|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-529 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 1059.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLH 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNY 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 241 AATLFASPTHPYTQKLLNSEPSGDPVPLPEPASTLLDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGE 320
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 321 SGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
Cdd:PRK15134 321 SGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 401 REQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYL 480
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16130118 481 FISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLALS 529
Cdd:PRK15134 481 FISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-527 |
0e+00 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 980.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVeYLSGDIRFHGESLLH 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAA-HPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNY 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 241 AATLFASPTHPYTQKLLNSEPSGDPVPLPEPASTLLDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGE 320
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 321 SGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
Cdd:COG4172 321 SGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 401 REQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYL 480
Cdd:COG4172 401 RRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16130118 481 FISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLA 527
Cdd:COG4172 481 FISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLA 527
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-527 |
0e+00 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 629.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQQtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVeyLSGDIRFHGESLLHAS 82
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGR--ISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQtlrgVRGNKIAMIFQEPMVSLNPLhTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGER 162
Cdd:COG1123 78 EA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDR---YPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAA 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 243 TLFASPTHPYTQKLLNSePSGDPVPLPEPASTLLDVEQLQVAFPIRKGilkrivDHNVVVKNISFTLRAGETLGLVGESG 322
Cdd:COG1123 229 EILAAPQALAAVPRLGA-ARGRAAPAAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 323 SGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQR 401
Cdd:COG1123 302 SGKSTLARLLLGLLRpTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHG-LLSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 402 EQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLF 481
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 16130118 482 ISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLA 527
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLA 506
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-527 |
1.54e-168 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 490.91 E-value: 1.54e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGES---- 77
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 78 -LLHASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQ 156
Cdd:PRK10261 89 eLSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 237 EQNYAATLFASPTHPYTQKLLNSEP-----SGDPVP-------LPEPASTLLDVEQ---------LQV-----AFPIRKG 290
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPqlgamKGLDYPrrfplisLEHPAKQEPPIEQdtvvdgepiLQVrnlvtRFPLRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 291 ILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQLLPIRHRIQVVFQ 369
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 370 DPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVHG-LLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLA 527
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-265 |
1.66e-138 |
|
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: 402.89 E-value: 1.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEylSGDIRFHGESLLHASDQ 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 16130118 245 FASPTHPYTQKLLNSEPSGDP 265
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
269-527 |
2.11e-119 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 354.42 E-value: 2.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 269 PEPASTLLDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQ 347
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEpTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 348 PLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFS 427
Cdd:COG4608 81 DITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHG-LASKAERRERVAELLELVGLRPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQ 507
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260
....*....|....*....|
gi 16130118 508 GPCARVFATPQQEYTRQLLA 527
Cdd:COG4608 240 APRDELYARPLHPYTQALLS 259
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-527 |
5.56e-113 |
|
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: 337.80 E-value: 5.56e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI----NSQGSIIFDGQPLQ 350
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 351 NLNRRQLLPIRHR-IQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMHEVGL-DPETR-HRYPAEFS 427
Cdd:COG0444 74 KLSEKELRKIRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLpDPERRlDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQ 507
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250 260
....*....|....*....|
gi 16130118 508 GPCARVFATPQQEYTRQLLA 527
Cdd:COG0444 233 GPVEELFENPRHPYTRALLS 252
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-508 |
6.52e-109 |
|
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: 323.69 E-value: 6.52e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQNLN 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVK-------ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 354 RRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-239 |
4.84e-108 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 321.76 E-value: 4.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESLLHASDQ 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP-----TSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRgVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILnCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
Cdd:cd03257 76 LRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQN 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-265 |
3.46e-100 |
|
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: 311.84 E-value: 3.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFR-HQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVeylSGDIRFHGESLL 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR--PT---SGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 HASDQTLRGVRGnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdYPHQLSG 159
Cdd:COG1123 331 KLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR--YPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQN 239
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250 260
....*....|....*....|....*.
gi 16130118 240 YAATLFASPTHPYTQKLLNSEPSGDP 265
Cdd:COG1123 488 PTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-529 |
3.86e-99 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 299.41 E-value: 3.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQnln 353
Cdd:COG1124 1 MLEVRNLSVSYGQGG-------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVT--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 354 RRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqptlSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQR 433
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIH----GLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARV 513
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*.
gi 16130118 514 FATPQQEYTRQLLALS 529
Cdd:COG1124 227 LAGPKHPYTRELLAAS 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-265 |
2.84e-95 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 292.79 E-value: 2.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGF--------RHQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDI 71
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgRTVGVVKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePT------SGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 72 RFHGESLLHASDQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIR-QAAKRl 150
Cdd:COG4608 76 LFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADR- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 151 tdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVM 230
Cdd:COG4608 154 --YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
|
250 260 270
....*....|....*....|....*....|....*
gi 16130118 231 QNGRCVEQNYAATLFASPTHPYTQKLLNSEPSGDP 265
Cdd:COG4608 232 YLGKIVEIAPRDELYARPLHPYTQALLSAVPVPDP 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-264 |
1.32e-94 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 290.86 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVeyLSGDIRFHGESLLHASDQ 84
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGR--IGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
Cdd:PRK09473 90 ELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
250 260
....*....|....*....|
gi 16130118 245 FASPTHPYTQKLLNSEPSGD 264
Cdd:PRK09473 250 FYQPSHPYSIGLLNAVPRLD 269
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-264 |
1.17e-89 |
|
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: 285.04 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQQTV--RTV-----VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveylSGDIRFHGE 76
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLfrRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS------EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 77 SLLHASDQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-GMRREAARGEILNCLDRVGI-RQAAKRltdYP 154
Cdd:COG4172 348 DLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHR---YP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|
gi 16130118 235 CVEQNYAATLFASPTHPYTQKLLNSEPSGD 264
Cdd:COG4172 504 VVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-259 |
6.38e-89 |
|
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: 273.22 E-value: 6.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVeylSGDIRFHGESLLHASDQ 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER--PW---SGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGvrgnKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAargEILNCLDRVGIRQAAkrLTDYPHQLSGGERQR 164
Cdd:COG1124 76 AFRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE---RIAELLEQVGLPPSF--LDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*
gi 16130118 245 FASPTHPYTQKLLNS 259
Cdd:COG1124 227 LAGPKHPYTRELLAA 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
273-526 |
2.36e-87 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 269.78 E-value: 2.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFPIRKGILKRivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQ 347
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRR--QQFEAVKPVSFTLEAGQTLAIIGENGSGKST----LAKMLAgiiepTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 348 PLQNLNRRQllpiR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETRHRYPAEF 426
Cdd:COG4167 76 KLEYGDYKY----RcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNT-DLTAEEREERIFATLRLVGLLPEHANFYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVE 506
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|
gi 16130118 507 QGPCARVFATPQQEYTRQLL 526
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLI 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
274-527 |
1.62e-84 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 264.90 E-value: 1.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 274 TLLDVEQLQVAFPIRKGILKrivDHNVV--VKNISFTLRAGETLGLVGESGSGKSTTGlALLRLIN--SQGSIIFDGQPL 349
Cdd:PRK11308 4 PLLQAIDLKKHYPVKRGLFK---PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLA-RLLTMIEtpTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 350 QNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGG 429
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINT-SLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
250
....*....|....*...
gi 16130118 510 CARVFATPQQEYTRQLLA 527
Cdd:PRK11308 239 KEQIFNNPRHPYTQALLS 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
275-527 |
6.36e-82 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 258.48 E-value: 6.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKG---------ILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIF 344
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwfwqppkTLK-------AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 345 DGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPA 424
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
250 260
....*....|....*....|...
gi 16130118 505 VEQGPCARVFATPQQEYTRQLLA 527
Cdd:PRK15079 241 VELGTYDEVYHNPLHPYTKALMS 263
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-261 |
6.51e-81 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 255.44 E-value: 6.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPvEYLSGDIRFHGESLLHASDQ 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPG-RVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*..
gi 16130118 245 FASPTHPYTQKLLNSEP 261
Cdd:PRK11022 242 FRAPRHPYTQALLRALP 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-265 |
5.32e-74 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 237.56 E-value: 5.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 15 FRHQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTAlsilRLL-----PSppveylSGDIRFHGESLLHASDQTLRGV 89
Cdd:PRK11308 22 FKPERLVKAL-DGVSFTLERGKTLAVVGESGCGKSTLA----RLLtmietPT------GGELYYQGQDLLKADPEAQKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 90 RgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIR-QAAKRltdYPHQLSGGERQRVMIA 168
Cdd:PRK11308 91 R-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDR---YPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASP 248
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
250
....*....|....*..
gi 16130118 249 THPYTQKLLNSEPSGDP 265
Cdd:PRK11308 247 RHPYTQALLSATPRLNP 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
272-526 |
2.73e-66 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 217.67 E-value: 2.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 272 ASTLLDVEQLQVAFPIRKGILkrivdhnVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQG----SIIFDGQ 347
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDV-------TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGriggSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 348 PLQNLNRRQLLPIR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLdPETRHR---YP 423
Cdd:PRK09473 82 EILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHK-GMSKAEAFEESVRMLDAVKM-PEARKRmkmYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGE 503
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
250 260
....*....|....*....|...
