVVTIAHRVSTILD-ADLVL 225
|
250 260
....*....|....*....|....*
gi 579304020 229 VMYGGQMVETGDVNEIFYDPKHPYT 253
Cdd:cd03288 226 VLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-232 |
9.60e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 14 SFDITAGEvqavrgvdfyLNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFLGEDLAKKPENelIKlrg 91
Cdd:cd03237 14 TLEVEGGS----------ISESEVIGILGPNGIGKTTFIKMLA-------GVLKpdEGDIEIELDTVSYKPQY--IK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 KDISMIFQDPMTSLNPTMqigkqvmeplikhknYSKAQAKKRALEILNLVGLPNAEKRfkayphQFSGGQRQRIVIATAL 171
Cdd:cd03237 72 ADYEGTVRDLLSSITKDF---------------YTHPYFKTEIAKPLQIEQILDREVP------ELSGGELQRVAIAACL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 172 ACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:cd03237 131 SKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
39-239 |
1.21e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 39 AIVGESGSGKSVttkaITKLFQGDTgRIKKGEILFLGEDLAKKPENeliKLRgKDISMIFQDPMT---SLNPTMQIGKQV 115
Cdd:PRK10790 371 ALVGHTGSGKST----LASLLMGYY-PLTEGEIRLDGRPLSSLSHS---VLR-QGVAMVQQDPVVladTFLANVTLGRDI 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 116 MEplikhknyskaQAKKRALEILNLV----GLPNA-EKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDV- 189
Cdd:PRK10790 442 SE-----------EQVWQALETVQLAelarSLPDGlYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSg 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 579304020 190 TMQA--QILDLMKElqqkiDTAIIFITHDLGVVANiADRVAVMYGGQMVETG 239
Cdd:PRK10790 511 TEQAiqQALAAVRE-----HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-246 |
1.69e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAKKpenELIKLRGKdISMIFQDPMTs 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGLNIAKI---GLHDLRFK-ITIIPQDPVL- 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMQIGkqvMEPLikhKNYSKAQAKKrALEILNLVGLPNAEKrfKAYPHQ-------FSGGQRQRIVIATALACEPKV 177
Cdd:TIGR00957 1372 FSGSLRMN---LDPF---SQYSDEEVWW-ALELAHLKTFVSALP--DKLDHEcaeggenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 178 LIADEPTTALDVTMQAQILDLMKelQQKIDTAIIFITHDLGVVANIAdRVAVMYGGQMVETGDVNE------IFY 246
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNllqqrgIFY 1514
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-240 |
2.71e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLakkPENELIKLRGKdISMIFQDPM- 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD-----VSEGDIRFHDIPL---TKLQLDSWRSR-LAVVSQTPFl 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 103 --TSLNPTMQIGKqvmeplikhKNYSKAQAKKRAL------EILNLvglPnaekrfKAYPHQ-------FSGGQRQRIVI 167
Cdd:PRK10789 401 fsDTVANNIALGR---------PDATQQEIEHVARlasvhdDILRL---P------QGYDTEvgergvmLSGGQKQRISI 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579304020 168 ATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKidTAIIFITHDLGVVANiADRVAVMYGGQMVETGD 240
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-227 |
3.81e-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: 54.69 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 34 KGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedlakkpeneliklrgkdismifqdpmtSLNPTmqigk 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------------------------------------YIDGE----- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 114 qvmeplikhknyskaqakkralEILNLVGLPNAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQA 193
Cdd:smart00382 40 ----------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579304020 194 QILDL-----MKELQQKIDTAIIFITHDLGVV--ANIADRV 227
Cdd:smart00382 98 LLLLLeelrlLLLLKSEKNLTVILTTNDEKDLgpALLRRRF 138
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-239 |
4.65e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFYLNkgETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGeilflGEDLakkpENELIKLRgKDISMIFQDPMtsLNP 107
Cdd:TIGR01257 951 ITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-----GKDI----ETNLDAVR-QSLGMCPQHNI--LFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 108 TMQIGKQVM-EPLIKHKNYSKAQAKKRA-LEILNLVGLPNAEKRfkayphQFSGGQRQRIVIATALACEPKVLIADEPTT 185
Cdd:TIGR01257 1017 HLTVAEHILfYAQLKGRSWEEAQLEMEAmLEDTGLHHKRNEEAQ------DLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579304020 186 ALDVTMQAQILDLMkeLQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETG 239