gi 16130118 504 VVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK09473 240 TMEYGNARDVFYQPSHPYSIGLL 262
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-275 |
3.95e-65 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 214.77 E-value: 3.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVEYLSGD-IRFHGESLLHASD 83
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK--DNWHVTADrFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVL--SLHRGM---RREAARGEILNCLDRVGIRQAAKRLTDYPHQLS 158
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpsWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 16130118 239 NYAATLFASPTHPYTQKLLNSEPS-GDPVPLPEPASTL 275
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDfRQPLPHKSRLNTL 278
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
278-527 |
2.25e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 213.02 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 278 VEQLQVAFPIRKGILkrivdhnVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNL 352
Cdd:COG1135 4 LENLSKTFPTKGGPV-------TALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINllerpTSGSVLVDGVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 353 NRRQLLPIRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQ 432
Cdd:COG1135 73 SERELRAARRKIGMIFQHFN--LLSSRTVAENVALPLEIAG--VPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 433 RIAIARALILKPSLIILDEPTSSLD-KTVQaQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCA 511
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDpETTR-SILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250
....*....|....*.
gi 16130118 512 RVFATPQQEYTRQLLA 527
Cdd:COG1135 227 DVFANPQSELTRRFLP 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-271 |
3.45e-64 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 212.26 E-value: 3.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQ----------QTVRTVvNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIR 72
Cdd:PRK15079 6 KVLLEVADLKVHFDIKdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGL-----VKATDGEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 73 FHGESLLHASDQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVL-SLHRGMRREAARGEILNCLDRVGIRqaAKRLT 151
Cdd:PRK15079 80 WLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLL--PNLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16130118 232 NGRCVEQNYAATLFASPTHPYTQKLLNSepsgdpVPLPEP 271
Cdd:PRK15079 237 LGHAVELGTYDEVYHNPLHPYTKALMSA------VPIPDP 270
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-257 |
7.93e-64 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 208.79 E-value: 7.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfrhqQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsPPVEYLSGDIRFHGESLLHASdqt 85
Cdd:PRK10418 5 IELRNIAL-----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGVRQTAGRVLLDGKPVAPCA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 lrgVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLsLHRGmrREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRV 165
Cdd:PRK10418 76 ---LRGRKIATIMQNPRSAFNPLHTMHTHARETC-LALG--KPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLF 245
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|..
gi 16130118 246 ASPTHPYTQKLL 257
Cdd:PRK10418 230 NAPKHAVTRSLV 241
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
288-527 |
2.49e-63 |
|
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: 207.74 E-value: 2.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 288 RKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLLPIRHRIQV 366
Cdd:TIGR02769 13 RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLDRKQRRAFRRDVQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPNSSLNPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
Cdd:TIGR02769 93 VFQDSPSAVNPRMTVRQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFaTPQQEYTRQLL 526
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL-SFKHPAGRNLQ 250
|
.
gi 16130118 527 A 527
Cdd:TIGR02769 251 S 251
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
273-509 |
3.56e-61 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 202.22 E-value: 3.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFpiRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQN 351
Cdd:PRK10419 1 MTLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 352 LNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQR 431
Cdd:PRK10419 79 LNRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-527 |
5.82e-61 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 201.56 E-value: 5.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 274 TLLDVEQLQVAFPIRKGILKRivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNL 352
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 353 N---RRQllpirhRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGG 429
Cdd:PRK15112 81 DysyRSQ------RIRMIFQDPSTSLNPRQRISQILDFPLRLNT-DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*...
gi 16130118 510 CARVFATPQQEYTRQLLA 527
Cdd:PRK15112 234 TADVLASPLHELTKRLIA 251
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
299-526 |
6.36e-60 |
|
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: 197.89 E-value: 6.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDP-- 371
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSV----LLKLIIgllrpDSGEILVDGQDITGLSEKELYELRRRIGMLFQGGal 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 -NSslnprLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:COG1127 94 fDS-----LTVFENVAFPLREH-TDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEILLYD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPqQEYTRQLL 526
Cdd:COG1127 167 EPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
300-518 |
1.82e-59 |
|
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: 196.26 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNss 374
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINglerpTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQHFN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03258 93 LLSSRTVFENVALPLEIAG--VPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:cd03258 170 ALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-259 |
2.24e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 197.37 E-value: 2.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLS------VGFRHQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLpSPPVEYLSGDIRFHGES 77
Cdd:COG4167 3 ALLEVRNLSktfkyrTGLFRRQQF-EAVKPVSFTLEAGQTLAIIGENGSGKSTLA----KML-AGIIEPTSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 78 LLHASDQTlrgvRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRqaAKRLTDYPHQL 157
Cdd:COG4167 77 LEYGDYKY----RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLL--PEHANFYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 16130118 238 QNYAATLFASPTHPYTQKLLNS 259
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIES 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-526 |
2.17e-57 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 194.19 E-value: 2.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSII-----FDGQPL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekleFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 350 QNLN---RRQLlpIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMHEVGL-DPETR-HRYPA 424
Cdd:PRK11022 76 QRISekeRRNL--VGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKKTRRQRAIDLLNQVGIpDPASRlDVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
250 260
....*....|....*....|..
gi 16130118 505 VEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK11022 233 VETGKAHDIFRAPRHPYTQALL 254
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
297-524 |
1.45e-55 |
|
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: 186.17 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ-----GSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDp 371
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKST----LLRLIVGLlrpdsGEVLIDGEDISGLSEAELYRLRRRMGMLFQS- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 nSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03261 86 -GALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATpQQEYTRQ 524
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQ 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-265 |
4.23e-55 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 195.46 E-value: 4.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQTLRGVRGNkIAMIFQEPMVS 104
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRL-----VESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIR-QAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWR---YPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 184 TTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLLNSEPSG 263
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA 570
|
..
gi 16130118 264 DP 265
Cdd:PRK10261 571 DP 572
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
297-515 |
5.02e-55 |
|
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: 184.46 E-value: 5.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQllpIRHRIQVVFQDP 371
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKST----LLRLLNgllkpTSGEVLVDGKDITKKNLRE---LRRKVGLVFQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NSslnprlnvlQIIEE--------GLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:COG1122 85 DD---------QLFAPtveedvafGPENLG--LPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-238 |
7.19e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 184.09 E-value: 7.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSppveylSGDIRFHGESLLH 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPT------SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLRGVRGNKIAMIFQEPmvslnplhtlekQLYEVLS---------LHRGMRREAARGEILNCLDRVGIrqaAKRLT 151
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF------------NLLPELTalenvalplLLAGVSRKERRERARELLERVGL---GDRLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRkLAHRVAVMQ 231
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLR 218
|
....*..
gi 16130118 232 NGRCVEQ 238
Cdd:COG1136 219 DGRIVSD 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
300-507 |
6.90e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 181.39 E-value: 6.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIR-HRIQVVFQDPNs 373
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVLIDGQDISSLSERELARLRrRHIGFVFQFFN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 sLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:COG1136 97 -LLPELTALENVALPLLLAG--VSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQ 507
Cdd:COG1136 173 GNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-265 |
1.13e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.51 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLHAS 82
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCInllerPT------SGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRGVRGnKIAMIFQepmvSLNPLHT----------LEkqlyevlslHRGMRREAARGEILNCLDRVGIRQAAKRltd 152
Cdd:COG1135 74 ERELRAARR-KIGMIFQ----HFNLLSSrtvaenvalpLE---------IAGVPKAEIRKRVAELLELVGLSDKADA--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQN 232
Cdd:COG1135 137 YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250 260 270
....*....|....*....|....*....|...
gi 16130118 233 GRCVEQNYAATLFASPTHPYTQKLLNSEPSGDP 265
Cdd:COG1135 217 GRIVEQGPVLDVFANPQSELTRRFLPTVLNDEL 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
297-527 |
6.18e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.42 E-value: 6.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqNLNRRQLLPIRHRIQVVFQDP 371
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINlleepDSGTITVDGEDL-TDSKKDINKLRRKVGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NssLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:COG1126 87 N--LFPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLA 527
Cdd:COG1126 163 PTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
289-513 |
1.16e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.10 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHR 363
Cdd:COG3638 6 RNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNglvepTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTL-------SAAQReQQVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAI 436
Cdd:COG3638 82 IGMIFQQFN--LVPRLSVLTNVLAGRLGRTSTWrsllglfPPEDR-ERALEALERVGLADKAYQR-ADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 437 ARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARV 513
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-234 |
7.70e-52 |
|
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: 175.76 E-value: 7.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQT 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPT----SGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGNKIAMIFQEpmvslnplHTLEKQL--YEVLSL---HRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGG 160
Cdd:cd03255 76 LAAFRRRHIGFVFQS--------FNLLPDLtaLENVELpllLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRkLAHRVAVMQNGR 234
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-505 |
8.95e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 180.98 E-value: 8.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSVGFRhqqTVRtVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpS---PPVeylSGDIRFHGESL 78
Cdd:COG1129 1 AEPLLEMRGISKSFG---GVK-ALDGVSLELRPGEVHALLGENGAGKS-TLMKIL----SgvyQPD---SGEILLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 LHASDqtlRGVRGNKIAMIFQEpmvsLNPLHTL----------EKQLYEVLSlHRGMRREAARgeilnCLDRVGIRQAAK 148
Cdd:COG1129 69 RFRSP---RDAQAAGIAIIHQE----LNLVPNLsvaeniflgrEPRRGGLID-WRAMRRRARE-----LLARLGLDIDPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 149 RLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVA 228
Cdd:COG1129 136 TPVG---DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 229 VMQNGRCVeqnyaATLfasPTHPYTQ----------KLLNSEPSGDpvplPEPASTLLDVEQLQVAfpirkgilkrivdh 298
Cdd:COG1129 212 VLRDGRLV-----GTG---PVAELTEdelvrlmvgrELEDLFPKRA----AAPGEVVLEVEGLSVG-------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 nVVVKNISFTLRAGETLGLVGESGSGKSttglALLRLI-----NSQGSIIFDGQPLQNLNRRQllPIRHRI--------- 364
Cdd:COG1129 266 -GVVRDVSFSVRAGEILGIAGLVGAGRT----ELARALfgadpADSGEIRLDGKPVRIRSPRD--AIRAGIayvpedrkg 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 365 QVVFQD----PNSSLnPRLNVLqiieeglrVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARAL 440
Cdd:COG1129 339 EGLVLDlsirENITL-ASLDRL--------SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 441 ILKPSLIILDEPTSSLD---KtvqAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVV 505
Cdd:COG1129 410 ATDPKVLILDEPTRGIDvgaK---AEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-254 |
1.98e-50 |
|
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: 172.86 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPD------SGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 HASDQTLRGVRgNKIAMIFQEPMV--SLNPLHTLEKQLYEvlslHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQL 157
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQGGALfdSLTVFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---MPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALD-VSVqAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*...