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-244 |
9.45e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 29 DFYLNKGETLAIVGESGSGKSVttkaitklfqgdtgrikkgeilflgedLAKKPENELIKLRG----------------- 91
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA---------------------------LARALAGELPLLSGerqsqfshitrlsfeql 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 92 -KDISMIFQDPMTS-LNPTMQ-IGKQVMEPLikhKNYSKAQAkkRALEILNLVGL-PNAEKRFKayphQFSGGQRQRIVI 167
Cdd:PRK10938 76 qKLVSDEWQRNNTDmLSPGEDdTGRTTAEII---QDEVKDPA--RCEQLAQQFGItALLDRRFK----YLSTGETRKTLL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 168 ATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
158-232 |
1.06e-08 |
|
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: 56.72 E-value: 1.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILYG 287
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
156-232 |
1.41e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 1.41e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQkiDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAYG 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-232 |
1.64e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFD-----ITAGEVqavrgvdfylNKGETLAIVGESGSGKSVTTKAITklfqgdtGRIK--KGEILFlG 75
Cdd:PRK13409 338 ETLVEYPDLTKKLGdfsleVEGGEI----------YEGEVIGIVGPNGIGKTTFAKLLA-------GVLKpdEGEVDP-E 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 76 EDLAKKPEneLIKlrgKDISMIFQDPMtslnptMQIGKQVMEPLIKHknyskaqakkralEILNLVGLpnaEKRFKAYPH 155
Cdd:PRK13409 400 LKISYKPQ--YIK---PDYDGTVEDLL------RSITDDLGSSYYKS-------------EIIKPLQL---ERLLDKNVK 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-245 |
3.40e-08 |
|
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: 55.34 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 14 SFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGEILFLgedlakkPENELIKlrgk 92
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHmKGSVAYV-------PQQAWIQ---- 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 93 dismifqdpMTSLNPTMQIGKQVMEPliKHKNYSKAQAKKRALEILnlvglPNAEK-RFKAYPHQFSGGQRQRIVIATAL 171
Cdd:TIGR00957 712 ---------NDSLRENILFGKALNEK--YYQQVLEACALLPDLEIL-----PSGDRtEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 172 ACEPKVLIADEPTTALDVTMQAQILDL----MKELQQKIDtaiIFITHDLGVVANIaDRVAVMYGGQMVETGDVNEIF 245
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEHvigpEGVLKNKTR---ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-244 |
4.00e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIK-KGE--ILFLGEDLAKKPEN-ELIKLRGkdISM-IF 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDiKGSaaLIAISSGLNGQLTGiENIELKG--LMMgLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 99 QDPMTSLNPTM----QIGKQVMEPLikhKNYSKaqakkraleilnlvglpnaekrfkayphqfsgGQRQRIVIATALACE 174
Cdd:PRK13545 117 KEKIKEIIPEIiefaDIGKFIYQPV---KTYSS--------------------------------GMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 175 PKVLIADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK13545 162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-244 |
1.58e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 25 VRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQgdtgrIKKGEILFLGEDLAKKPENELIKLrgkdISMIFQDPMTs 104
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREIGAYGLRELRRQ----FSMIPQDPVL- 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 105 LNPTMqigKQVMEPLIKHknySKAQAkKRALEilnLVGL--------PNAEKRFKAYPHQFSGGQRQRIVIATALACEPK 176
Cdd:PTZ00243 1396 FDGTV---RQNVDPFLEA---SSAEV-WAALE---LVGLrervasesEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 177 VLI-ADEPTTALDVTMQAQIldlmkelQQKIDTA-----IIFITHDLGVVANIaDRVAVMYGGQMVETGDVNEI 244
Cdd:PTZ00243 1466 GFIlMDEATANIDPALDRQI-------QATVMSAfsaytVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-232 |
1.66e-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: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 1 MTERILEVNDLHVSFD-----ITAGEVqavrgvdfylNKGETLAIVGESGSGKsvTTKAitKLFqgdTGRIK--KGEIlF 73