gi 16130118 237 EQNYAATLFASpTHPYTQ 254
Cdd:COG1127 222 AEGTPEELLAS-DDPWVR 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
300-504 |
3.84e-50 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 171.52 E-value: 3.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHR-IQVVFQDPNs 373
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSFN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 sLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03255 93 -LLPDLTALENVELPLLLAG--VPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRaLCHQVIILRQGEV 504
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
302-526 |
1.59e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 173.83 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPN--SS 374
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKST----LIRCINllerpTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNllSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNV---LQIieEGLrvhqptlSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK11153 97 RTVFDNValpLEL--AGT-------PKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-267 |
9.27e-49 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 171.52 E-value: 9.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpSPPVEYLSGD-IRFHGESLLHASD 83
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV--TKDNWRVTADrMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVL--SLHRG---MRREAARGEILNCLDRVGIRQAAKRLTDYPHQLS 158
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGrwwQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270
....*....|....*....|....*....|
gi 16130118 239 NYAATLFASPTHPYTQKLLNSEPS-GDPVP 267
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDfGSAMP 270
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
292-508 |
2.03e-48 |
|
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: 166.54 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNrrqllPIRHRIQV 366
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTT----LLRLIAglerpDSGEILIDGRDVTGVP-----PERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPnsSLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPSL 446
Cdd:cd03259 77 VFQDY--ALFPHLTVAENIAFGLKLR--GVPKAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
272-518 |
3.26e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 170.66 E-value: 3.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 272 ASTLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDG 346
Cdd:COG3842 2 AMPALELENVSKRY-----------GDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAgfetpDSGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 347 QPLQNL--NRRqllpirhRIQVVFQDPnsSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPA 424
Cdd:COG3842 67 RDVTGLppEKR-------NVGMVFQDY--ALFPHLTVAENVAFGLRMRG--VPKAEIRARVAELLELVGLE-GLADRYPH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
250
....*....|....
gi 16130118 505 VEQGPCARVFATPQ 518
Cdd:COG3842 215 EQVGTPEEIYERPA 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-258 |
4.01e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 166.71 E-value: 4.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppVEYLSGDIRFHGESLlHASDQ 84
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLL----EEPDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGnKIAMIFQE----P-M-----VSLNPLHtlekqlyevlslHRGMRREAARGEILNCLDRVGIRQAAKRltdYP 154
Cdd:COG1126 71 DINKLRR-KVGMVFQQfnlfPhLtvlenVTLAPIK------------VKKMSKAEAEERAMELLERVGLADKADA---YP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:COG1126 135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
250 260
....*....|....*....|....
gi 16130118 235 CVEQNYAATLFASPTHPYTQKLLN 258
Cdd:COG1126 214 IVEEGPPEEFFENPQHERTRAFLS 237
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
275-526 |
2.16e-47 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 167.78 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSII-----FDGQPL 349
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVK-------AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTadrfrWNGIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 350 QNLN---RRQLlpIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLS----AAQREQQVIAVMHEVGL-DPETRHR 421
Cdd:COG4170 76 LKLSpreRRKI--IGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIkDHKDIMN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 422 -YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILR 500
Cdd:COG4170 154 sYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY 233
|
250 260
....*....|....*....|....*.
gi 16130118 501 QGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALL 259
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
297-518 |
2.38e-47 |
|
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: 165.22 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP 371
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKST----LLRALAgllkpSSGEVLLDGRDLASLSRREL---ARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NSSLNprLNVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:COG1120 85 PAPFG--LTVRELVALGRYPHLGLFGRPSAEdrEAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFaTPQ 518
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-TPE 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
300-524 |
3.64e-47 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 165.12 E-value: 3.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIR-HRIQVVFQdpNS 373
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKST----LLRCINrliepTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQ--SF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQG--VPRAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQ 524
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
293-506 |
6.48e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 162.91 E-value: 6.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 293 KRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHRIQVV 367
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQVLVNGQDLSRLKRREIPYLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 368 FQDPNssLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:COG2884 85 FQDFR--LLPDRTVYENVALPLRVT--GKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVE 506
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-248 |
7.60e-47 |
|
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: 163.14 E-value: 7.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLR 87
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT----SGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQ------EPMVSLNPLHTLEkqlyevlslHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGE 161
Cdd:cd03258 79 KAR-RRIGMIFQhfnllsSRTVFENVALPLE---------IAGVPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYA 241
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*..
gi 16130118 242 ATLFASP 248
Cdd:cd03258 226 EEVFANP 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
298-503 |
7.88e-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: 161.20 E-value: 7.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLnRRQLLPIRHRIQVVFQDPN 372
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKST----LLRCIAgleepDSGSILIDGEDLTDL-EDELPPLRRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 ssLNPRLNVLQIIEEGLrvhqptlsaaqreqqviavmhevgldpetrhrypaefSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03229 87 --LFPHLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGE 503
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
301-503 |
8.12e-47 |
|
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: 162.25 E-value: 8.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPNSSL 375
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKST----LLRLLNgllgpTSGEVLVDGKDLTKLSLKEL---RRKVGLVFQNPDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 -NPRlnvlqIIEE---GLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03225 89 fGPT-----VEEEvafGLENLG--LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGE 503
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-515 |
8.87e-47 |
|
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: 170.75 E-value: 8.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSVTaLSILRLLPSppVEYLSGDIRFH----------- 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQ--YEPTSGRIIYHvalcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 75 ------------GESL-------LHASDQTLRGVRgNKIAMIFQ-------EPMVSLNPLHTLEKQLYEVlslhrgmrrE 128
Cdd:TIGR03269 74 rpskvgepcpvcGGTLepeevdfWNLSDKLRRRIR-KRIAIMLQrtfalygDDTVLDNVLEALEEIGYEG---------K 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 129 AARGEILNCLDRVgirQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNM 208
Cdd:TIGR03269 144 EAVGRAVDLIEMV---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 209 GMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFAspthpytqKLLNSepsgdpVPLPEPAstlldvEQLQVAFPIR 288
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA--------VFMEG------VSEVEKE------CEVEVGEPII 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 K--GILKRI--VDHNVV--VKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIF-------DGQPLQNLNR 354
Cdd:TIGR03269 281 KvrNVSKRYisVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVrvgdewvDMTKPGPDGR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 355 RQLLPIrhrIQVVFQDpnSSLNPRLNVLQIIEEGLRVHQPTLSAAQReqqVIAVMHEVGLDPETR----HRYPAEFSGGQ 430
Cdd:TIGR03269 361 GRAKRY---IGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMK---AVITLKMVGFDEEKAeeilDKYPDELSEGE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL-TLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQ-TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 16130118 510 CARVFA 515
Cdd:TIGR03269 512 PEEIVE 517
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-238 |
2.63e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.77 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLHASD 83
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIRMLlgLLRPT------SGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRgvrgnKIAMIFQEPmvSLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQ 163
Cdd:COG1131 70 EVRR-----RIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVG---TLSGGMKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-507 |
2.87e-46 |
|
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: 161.10 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 276 LDVEQLQVAFPIRKGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQ 350
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVT-------ALEDISLSVEEGEFVALVGPSGCGKST----LLRIIAglerpTSGEVLVDGEPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 351 NLNRRqllpirhrIQVVFQDPnsSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQ 430
Cdd:cd03293 70 GPGPD--------RGYVFQQD--ALLPWLTVLDNVALGLELQG--VPKAEARERAEELLELVGLS-GFENAYPHQLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIIL--RQGEVVEQ 507
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
3.47e-46 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 162.02 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVRtvvnDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGES- 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCR----DVSFDLYPGEVLGIVGESGSGKT-TLLNALsaRLAPD------AGEVHYRMRDg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 78 ----LLHASDQTLRGVRGNKIAMIFQEPMVSLNPLHT----LEKQLYEVLSLHRGMRREAArgeiLNCLDRVGIrqAAKR 149
Cdd:PRK11701 71 qlrdLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSaggnIGERLMAVGARHYGDIRATA----GDWLERVEI--DAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 150 LTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAV 229
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|
gi 16130118 230 MQNGRCVEQNYAATLFASPTHPYTQKLLNS 259
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
294-527 |
3.71e-46 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 162.18 E-value: 3.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 294 RIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-----NSQGSIIFDGQPLQNlnrrQLLPIRHrIQVVF 368
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAP----CALRGRK-IATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 369 QDPNSSLNPRLNVLQIIEEGLRVhqptLSAAQREQQVIAVMHEVGLDPETR--HRYPAEFSGGQRQRIAIARALILKPSL 446
Cdd:PRK10418 86 QNPRSAFNPLHTMHTHARETCLA----LGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
.