Cdd:COG1245 337 EEETLVEYPDLTKSYGgfsleVEGGEI----------REGEVLGIVGPNGIGK--TTFA--KIL---AGVLKpdEGEV-D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 74 LGEDLAKKPEneliKLRGkDISMifqdpmtslnptmqigkQVMEPLIKHkNYSKAQAKKRALEILNLVGLpnaEKRFKAY 153
Cdd:COG1245 399 EDLKISYKPQ----YISP-DYDG-----------------TVEEFLRSA-NTDDFGSSYYKTEIIKPLGL---EKLLDKN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 154 PHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYG 232
Cdd:COG1245 453 VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-243 |
1.76e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGdtgriKKGEILFLGEDLAKKPENELIKLrgkdISMIFQDpmt 103
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP-----QSGEILLDGKPVTAEQPEDYRKL----FSAVFTD--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 slnptMQIGKQVMEPlikhKNYSKAQAKKRA-LEILNLVG-LPNAEKRFKAYphQFSGGQRQRIVIATALACEPKVLIAD 181
Cdd:PRK10522 406 -----FHLFDQLLGP----EGKPANPALVEKwLERLKMAHkLELEDGRISNL--KLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 182 EPTTALDVTMQAQI-LDLMKELQQKIDTaIIFITHDLGVVANiADRVAVMYGGQMVE-TGDVNE 243
Cdd:PRK10522 475 EWAADQDPHFRREFyQVLLPLLQEMGKT-IFAISHDDHYFIH-ADRLLEMRNGQLSElTGEERD 536
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-233 |
2.19e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.18 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIkkgeilFLGEDLAKKPENELIKLRGK-DISMIFQDPMTsLN 106
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------HWSNKNESEPSFEATRSRNRySVAYAAQKPWL-LN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 107 PTMQIGKQVMEPLIK--HKNYSKAQAKKRALEILnlvglPNAEK-RFKAYPHQFSGGQRQRIVIATALACEPKVLIADEP 183
Cdd:cd03290 93 ATVEENITFGSPFNKqrYKAVTDACSLQPDIDLL-----PFGDQtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 184 TTALDV-----TMQAQILDLMKELQQkidtAIIFITHDLGVVANiADRVAVMYGG 233
Cdd:cd03290 168 FSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-216 |
2.78e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFditaGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLG------EDL 78
Cdd:TIGR03719 322 VIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAyvdqsrDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 79 -AKKPENELIKlRGKDIsmifqdpmtslnptMQIGKqvmeplikhknyskAQAKKRA-LEILNLVGlPNAEKRFKayphQ 156
Cdd:TIGR03719 398 dPNKTVWEEIS-GGLDI--------------IKLGK--------------REIPSRAyVGRFNFKG-SDQQKKVG----Q 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDV-TMQAqildlmkeLQQKID----TAIIfITHD 216
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLRA--------LEEALLnfagCAVV-ISHD 499
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-239 |
3.65e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSvttkaiTKLFQGdtgrikkgeilflgedLAKKPENELIKLRgkdismifqd 100
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKS------TLVNEG----------------LYASGKARLISFL---------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 101 PMTSLNPTMQIGKqvMEPLIKhknyskaqakkraleiLNLVGLPNAEKRfkaypHQFSGGQRQRIVIATALACEPK--VL 178
Cdd:cd03238 55 PKFSRNKLIFIDQ--LQFLID----------------VGLGYLTLGQKL-----STLSGGELQRVKLASELFSEPPgtLF 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579304020 179 IADEPTTALDVTMQAQILDLMKELQQKIDTaIIFITHDLGVVANiADRVAVM------YGGQMVETG 239
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGLIDLGNT-VILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
158-249 |
5.55e-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: 49.11 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGgqmvE 237
Cdd:cd03222 73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG----E 148
|
90
....*....|..
gi 579304020 238 TGdVNEIFYDPK 249
Cdd:cd03222 149 PG-VYGIASQPK 159
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
158-236 |
5.72e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKEL--QQKidtAIIFITHDLGVVANIADRVAVMYGGQM 235
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELaaEGK---GVIVISSELPELLGMCDRIYVMNEGRI 482
|
.
gi 579304020 236 V 236
Cdd:NF040905 483 T 483
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-231 |
7.09e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.51 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 155 HQFSGGQRQRIVIATALA---CEPKVLIA-DEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGvVANIADRVAVM 230
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPE-LAELADKLIHI 153
|
.