gi 16130118 527 A 527
Cdd:PRK10418 242 S 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-233 |
6.34e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 161.41 E-value: 6.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQ--TLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRF 73
Cdd:COG1116 1 MSAaaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIaglekPT------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 74 HGESLLHAsdqtlrgvrGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdY 153
Cdd:COG1116 71 DGKPVTGP---------GPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDA---Y 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLS-IVRkLAHRVAVMQN 232
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLSA 214
|
.
gi 16130118 233 G 233
Cdd:COG1116 215 R 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
271-528 |
8.39e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 161.03 E-value: 8.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 271 PASTLLDVEQLQVAFPIRKGilkrivdHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFD 345
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIaglekPTSGEVLVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 346 GQPLQNLNRRqllpirhrIQVVFQDPnsSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAE 425
Cdd:COG1116 72 GKPVTGPGPD--------RGVVFQEP--ALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGLA-GFEDAYPHQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQ--AQILTLLKSLQQKHQLAYLFISHDLH--VvrALCHQVIIL-- 499
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALD--ALtrERLQDELLRLWQETGKTVLFVTHDVDeaV--FLADRVVVLsa 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130118 500 RQGEVVEQ----GPCAR---VFATPQ-QEYTRQLLAL 528
Cdd:COG1116 215 RPGRIVEEidvdLPRPRdreLRTSPEfAALRAEILDL 251
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-246 |
1.31e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 159.81 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVeylSGDIRFHGESLlhaSDQT 85
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK--PT---SGEVLVDGKDI---TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRgNKIAMIFQEPmvslnplhtlEKQLYE--VLS------LHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQL 157
Cdd:COG1122 70 LRELR-RKVGLVFQNP----------DDQLFAptVEEdvafgpENLGLPREEIRERVEEALELVGLEHLADR---PPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
....*....
gi 16130118 238 QNYAATLFA 246
Cdd:COG1122 215 DGTPREVFS 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
300-509 |
1.31e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.84 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLqnlnRRQLLPIRHRIQVVFQDPNssLNPR 378
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDV----ARDPAEVRRRIGYVPQEPA--LYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:COG1131 88 LTVRENLRFFARLYG--LPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 459 TVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:COG1131 165 EARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-252 |
2.20e-45 |
|
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: 159.20 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPveyLSGDIRFHGESLLHASDQTLR 87
Cdd:cd03261 3 LRGLTKSFGG----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--P---DSGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQEPMV--SLNPLHTLEKQLYEVLSLHRGMRREAARgeilNCLDRVGIRQAAKRltdYPHQLSGGERQRV 165
Cdd:cd03261 74 RLR-RRMGMLFQSGALfdSLTVFENVAFPLREHTRLSEEEIREIVL----EKLEAVGLRGAEDL---YPAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLF 245
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
....*..
gi 16130118 246 ASpTHPY 252
Cdd:cd03261 226 AS-DDPL 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
301-509 |
4.52e-45 |
|
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: 168.86 E-value: 4.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---N 372
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKST----LLKLLlglyePTSGRILIDGIDLRQIDPASL---RRQIGVVLQDVflfS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSlnprlnvlqiIEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDPETRHRyP-----------AEFSGGQRQRIAIARALI 441
Cdd:COG2274 563 GT----------IRENITLGDPDAT----DEEIIEAARLAGLHDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRaLCHQVIILRQGEVVEQGP 509
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIR-LADRIIVLDKGRIVEDGT 692
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
289-513 |
4.84e-45 |
|
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: 158.50 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHR 363
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKST----LLRCLNglvepTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTLSA------AQREQQVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAIA 437
Cdd:cd03256 80 IGMIFQQFN--LIERLSVLENVLSGRLGRRSTWRSlfglfpKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 438 RALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARV 513
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-509 |
1.71e-44 |
|
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: 157.07 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKgilkrivdhnVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPL 349
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----------QALKNINLNINPGEFVAIIGPSGAGKST----LLRCINrlvepSSGSILLEGTDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 350 QNLNRRQLLPIRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQPT----LSAAQREQQVIAV--MHEVGLDpETRHRYP 423
Cdd:TIGR02315 67 TKLRGKKLRKLRRRIGMIFQHYN--LIERLTVLENVLHGRLGYKPTwrslLGRFSEEDKERALsaLERVGLA-DKAYQRA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGE 503
Cdd:TIGR02315 144 DQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
....*.
gi 16130118 504 VVEQGP 509
Cdd:TIGR02315 224 IVFDGA 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-274 |
1.73e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 157.93 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQQTVR-----TVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPveylSGDIRFHGESL 78
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLA-RLLVGLESPS----QGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 LHASDQTLRGVRGNkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQA-AKRLtdyPHQL 157
Cdd:PRK10419 77 AKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKR---PPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130118 238 QNyAATLFASPTHPYTQKLLNSEPSGDPVPLPEPAST 274
Cdd:PRK10419 233 TQ-PVGDKLTFSSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
289-527 |
4.99e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 156.50 E-value: 4.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVvKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQP----------LQNLN 353
Cdd:COG4598 12 RDLHKSFGDLEVL-KGVSLTARKGDVISIIGSSGSGKST----FLRCINlletpDSGEIRVGGEEirlkpdrdgeLVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 354 RRQLLPIRHRIQVVFQDPNssLNPRLNVLQ-IIEEGLRVHQptLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQ 432
Cdd:COG4598 87 RRQLQRIRTRLGMVFQSFN--LWSHMTVLEnVIEAPVHVLG--RPKAEAIERAEALLAKVGL-ADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCAR 512
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
250
....*....|....*
gi 16130118 513 VFATPQQEYTRQLLA 527
Cdd:COG4598 241 VFGNPKSERLRQFLS 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-519 |
5.18e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 162.89 E-value: 5.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 26 NDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLHASDqtlRGVRGNKIAMIFQEPMv 103
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKS-TLMKILygLYQPD------SGEILIDGKPVRIRSP---RDAIALGIGMVHQHFM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 sLNPLHTLekqlYE--VLSLHRG----MRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPEL 177
Cdd:COG3845 91 -LVPNLTV----AEniVLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKV---EDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 178 LIADEPTTALdvSVQ--AQILQLLREL--QGelnMGMLFITHNLSIVRKLAHRVAVMQNGRCVeqnyaATLFASPThpyt 253
Cdd:COG3845 163 LILDEPTAVL--TPQeaDELFEILRRLaaEG---KSIIFITHKLREVMAIADRVTVLRRGKVV-----GTVDTAET---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 254 qkllnSEPS------GDPVPLP------EPASTLLDVEQLQVAFPirkgilkrivDHNVVVKNISFTLRAGETLGLVGES 321
Cdd:COG3845 229 -----SEEElaelmvGREVLLRvekapaEPGEVVLEVENLSVRDD----------RGVPALKDVSLEVRAGEILGIAGVA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 322 GSGKSTTGLAL--LRLINSqGSIIFDGQPLQNLNRRQLlpIRHRIQVVFQDPNSS-LNPRLNVlqiiEEGL---RVHQPT 395
Cdd:COG3845 294 GNGQSELAEALagLRPPAS-GSIRLDGEDITGLSPRER--RRLGVAYIPEDRLGRgLVPDMSV----AENLilgRYRRPP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 396 LS---------AAQREQQVIAVMHEVGLDPETRHRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILT 466
Cdd:COG3845 367 FSrggfldrkaIRAFAEELIEEFDVRTPGPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQ 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 467 LLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVeqGPCARVFATPQQ 519
Cdd:COG3845 444 RLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV--GEVPAAEATREE 493
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
292-504 |
9.54e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.20 E-value: 9.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQV 366
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKST----LLRALAdldppTSGEIYLDGKPLSAMPPPEW---RRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPnsslnpRL---NVLQIIEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:COG4619 79 VPQEP------ALwggTVRDNLPFPFQLRERKFD----RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-236 |
1.25e-43 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 155.20 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTAL-SILRLLPsppveYLSGDIRFHGESLLHASd 83
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLK-----PSSGEVLLDGRDLASLS- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 qtlRGVRGNKIAMIFQEPMVSLnPLHtlekqLYEVLSL----HRG-MRREAARGE--ILNCLDRVGIRQAAKRLTDyphQ 156
Cdd:COG1120 70 ---RRELARRIAYVPQEPPAPF-GLT-----VRELVALgrypHLGlFGRPSAEDReaVEEALERTGLEHLADRPVD---E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
2.47e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTAL-SILRLLPspPVeylSGDIRFHGESLl 79
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP--PT---SGTVRLFGKPP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 hasdqtlrGVRGNKIAMIFQEPMVSLN-PLHtlekqLYEVLSL----HRGMRR---EAARGEILNCLDRVGIRQAAKRLT 151
Cdd:COG1121 71 --------RRARRRIGYVPQRAEVDWDfPIT-----VRDVVLMgrygRRGLFRrpsRADREAVDEALERVGLEDLADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:COG1121 138 G---ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN 213
|
....