gi 579304020 231 Y 231
Cdd:cd03227 154 K 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-250 |
7.16e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 21 EVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAIT-KLFQGDTGriKKGEILFLG---EDLAKKPENELIKLRGKDISM 96
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDGFHIG--VEGVITYDGitpEEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 97 ifqdPMTSLNPTMQIGKQVMEPLIKHKNYSK-AQAKKRALEILNLVGLPNAE--KRFKAYPHQFSGGQRQRIVIATALAC 173
Cdd:TIGR00956 151 ----PHLTVGETLDFAARCKTPQNRPDGVSReEYAKHIADVYMATYGLSHTRntKVGNDFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 174 EPKVLIADEPTTALDVTMQAQILDLMKELQQKID-TAIIFITHDLGVVANIADRVAVMYGGQmvetgdvnEIFYDPKH 250
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGY--------QIYFGPAD 296
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
158-234 |
1.09e-06 |
|
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: 48.62 E-value: 1.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILD--LMKELqqKIDTAIIFITHDLGVVANiADRVAVMYGGQ 234
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-215 |
2.55e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFYLNKGETLAIVGESGSGKSVTTKAITKLFqgdtgRIKKGEILFLGEDLAKkpeneliKLRGKDISMIFQDPMTSLNP 107
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL-----NPEKGEILFERQSIKK-------DLCTYQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 108 TMQigkqvmeplIKHKNYSKAQAKKRALEILNLVGLPNAEkRFKAYP-HQFSGGQRQRIVIATALACEPKVLIADEPTTA 186
Cdd:PRK13540 88 YLT---------LRENCLYDIHFSPGAVGITELCRLFSLE-HLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|.
gi 579304020 187 LDvtmQAQILDLMKELQ--QKIDTAIIFITH 215
Cdd:PRK13540 158 LD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-244 |
4.56e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 24 AVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKkgeilflgedlakkpeneliklRGKDISMIFQDPMT 103
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD----------------------RNGEVSVIAISAGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 104 SLNPTmqiGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLpnaeKRFKAYP-HQFSGGQRQRIVIATALACEPKVLIADE 182
Cdd:PRK13546 97 SGQLT---GIENIEFKMLCMGFKRKEIKAMTPKIIEFSEL----GEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579304020 183 PTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEI 244
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-222 |
5.13e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 26 RGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGrikkgEILFLGEDLAKKPEneliklrgkdismIFQDPMtsl 105
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG-----EVLWQGEPIRRQRD-------------EYHQDL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 106 nptMQIGKQvmePLIK---------------HKNYSKAQAkkraLEILNLVGLpnaeKRFKAYP-HQFSGGQRQRIVIAT 169
Cdd:PRK13538 77 ---LYLGHQ---PGIKteltalenlrfyqrlHGPGDDEAL----WEALAQVGL----AGFEDVPvRQLSAGQQRRVALAR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 170 ALACEPKVLIADEPTTALDVTMQAQILDLMKE-LQQkiDTAIIFITH-DLGVVAN 222
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQ--GGMVILTTHqDLPVASD 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-202 |
7.26e-06 |
|
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: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 3 ERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKlfQGDTGRIKKGEILFLGEDLAKKP 82
Cdd:TIGR00956 757 EDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 83 ENELIKLRGKDI---------SMIF-----QDPMTSLNPTMQIGKQVMEpLIKHKNYSKAqakkraleilnLVGLP---- 144
Cdd:TIGR00956 835 QRSIGYVQQQDLhlptstvreSLRFsaylrQPKSVSKSEKMEYVEEVIK-LLEMESYADA-----------VVGVPgegl 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 145 NAEkrfkayphqfsggQRQRIVIATALACEPKVLI-ADEPTTALDVTMQAQILDLMKEL 202
Cdd:TIGR00956 903 NVE-------------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
158-244 |
2.12e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILD--LMKELQQKIDtaiIFITHDLGVVANIaDRVAVMYGGQM 235
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTR---VLVTNQLHFLSQV-DRIILVHEGMI 817
|
....*....
gi 579304020 236 VETGDVNEI 244
Cdd:PLN03130 818 KEEGTYEEL 826
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-189 |
2.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 2.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 130 AKKRALEILnlVGLP-NAEKRFKAyPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDV 189
Cdd:PLN03073 320 AEARAASIL--AGLSfTPEMQVKA-TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
147-221 |
3.45e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 3.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 147 EKRFKAYPHQFSGGQRQRIVIATALAC---EPKVLIADEPTTALDVTMQAQILDLMKELQQKiDTAIIFITHDLGVVA 221
Cdd:pfam13304 227 GGGGELPAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRN-GAQLILTTHSPLLLD 303
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
158-245 |
4.56e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILD--LMKELQQKIDTAIIFITHDLGVVaniaDRVAVMYGGQM 235
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTRVLVTNQLHFLPLM----DRIILVSEGMI 817
|
90
....*....|
gi 579304020 236 VETGDVNEIF 245
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
158-239 |
4.87e-05 |
|
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: 44.53 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATAL---ACEPKVLIADEPTTAL---DVtmqAQILDLMKELQQKIDTAIIfITHDLGVVANiADRVAVM- 230
Cdd:cd03271 171 SGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfhDV---KKLLEVLQRLVDKGNTVVV-IEHNLDVIKC-ADWIIDLg 245
|
90
....*....|....