gi 16130118 232 NGRC 235
Cdd:COG1121 214 RGLV 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-235 |
3.35e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 153.01 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpveyLSGDIRFHGESLlhasdqt 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIAGLERP----TSGEVLVDGEPV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 lRGVrGNKIAMIFQEPmvSLNPLHTLEKQLyeVLSL-HRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164
Cdd:cd03293 69 -TGP-GPDRGYVFQQD--ALLPWLTVLDNV--ALGLeLQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRC 235
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
3.74e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 153.67 E-value: 3.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTAL-SILRLL-PSppveylSGDIRFHGESLLHA 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVePT------SGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLRGVRGnKIAMIFQEpmvslnplHTLEKQLYeVL-----------SLHRGMRREAARGEI---LNCLDRVGIRQAA 147
Cdd:COG3638 71 RGRALRRLRR-RIGMIFQQ--------FNLVPRLS-VLtnvlagrlgrtSTWRSLLGLFPPEDReraLEALERVGLADKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 148 KRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRV 227
Cdd:COG3638 141 YQRAD---QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
....*....
gi 16130118 228 AVMQNGRCV 236
Cdd:COG3638 218 IGLRDGRVV 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
297-503 |
4.69e-43 |
|
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: 151.00 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---N 372
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESL---RKNIAYVPQDPflfS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLnpRLNVLqiieeglrvhqptlsaaqreqqviavmhevgldpetrhrypaefSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03228 90 GTI--RENIL--------------------------------------------SGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRaLCHQVIILRQGE 503
Cdd:cd03228 124 TSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-287 |
4.77e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 156.11 E-value: 4.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLR 87
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPT----SGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQEpmvsLNPLHTleKQLYEVLSLH---RGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164
Cdd:PRK11153 79 KAR-RQIGMIFQH----FNLLSS--RTVFDNVALPlelAGTPKAEIKARVTELLELVGLSDKADR---YPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16130118 245 FASPTHPYTQKLLNsepSGDPVPLPEPASTLLDVEQLQVAFPI 287
Cdd:PRK11153 229 FSHPKHPLTREFIQ---STLHLDLPEDYLARLQAEPTTGSGPL 268
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
1.91e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 154.87 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLL-----PSppveylSGDIRFHG 75
Cdd:COG3842 1 MAMPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMIagfetPD------SGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 76 ESLLH-ASDQtlrgvRGnkIAMIFQEPmvSLNPLHT--------LEkqlyevlslHRGMRREAARGEILNCLDRVGIRQA 146
Cdd:COG3842 67 RDVTGlPPEK-----RN--VGMVFQDY--ALFPHLTvaenvafgLR---------MRGVPKAEIRARVAELLELVGLEGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 147 AKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHN----LSivrk 222
Cdd:COG3842 129 ADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA---- 201
|
250 260 270
....*....|....*....|....*....|
gi 16130118 223 LAHRVAVMQNGRCVEQNYAATLFASPTHPY 252
Cdd:COG3842 202 LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
299-504 |
2.98e-42 |
|
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: 149.99 E-value: 2.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqNLNRRQLLPIRHRIQVVFQDPNs 373
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleepDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQFN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 sLNPRLNVLQIIEEGLR-VHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03262 87 -LFPHLTVLENITLAPIkVKG--MSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGM-TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
303-518 |
3.93e-42 |
|
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: 151.84 E-value: 3.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSslnp 377
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKST----LIQHLNgllkpTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEH---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 rlnvlQIIEE--------GLRvhQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:TIGR04521 94 -----QLFEEtvykdiafGPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
299-520 |
5.70e-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: 150.18 E-value: 5.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-----QGSIIFDGQPLQNLNrrqllPIRHRIQVVFQdpNS 373
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSV----LLETIAGfikpdSGKILLNGKDITNLP-----PEKRDISYVPQ--NY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKR--KVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQE 520
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
271-529 |
7.39e-42 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 150.46 E-value: 7.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 271 PASTLLDVEQLQVAFPIRKGIlkrivdhnvvvKNISFTLRAGETLGLVGESGSGKSTTgLALL--RLINSQGSIIFDGQ- 347
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGC-----------RDVSFDLYPGEVLGIVGESGSGKTTL-LNALsaRLAPDAGEVHYRMRd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 348 ----PLQNLN---RRQLLpiRHRIQVVFQDPNSSLnpRLNVlqiiEEGLRVHQPTLSAAQRE-----QQVIAVMHEVGLD 415
Cdd:PRK11701 70 gqlrDLYALSeaeRRRLL--RTEWGFVHQHPRDGL--RMQV----SAGGNIGERLMAVGARHygdirATAGDWLERVEID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 416 PETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQ 495
Cdd:PRK11701 142 AARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHR 221
|
250 260 270
....*....|....*....|....*....|....
gi 16130118 496 VIILRQGEVVEQGPCARVFATPQQEYTrQLLALS 529
Cdd:PRK11701 222 LLVMKQGRVVESGLTDQVLDDPQHPYT-QLLVSS 254
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-234 |
1.01e-41 |
|
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: 148.77 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESLLHASDQTLR 87
Cdd:cd03225 2 LKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-----TSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GvrgnKIAMIFQEPmvslnplhtlEKQLY------EVLS--LHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSG 159
Cdd:cd03225 75 R----KVGLVFQNP----------DDQFFgptveeEVAFglENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
297-508 |
1.22e-41 |
|
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: 149.62 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRqllpIRHRIQVVFQDP 371
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTT----LLRMLagllkPDSGSILIDGEDVRKEPRE----ARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NssLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:COG4555 84 G--LYDRLTVRENIRYFAELYG--LFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 452 PTSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:COG4555 159 PTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
271-514 |
1.62e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.08 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 271 PASTLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFD 345
Cdd:COG1121 2 MMMPAIELENLTVSY-----------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKAIlgllpPTSGTVRLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 346 GQPLQNLnrrqllpiRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQP---TLSAAQREQqVIAVMHEVGLDpETRHRY 422
Cdd:COG1121 67 GKPPRRA--------RRRIGYVPQRAEVDWDFPITVRDVVLMGRYGRRGlfrRPSRADREA-VDEALERVGLE-DLADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQkHQLAYLFISHDLHVVRALCHQVIILRQG 502
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
250
....*....|..
gi 16130118 503 eVVEQGPCARVF 514
Cdd:COG1121 216 -LVAHGPPEEVL 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-259 |
2.14e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 149.55 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFR------HQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLpSPPVEYLSGDIRFHGE 76
Cdd:PRK15112 2 ETLLEVRNLSKTFRyrtgwfRRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLA----KML-AGMIEPTSGELLIDDH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 77 SLlHASDQTLRGVRgnkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRqaAKRLTDYPHQ 156
Cdd:PRK15112 76 PL-HFGDYSYRSQR---IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLL--PDHASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 16130118 237 EQNYAATLFASPTHPYTQKLLNS 259
Cdd:PRK15112 230 ERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
302-454 |
3.14e-41 |
|
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: 145.10 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPNssLN 376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKST----LLKLIAgllspTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQ--LF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMHEVGL--DPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:pfam00005 72 PRLTVRENLRLGLLL--KGLSKREKDARAEEALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 16130118 454 S 454
Cdd:pfam00005 150 A 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
301-526 |
3.64e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 151.45 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqNLNrrqlLPIRHR-IQVVFQDPnsS 374
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAgletpDSGRIVLNGRDL-FTN----LPPRERrVGFVFQHY--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:COG1118 86 LFPHMTVAENIAFGLRVRPP--SKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
254-508 |
6.50e-41 |
|
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: 155.30 E-value: 6.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 254 QKLLNSEPSGDP---VPLPEPASTLLDVEQLQVAFPirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGL 330
Cdd:COG4988 312 FALLDAPEPAAPagtAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 331 ALLRLI-NSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSlnprlnvlqiIEEGLRVHQPTLSaaqrEQQVI 406
Cdd:COG4988 382 LLLGFLpPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPylfAGT----------IRENLRLGRPDAS----DEELE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 407 AVMHEVGLDPETRhRYP-----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKH 475
Cdd:COG4988 445 AALEAAGLDEFVA-ALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR 523
|
250 260 270
....*....|....*....|....*....|...
gi 16130118 476 QLayLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:COG4988 524 TV--ILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
297-521 |
8.84e-41 |
|
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: 147.00 E-value: 8.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNL--NRRQllpirhrIQVVFQ 369
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIAgfetpTSGEILLDGKDITNLppHKRP-------VNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 370 dpNSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:cd03300 80 --NYALFPHLTVFENIAFGLRLKK--LPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGpcarvfaTPQQEY 521
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG-------TPEEIY 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
304-526 |
1.55e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.05 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqnlnrRQLLPIRHRIQVVFQDPNssLNPR 378
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKST----LLNLIAgflppDSGRILWNGQDL-----TALPPAERPVSMLFQENN--LFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGLRvhqPT--LSAAQReQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:COG3840 86 LTVAQNIGLGLR---PGlkLTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 457 DKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
2.00e-40 |
|
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: 146.04 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLH 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPT----SGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLRGVRGNKIAMIFQEPMVsLNPLHTLEkqlYEVLSLH-RGMRREAARGEILncLDRVGIrqaAKRLTDYPHQLSG 159
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSFQL-LPTLTALE---NVMLPLElAGRRDARARARAL--LERVGL---GHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKlAHRVAVMQNGRCVE 237
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-506 |
2.84e-40 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 152.53 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHgesllhasdqt 85
Cdd:COG0488 1 LENLSKSFGG----RPLLDDVSLSINPGDRIGLVGRNGAGKS-TLLKILagELEPD------SGEVSIP----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 lrgvRGNKIAMIFQEP------------MVSLNPLHTLEKQLYEVLSLHRGMRREAAR-GEILNCLDRVG-------IRQ 145
Cdd:COG0488 59 ----KGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERlAELQEEFEALGgweaearAEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 146 AAKRL--TDYPHQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAqiL-QLLRELQGelnmGMLFITHN 216
Cdd:COG0488 135 ILSGLgfPEEDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW--LeEFLKNYPG----TVLVVSHD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 217 LSIVRKLAHRVAVMQNGRCV---------------------------------EQNYAATLFASPTHpYTQ--------- 254
Cdd:COG0488 209 RYFLDRVATRILELDRGKLTlypgnysayleqraerleqeaaayakqqkkiakEEEFIRRFRAKARK-AKQaqsrikale 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 255 KLLNSEP--SGDPVPL-----PEPASTLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKST 327
Cdd:COG0488 288 KLEREEPprRDKTVEIrfpppERLGKKVLELEGLSKSY-----------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKST 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 328 tglaLLRLIN-----SQGSIIfdgqplqnlnrrqllpIRHRIQVVF--QDpNSSLNPRLNVLQIIEEGlrvhqptlSAAQ 400
Cdd:COG0488 357 ----LLKLLAgelepDSGTVK----------------LGETVKIGYfdQH-QEELDPDKTVLDELRDG--------APGG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 401 REQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAqiltLLKSLQQkhqlaY 479
Cdd:COG0488 408 TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDiETLEA----LEEALDD-----F 478
|
570 580 590
....*....|....*....|....*....|.
gi 16130118 480 ----LFISHDLHVVRALCHQVIILRQGEVVE 506
Cdd:COG0488 479 pgtvLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-237 |
3.81e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.81 E-value: 3.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLHASDQTLRGVRgNKIAM 96
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLygeerPT------SGQVLVNGQDLSRLKRREIPYLR-RRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 97 IFQEpmvslnplHTL--EKQLYE--VLSLH-RGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMAL 171
Cdd:COG2884 84 VFQD--------FRLlpDRTVYEnvALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKA---LPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQgelNMGM--LFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEIN---RRGTtvLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
289-526 |
5.58e-40 |
|
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: 145.14 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTglalLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHR 363
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINrliepTSGEIFIDGEDIREQDPVEL---RRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQdpNSSLNPRLNVLQIIeeGLrvhQPTL---SAAQREQQVIAVMHEVGLDPET-RHRYPAEFSGGQRQRIAIARA 439
Cdd:cd03295 77 IGYVIQ--QIGLFPHMTVEENI--AL---VPKLlkwPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 440 LILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQ 519
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*..
gi 16130118 520 EYTRQLL 526
Cdd:cd03295 230 DFVAEFV 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-237 |
8.57e-40 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 143.86 E-value: 8.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPPVEYLSGDIRFHGESLLhASDQ 84
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKS-TLLRLLnRLNDLIPGAPDEGEVLLDGKDIY-DLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRgNKIAMIFQEPmvslNPLHtleKQLYEVLSL---HRGMRREAARGEI-LNCLDRVGIRQAAKRLTDyPHQLSGG 160
Cdd:cd03260 75 DVLELR-RRVGMVFQKP----NPFP---GSIYDNVAYglrLHGIKLKEELDERvEEALRKAALWDEVKDRLH-ALGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElnMGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
289-526 |
1.54e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 145.62 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTglalLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHR 363
Cdd:COG1125 5 ENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT----LRMINrliepTSGRILIDGEDIRDLDPVEL---RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQdpNSSLNPRLNVLQIIEeglRVhqPTL---SAAQREQQVIAVMHEVGLDPET-RHRYPAEFSGGQRQRIAIARA 439
Cdd:COG1125 78 IGYVIQ--QIGLFPHMTVAENIA---TV--PRLlgwDKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 440 LILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQ 519
Cdd:COG1125 151 LAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPAN 230
|
....*..
gi 16130118 520 EYTRQLL 526
Cdd:COG1125 231 DFVADFV 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-234 |
1.97e-39 |
|
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: 142.67 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHaSDQTLR 87
Cdd:cd03262 3 IKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEEPD----SGTIIIDGLKLTD-DKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMI 167
Cdd:cd03262 73 ELR-QKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
304-517 |
2.38e-39 |
|
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: 146.78 E-value: 2.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQLLPI-RHRIQVVFQDPnsSLNP 377
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTT----LLRAIaglerPDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQEA--RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RLNVLQIIEEGLRVHQPTLSAAQREQqVIAVMhevGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDE-VVELL---GIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 458 KTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-237 |
2.88e-39 |
|
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: 142.49 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQ 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPT----SGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGNKIAMIFQ--EPMVSLNPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIRqaaKRLTDYPHQLSGGER 162
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKSVKEAKERAYEMLEKVGLE---HRINHRPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAhRVAVMQNGRCVE 237
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEMKDGQLFN 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
3.04e-39 |
|
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: 141.03 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 7 AIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTAL-SILRLLPSppveyLSGDIRFHGESLLHASdqt 85
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKP-----SSGEILLDGKDLASLS--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 lrgvrgnkiamifqepmvslnplhtlekqlyevlslhrgmRREAAR--GEILNCLDRVGIRQAAKRLTDyphQLSGGERQ 163
Cdd:cd03214 68 ----------------------------------------PKELARkiAYVPQALELLGLAHLADRPFN---ELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
292-504 |
3.12e-39 |
|
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: 140.61 E-value: 3.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLqnlnRRQLLPIRHRIQV 366
Cdd:cd03230 6 LSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTT----LIKIIlgllkPDSGEIKVLGKDI----KKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPnsSLNPRLNVLQIIeeglrvhqptlsaaqreqqviavmhevgldpetrhrypaEFSGGQRQRIAIARALILKPSL 446
Cdd:cd03230 78 LPEEP--SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-237 |
3.24e-39 |
|
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: 141.89 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLH 80
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIaglerPD------SGEILIDGRDVTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 asdqtlRGVRGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGG 160
Cdd:cd03259 67 ------VPPERRNIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
4.51e-39 |
|
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: 140.23 E-value: 4.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLHASD 83
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKT-TLIKIIlgLLKPD------SGEIKVLGKDIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRgvrgnKIAMIFQEPMvslnplhtlekqLYEVLSLHrgmrreaargEILncldrvgirqaakrltdyphQLSGGERQ 163
Cdd:cd03230 70 EVKR-----RIGYLPEEPS------------LYENLTVR----------ENL--------------------KLSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
301-515 |
7.39e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 142.57 E-value: 7.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGqpLQNLNRRQLLPIRHRIQVVFQDPNSSL 375
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKST----LAKLLNglllpTSGKVTVDG--LDTLDEENLWEIRKKVGMVFQNPDNQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprlnVLQIIEE----GLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:TIGR04520 91 -----VGATVEDdvafGLENLG--VPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:TIGR04520 163 ATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
297-499 |
2.16e-38 |
|
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: 139.59 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNlnrrqllpIRHRIQVVFQDP 371
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKST----LLKAIlgllkPTSGSIRVFGKPLEK--------ERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NSSLNPRLNVLQIIEEGL---RVHQPTLSAAQREQqVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:cd03235 78 SIDRDFPISVRDVVLMGLyghKGLFRRLSKADKAK-VDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 449 LDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIIL 499
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
292-517 |
2.24e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.67 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLnrrqllPIRHR-IQ 365
Cdd:COG3839 9 VSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAgledpTSGEILIGGRDVTDL------PPKDRnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 366 VVFQDPnsSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPS 445
Cdd:COG3839 79 MVFQSY--ALYPHMTVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 446 LIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
287-508 |
2.29e-38 |
|
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: 139.74 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 287 IRKGILKRIVDHNVvvkNISFTLRaGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIR 361
Cdd:cd03297 2 LCVDIEKRLPDFTL---KIDFDLN-EEVTGIFGASGAGKST----LLRCIAglekpDGGTIVLNGTVLFDSRKKINLPPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 362 HR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVHQPtlsaAQREQQVIAVMHEVGLDPETRhRYPAEFSGGQRQRIAIARAL 440
Cdd:cd03297 74 QRkIGLVFQ--QYALFPHLNVRENLAFGLKRKRN----REDRISVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 441 ILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-252 |
2.95e-38 |
|
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: 141.24 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 7 AIENLSVGFRHQQTVR----TV-VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHA 81
Cdd:cd03294 17 AFKLLAKGKSKEEILKktgqTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL-----IEPTSGKVLIDGQDIAAM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLRGVRGNKIAMIFQEpmVSLNPLHT-LEKQLY--EVLSLHRGMRREAARgeilNCLDRVGIRQAAKRltdYPHQLS 158
Cdd:cd03294 92 SRKELRELRRKKISMVFQS--FALLPHRTvLENVAFglEVQGVPRAEREERAA----EALELVGLEGWEHK---YPDELS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQV 242
|
250
....*....|....