gi 579304020 231 -----YGGQMVETG 239
Cdd:cd03271 246 peggdGGGQVVASG 259
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
157-227 |
1.09e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 1.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579304020 157 FSGGQRQRIVIATALACEPKVLIADEPTTALDvtMQAQILdLMKELQQKIDTaIIFITHDLGVVANIADRV 227
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIW-LEKWLKSYQGT-LILISHDRDFLDPIVDKI 216
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
156-243 |
1.91e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 156 QFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELqqkiDTAIIFITHDLGVVANIADRVAVMYGGQm 235
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLLRSTTDDLYLVHDGK- 504
|
90
....*....|
gi 579304020 236 VE--TGDVNE 243
Cdd:PRK10636 505 VEpfDGDLED 514
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-268 |
2.02e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.46 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 35 GETLAIVGESGSGKSVTTKAITklfqGDTGrIKKGEILFLGEDLAKkpeneliklrgkDISMIFQD----PMTSLNPTMQ 110
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLT----GDTT-VTSGDATVAGKSILT------------NISDVHQNmgycPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 111 IGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAyphQFSGGQRQRIVIATALACEPKVLIADEPTTALDVT 190
Cdd:TIGR01257 2028 TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579304020 191 MQAQILDLMKELQQKiDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIfydpKHPYTWGLLSSMPDLSTTND 268
Cdd:TIGR01257 2105 ARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDGYIVTMKIKSPKDD 2177
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
158-239 |
2.14e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 158 SGGQRQRIVIATAL---ACEPKVLIADEPTTAL---DVtmqAQILDLMKELQQKIDTAIIfITHDLGVVANiADRVAVM- 230
Cdd:TIGR00630 831 SGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGNTVVV-IEHNLDVIKT-ADYIIDLg 905
|
90
....*....|....
gi 579304020 231 -----YGGQMVETG 239
Cdd:TIGR00630 906 peggdGGGTVVASG 919
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
126-215 |
2.28e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 126 SKAQAKKrALEILNLVGLPN--AEKRFkaypHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQ 203
Cdd:PRK10938 374 SDRQQKL-AQQWLDILGIDKrtADAPF----HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLI 448
|
90
....*....|..
gi 579304020 204 QKIDTAIIFITH 215
Cdd:PRK10938 449 SEGETQLLFVSH 460
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-239 |
2.63e-04 |
|
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: 41.86 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 26 RGVDFYLNKGETLAIVGESGSGKSvtTKAITKLFQgdTGRIKKGEIL------FLGEdlAKKPENELIKlrGKDISMIFQ 99
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKS--SLAFDTIYA--EGQRRYVESLsayarqFLGQ--MDKPDVDSIE--GLSPAIAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 100 DPMTSLNPTMQIGkQVME-----PLIkhknYSKAQAKKRaLEILNLVGLP------NAEkrfkayphQFSGGQRQRIVIA 168
Cdd:cd03270 84 QKTTSRNPRSTVG-TVTEiydylRLL----FARVGIRER-LGFLVDVGLGyltlsrSAP--------TLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 169 TALACE-PKVL-IADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANiADRV------AVMYGGQMVETG 239
Cdd:cd03270 150 TQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLV-VEHDEDTIRA-ADHVidigpgAGVHGGEIVAQG 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-215 |
3.25e-04 |
|
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: 42.43 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 5 ILEVNDLHVSFD-----ITAGEVqAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKK---GEILFLge 76
Cdd:TIGR00954 444 IVEYQDNGIKFEniplvTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpakGKLFYV-- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 77 dlAKKPENELIKLRGKDISmifqdPMTSLNptmqigkqvmeplIKHKNYSKAQAKKraleILNLVGLPNAEKR---FKA- 152
Cdd:TIGR00954 521 --PQRPYMTLGTLRDQIIY-----PDSSED-------------MKRRGLSDKDLEQ----ILDNVQLTHILEReggWSAv 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579304020 153 --YPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQaqilDLMKELQQKIDTAIIFITH 215