gi 16130118 239 NYAATLFASPTHPY 252
Cdd:cd03294 243 GTPEEILTNPANDY 256
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
267-528 |
3.31e-38 |
|
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: 147.61 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 267 PLPEPASTLLDVEQLQVAFPIRKGIlkrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFD 345
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRP---------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpQSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 346 GQPLQNLNRRQLlpiRHRIQVVFQDP---NSSlnprlnvlqiIEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDP------ 416
Cdd:COG4987 396 GVDLRDLDEDDL---RRRIAVVPQRPhlfDTT----------LRENLRLARPDAT----DEELWAALERVGLGDwlaalp 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 417 ---ETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL-TLLKSLQQKhqlAYLFISHDLHVVrA 491
Cdd:COG4987 459 dglDTWlGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGR---TVLLITHRLAGL-E 534
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130118 492 LCHQVIILRQGEVVEQGPCARVFAtpQQEYTRQLLAL 528
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQR 569
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
296-508 |
3.61e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 137.95 E-value: 3.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 296 VDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQd 370
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKST----LLKTLAgllkpSSGEILLDGKDLASLSPKEL---ARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 371 pnsslnprlnvlqiieeglrvhqptlsaaqreqqviaVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:cd03214 81 -------------------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
301-509 |
5.12e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.23 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---N 372
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKST----LVNLLLrfydpTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTflfS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSlnprlnvlqiIEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDPETRhRYP-----------AEFSGGQRQRIAIARALI 441
Cdd:COG1132 428 GT----------IRENIRYGRPDAT----DEEVEEAAKAAQAHEFIE-ALPdgydtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRAlCHQVIILRQGEVVEQGP 509
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTT--IVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
303-529 |
8.12e-38 |
|
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: 139.58 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKSTTGLALL-RLINSQGSIIF---DGQP-----LQNLNRRQLLpiRHRIQVVFQDPNS 373
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYimrSGAElelyqLSEAERRRLM--RTEWGFVHQNPRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLnpRLNVlqiiEEGLRVHQPTLSAAQRE-----QQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:TIGR02323 98 GL--RMRV----SAGANIGERLMAIGARHygnirATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 449 LDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTrQLLAL 528
Cdd:TIGR02323 172 MDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYT-QLLVS 250
|
.
gi 16130118 529 S 529
Cdd:TIGR02323 251 S 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-236 |
1.61e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 138.47 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQT 85
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-----VEPTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGnKIAMIFQEPMVsLNPLHTLEKQLYEVL---SLHRGMRR---EAARGEILNCLDRVGIRQAAKRLTDyphQLSG 159
Cdd:cd03256 73 LRQLRR-QIGMIFQQFNL-IERLSVLENVLSGRLgrrSTWRSLFGlfpKEEKQRALAALERVGLLDKAYQRAD---QLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
269-506 |
1.99e-37 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 137.95 E-value: 1.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 269 PEPASTLLDVEQLQVAFPIRKGILkrivdhnVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSII 343
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGEL-------TILKGISLEVEAGESVAIVGASGSGKST----LLGLLagldrPTSGTVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 344 FDGQPLQNLNRRQLLPIR-HRIQVVFQdpNSSLNPRL----NVLQIIEegLRvhqptlSAAQREQQVIAVMHEVGLDPET 418
Cdd:COG4181 71 LAGQDLFALDEDARARLRaRHVGFVFQ--SFQLLPTLtaleNVMLPLE--LA------GRRDARARARALLERVGLGHRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 419 RHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVII 498
Cdd:COG4181 141 DH-YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLR 218
|
....*...
gi 16130118 499 LRQGEVVE 506
Cdd:COG4181 219 LRAGRLVE 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-230 |
2.41e-37 |
|
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: 136.89 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTAL-SILRLLPSppveyLSGDIRFHGESLlhasdqtl 86
Cdd:cd03235 2 VEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLKP-----TSGSIRVFGKPL-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 rGVRGNKIAMIFQEPMVSLN-PLHTLE---KQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKRLTDyphQLSGGER 162
Cdd:cd03235 64 -EKERKRIGYVPQRRSIDRDfPISVRDvvlMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIG---ELSGGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVM 230
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
3.22e-37 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 135.39 E-value: 3.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLlhASDQT 85
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKS-TLLRCIAGLEEPD----SGSILIDGEDL--TDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGNKIAMIFQEPmvSLNPLhtlekqlyevlslhrgmrreaargeiLNCLDRVGIRqaakrltdyphqLSGGERQRV 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDF--ALFPH--------------------------LTVLENIALG------------LSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
293-527 |
1.22e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 136.64 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 293 KRIVDHNVVvKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQ----------PLQNLNRRQL 357
Cdd:PRK10619 13 KRYGEHEVL-KGVSLQANAGDVISIIGSSGSGKST----FLRCINflekpSEGSIVVNGQtinlvrdkdgQLKVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 358 LPIRHRIQVVFQDPNssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIA 437
Cdd:PRK10619 88 RLLRTRLTMVFQHFN--LWSHMTVLENVMEA-PIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 438 RALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
250
....*....|
gi 16130118 518 QQEYTRQLLA 527
Cdd:PRK10619 244 QSPRLQQFLK 253
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
301-509 |
1.44e-36 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 135.39 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN----------SQGSIIFDGQPLQNLNRRQLLpIRHRIQVVFQD 370
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKST----LLRLLNrlndlipgapDEGEVLLDGKDIYDLDVDVLE-LRRRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 371 PNsslnP-RLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:cd03260 90 PN----PfPGSIYDNVAYGLRLHG-IKLKEELDERVEEALRKAALWDEVkDRLHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 449 LDEPTSSLDKTVQAQILTLLKSLqqKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-260 |
1.84e-36 |
|
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: 135.51 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQT 85
Cdd:cd03295 1 IEFENVTKRYGG---GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL-----IEPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRgvrgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGI--RQAAKRltdYPHQLSGGERQ 163
Cdd:cd03295 73 LR----RKIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLdpAEFADR---YPHELSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAAT 243
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
250
....*....|....*..
gi 16130118 244 LFASPTHPYTQKLLNSE 260
Cdd:cd03295 223 ILRSPANDFVAEFVGAD 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
299-513 |
2.61e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.92 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQllPIRHRIQVVFQDPNs 373
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKST----LMKILSgvyqpDSGEILLDGEPVRFRSPRD--AQAAGIAIIHQELN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 sLNPRLNVLQIIEEGlrvHQPT----LSAAQREQQVIAVMHEVGL--DPETRHRypaEFSGGQRQRIAIARALILKPSLI 447
Cdd:COG1129 90 -LVPNLSVAENIFLG---REPRrgglIDWRAMRRRARELLARLGLdiDPDTPVG---DLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARV 513
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQG-VAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-234 |
3.17e-36 |
|
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: 132.51 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGESLLHASDQT 85
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-----DPTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRgvrgNKIAMIFQEPmvslnplhtlekQLYEvlslhrgmrreaarGEILNCLdrvgirqaakrltdyphqLSGGERQRV 165
Cdd:cd03228 74 LR----KNIAYVPQDP------------FLFS--------------GTIRENI------------------LSGGQRQRI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGR 234
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-238 |
3.24e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 143.05 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLH 80
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRgmrREAARGEILNCLDRVGIRQAAKRLtdyPH----- 155
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFL-------FSGTIRENITLGD---PDATDEEIIEAARLAGLHDFIEAL---PMgydtv 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRkLAHRVAV 229
Cdd:COG2274 605 vgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIV 681
|
....*....
gi 16130118 230 MQNGRCVEQ 238
Cdd:COG2274 682 LDKGRIVED 690
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
298-526 |
3.28e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.84 E-value: 3.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqNLNRRQLLPIRHRIQVVFQDPN 372
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCINkleeiTSGDLIVDGLKV-NDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 ssLNPRLNVLQIIEEGlRVHQPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK09493 88 --LFPHLTALENVMFG-PLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-258 |
3.44e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.88 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVEYLS-GDIRFHGESLLHAS 82
Cdd:PRK11264 2 SAIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAGTIRvGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGER 162
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAA 242
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*.
gi 16130118 243 TLFASPTHPYTQKLLN 258
Cdd:PRK11264 230 ALFADPQQPRTRQFLE 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
299-526 |
3.93e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.88 E-value: 3.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN----------SQGSIIFDGQPLQNLNRRQLLPIRHRIQVVF 368
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTT----LLRCINlleqpeagtiRVGDITIDTARSLSQQKGLIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 369 QDPNssLNPRLNVLQIIEEGLRV--HQPTLSAAQREQQVIAvmhEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPSL 446
Cdd:PRK11264 92 QNFN--LFPHRTVLENIIEGPVIvkGEPKEEATARARELLA---KVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
272-518 |
4.04e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 134.78 E-value: 4.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 272 ASTLLDVEQLQVAFpirKGIlkrivdhnVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDG 346
Cdd:COG0411 1 SDPLLEVRGLTKRF---GGL--------VAVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLITgfyrpTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 347 QPLQNLNRRQLlpIRHRIQVVFQdpNSSLNPRLNVLQ-------------IIEEGLRVHQPTLSAAQREQQVIAVMHEVG 413
Cdd:COG0411 66 RDITGLPPHRI--ARLGIARTFQ--NPRLFPELTVLEnvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 414 LDPEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALC 493
Cdd:COG0411 142 LADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
250 260
....*....|....*....|....*
gi 16130118 494 HQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:COG0411 221 DRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-518 |
4.29e-36 |
|
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: 134.10 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 276 LDVEQLQVAFpirkGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQ 350
Cdd:cd03219 1 LEVRGLTKRF----GGLV-------ALDDVSFSVRPGEIHGLIGPNGAGKTT----LFNLISgflrpTSGSVLFDGEDIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 351 NLNRRQLlpIRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVHQPTLSAAQR--------EQQVIAVMHEVGLDPEtRHRY 422
Cdd:cd03219 66 GLPPHEI--ARLGIGRTFQ--IPRLFPELTVLENVMVAAQARTGSGLLLARarreereaRERAEELLERVGLADL-ADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQG 502
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQG 219
|
250
....*....|....*.