Cdd:TIGR00954 577 qdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFGITLFSVSH 637
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
28-226 |
1.39e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 39.88 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 28 VDFylNKGETlAIVGESGSGKSVTTKAITKLF--QGDTGRIKKGE----------------ILFLGEDLAKKPENELIKL 89
Cdd:cd03241 17 LDF--EEGLT-VLTGETGAGKSILLDALSLLLggRASADLIRSGAekavvegvfdisdeeeAKALLLELGIEDDDDLIIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 90 R-----GKDISMIfQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQaKKRALEILNLvGLPNAEKRFKAYPHQ-------- 156
Cdd:cd03241 94 ReisrkGRSRYFI-NGQSVTLKLLRELGSLLVDIHGQHDHQNLLN-PERQLDLLDG-GLDDVEFLFSTNPGEplkplaki 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579304020 157 FSGGQRQRIVIA-TALACEPK---VLIADEPTTALDVTMQAQILDLMKELQQKidTAIIFITHdLGVVANIADR 226
Cdd:cd03241 171 ASGGELSRLMLAlKAILARKDavpTLIFDEIDTGISGEVAQAVGKKLKELSRS--HQVLCITH-LPQVAAMADN 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
86-208 |
2.14e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 86 LIKLRGKDISMIFQDpmtslnptmqigkQVMEpLIKHKNYSKAqakkraleilnLVGLPNAEKrfkayphqFSGGQRQRI 165
Cdd:PLN03140 982 LPKEVSKEEKMMFVD-------------EVME-LVELDNLKDA-----------IVGLPGVTG--------LSTEQRKRL 1028
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 579304020 166 VIATALACEPKVLIADEPTTALDVTMQAQIldlMKELQQKIDT 208
Cdd:PLN03140 1029 TIAVELVANPSIIFMDEPTSGLDARAAAIV---MRTVRNTVDT 1068
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-66 |
3.08e-03 |
|
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: 39.40 E-value: 3.08e-03
10 20 30
....*....|....*....|....*....|....*....
gi 579304020 28 VDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRI 66
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
81-249 |
4.01e-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: 39.23 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 81 KPENELIKLRGKDISMIFQDPMT-------SLNPTMQiGKQVMEPLIKhknyskaQAKKRaLEILNLVGLP--NAEKRFK 151
Cdd:TIGR00630 417 KPEALAVTVGGKSIADVSELSIReaheffnQLTLTPE-EKKIAEEVLK-------EIRER-LGFLIDVGLDylSLSRAAG 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 152 AyphqFSGGQRQRIVIATALACE-PKVL-IADEPTTALDVTMQAQILDLMKELQQKIDTAIIfITHDLGVVANiADRV-- 227
Cdd:TIGR00630 488 T----LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV-VEHDEDTIRA-ADYVid 561
|
170 180
....*....|....*....|....*.
gi 579304020 228 ----AVMYGGQMVETGDVNEIFYDPK 249
Cdd:TIGR00630 562 igpgAGEHGGEVVASGTPEEILANPD 587
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
167-225 |
4.22e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.49 E-value: 4.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 167 IATALAcEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIAD 225
Cdd:COG1106 217 LLDALA-KGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHSTELLDAFLE 274
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
130-216 |
4.46e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 130 AKKRALEILNLVGLPnAEKRFKAYpHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTmqaQILDLMKELQQKIDTA 209
Cdd:PRK15064 131 AEARAGELLLGVGIP-EEQHYGLM-SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN---TIRWLEDVLNERNSTM 205
|
....*..
gi 579304020 210 IIfITHD 216
Cdd:PRK15064 206 II-ISHD 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
160-239 |
5.00e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.95 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579304020 160 GQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKEL--QQKIdTaiIFI-THDLgvvaNIA---DRVAVMYGG 233
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGV-T--IFIsTHFM----NEAercDRISLMHAG 473
|
....*.
gi 579304020 234 QMVETG 239
Cdd:NF033858 474 RVLASD 479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
158-216 |
5.55e-03 |
|
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: 38.76 E-value: 5.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 579304020 158 SGGQRQRIVIATALACEPKVLIADEPTTALDvtmqAQILDLMKELQQKIDTAIIFITHD 216
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| |