gi 16130118 503 EVVEQGPCARVFATPQ 518
Cdd:cd03219 220 RVIAEGTPDEVRNNPR 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
5.86e-36 |
|
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: 130.85 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLRGvrgnKIAMIFQEPmvS 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKS-TLLKLIAGLLSPT----EGTILLDGQDLTDDERKSLRK----EIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIR-QAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 16130118 184 TT 185
Cdd:pfam00005 149 TA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-256 |
7.43e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 7.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESLlh 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-----AGTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 aSDQTLRGVRgNKIAMIFQEP-------MVSLNPLHTLEKQlyevlslhrGMRREAARGEILNCLDRVGIRQAAKRltdY 153
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPdnqfvgaTVQDDVAFGLENI---------GVPREEMVERVDQALRQVGMEDFLNR---E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKlAHRVAVMQNG 233
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
250 260 270
....*....|....*....|....*....|.
gi 16130118 234 RCVEQNYAATLFASPTH--------PYTQKL 256
Cdd:PRK13635 217 EILEEGTPEEIFKSGHMlqeigldvPFSVKL 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-248 |
7.73e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 7.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESL---LHASDQTLRGVRgNKIAMIFQEpmV 103
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPR----SGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQ--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 SLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK11124 92 NLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 184 TTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNyAATLFASP 248
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQP 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-236 |
9.78e-36 |
|
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: 133.58 E-value: 9.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQ 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-----VEPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRgNKIAMIFQEPMVsLNPLHTLEKQLYEVLSLHRGMRR------EAARGEILNCLDRVGIRQAAKRLTDyphQLS 158
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQHYNL-IERLTVLENVLHGRLGYKPTWRSllgrfsEEDKERALSALERVGLADKAYQRAD---QLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
275-526 |
1.38e-35 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 135.70 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPIRKGILKrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNR 354
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVK-------AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 355 RQLLP------IRHRIQVVFQDPNSSLNPRLNV-LQIIEE----------GLRVHQptlsaaqREQQVIAVMHEVGL-DP 416
Cdd:PRK15093 76 LRLSPrerrklVGHNVSMIFQEPQSCLDPSERVgRQLMQNipgwtykgrwWQRFGW-------RKRRAIELLHRVGIkDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 417 -ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQ 495
Cdd:PRK15093 149 kDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
250 260 270
....*....|....*....|....*....|.
gi 16130118 496 VIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-257 |
1.45e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.57 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 29 SLQIEAGETLALVGESGSGKSvTALSILR--LLPSppveylSGDIRFHGESLLHasdqTLRGVRgnKIAMIFQEpmvslN 106
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS-TLLNLIAgfLPPD------SGRILWNGQDLTA----LPPAER--PVSMLFQE-----N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 107 PL--H-TLEKQLYevLSLHRGMR-REAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:COG3840 81 NLfpHlTVAQNIG--LGLRPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 183 PTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLL 257
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
301-520 |
1.57e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 132.83 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPL---QNLNRRQLLPIRHRIQVVFQDPN 372
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSS----LLRVLNlletpDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 ssLNPRLNVLQ-IIEEGLRVHQPTLSAAQREQQVIavMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:COG4161 93 --LWPHLTVMEnLIEAPCKVLGLSKEQAREKAMKL--LARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCArVFATPQQE 520
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTE 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-504 |
1.75e-35 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 138.91 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFrhqQTVRTVvNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPspPVEYLSGDIRFHGEsLLH 80
Cdd:PRK13549 1 MMEYLLEMKNITKTF---GGVKAL-DNVSLKVRAGEIVSLCGENGAGKS-TLMKVLSGVY--PHGTYEGEIIFEGE-ELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 AsdQTLRGVRGNKIAMIFQEPMvslnplhtLEKQLYEVLSLHRGmrREAARGEILNcLDRVGIRqAAKRLTDY-----PH 155
Cdd:PRK13549 73 A--SNIRDTERAGIAIIHQELA--------LVKELSVLENIFLG--NEITPGGIMD-YDAMYLR-AQKLLAQLkldinPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 ----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:PRK13549 139 tpvgNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 232 NGRCVEQNYAATLfaSPTHPYTQ-------KLLNSEPSgdpvplpEPASTLLDVEQLQVAFPIRKGIlKRivdhnvvVKN 304
Cdd:PRK13549 218 DGRHIGTRPAAGM--TEDDIITMmvgreltALYPREPH-------TIGEVILEVRNLTAWDPVNPHI-KR-------VDD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 305 ISFTLRAGETLGLVGESGSGKSTTGLALL-----RlinSQGSIIFDGQPLQNLNRRQllPIRHRIQVVFQD-------PN 372
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgR---WEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDrkrdgivPV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSL--NPRLNVLQIIEEGLRVHQPT-LSAAQREqqvIAVMHEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK13549 356 MGVgkNITLAALDRFTGGSRIDDAAeLKTILES---IQRLKVKTASPELA---IARLSGGNQQKAVLAKCLLLNPKILIL 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-257 |
2.02e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.66 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESL-- 78
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNGRDLft 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 -LHASDqtlRGVrgnkiAMIFQEPM------VSLNPLHTLEkqlyevlslHRGMRREAARGEILNCLDRVGIRQAAKRlt 151
Cdd:COG1118 69 nLPPRE---RRV-----GFVFQHYAlfphmtVAENIAFGLR---------VRPPSKAEIRARVEELLELVQLEGLADR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 dYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:COG1118 130 -YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
250 260
....*....|....*....|....*.
gi 16130118 232 NGRCVEQNYAATLFASPTHPYTQKLL 257
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-234 |
2.12e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQT 85
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKS-TLLRALADLDPPT----SGEIYLDGKPLSAMPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGvrgnKIAMIFQEPMVslnPLHTLEKQLYEVLSL-HRGMRREAARGEilncLDRVGIRQAAkrLTDYPHQLSGGERQR 164
Cdd:COG4619 72 WRR----QVAYVPQEPAL---WGGTVRDNLPFPFQLrERKFDRERALEL----LERLGLPPDI--LDKPVERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-227 |
2.83e-35 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 131.20 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLR 87
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFD----SGQVYLNGQETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAaRGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMI 167
Cdd:TIGR03608 72 KFRREKLGYLFQN--FALIENETVEENLDLGLKYKKLSKKEK-REKKKEALEKVGLNLKLKQ---KIYELSGGEQQRVAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKlAHRV 227
Cdd:TIGR03608 146 ARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRV 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
298-503 |
3.72e-35 |
|
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: 128.90 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQdpnssln 376
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEEL---RRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnvlqiieeglrvhqptlsaaqreqqviavmhevgldpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130118 457 DKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGE 503
Cdd:cd00267 112 DPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-234 |
4.75e-35 |
|
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: 130.88 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEaGETLALVGESGSGKSvTALSILRLLPSPPVeylsGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEpmVSLN 106
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKS-TLLRCIAGLEKPDG----GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 107 PLHTLEKQLYEVLSLHRGMRREAARGEILnclDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELL---DLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130118 187 LDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-248 |
4.84e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 131.67 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESL---LHASDQTLRGVRGnKIAMIFQE 100
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPD----SGQLNIAGHQFdfsQKPSEKAIRLLRQ-KVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 101 pmVSLNPLHTLEKQLYE----VLslhrGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPE 176
Cdd:COG4161 91 --YNLWPHLTVMENLIEapckVL----GLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 177 LLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNyAATLFASP 248
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
301-506 |
4.99e-35 |
|
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: 130.93 E-value: 4.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHR-IQVVFQdpNSS 374
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKST----LLHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIYQ--FHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNVLQiieeglRVHQPTL----SAAQREQQVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:TIGR02211 94 LLPDFTALE------NVAMPLLigkkSVKEAKERAYEMLEKVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALcHQVIILRQGEVVE 506
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-257 |
6.38e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 131.37 E-value: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvEYLSGDIRFHGESLL--HASDQTLRGVRGnkiaMIFQE 100
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLE----EITSGDLIVDGLKVNdpKVDERLIRQEAG----MVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 101 pmVSLNP-LHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK09493 86 --FYLFPhLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 180 ADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLL 257
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
305-517 |
7.53e-35 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 134.08 E-value: 7.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 305 ISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-----QGSIIFDGQPLQNLNRRQLLPI-RHRIQVVFQDpnSSLNPR 378
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTT----LIRLIAGltrpdEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGLRVHQPTLSAAqREQQVIAVMhevGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRI-SFERVIELL---GIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 459 TVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
289-508 |
9.47e-35 |
|
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: 129.68 E-value: 9.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHnVVVKNISFTLRAGETLGLVGESGSGKSTTglalLRLIN-----SQGSIIFDGQPLQNLnrrqllPIRHR 363
Cdd:cd03301 4 ENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGGRDVTDL------PPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 -IQVVFQdpNSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALIL 442
Cdd:cd03301 73 dIAMVFQ--NYALYPHMTVYDNIAFGLKLRK--VPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 443 KPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-248 |
1.13e-34 |
|
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: 133.69 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 11 LSVGFRHQQTVRTVvnDVSLQIEAGETLALVGESGSGKSvtalSILRL---LPSPPveylSGDIRFHGESLLHASDQTLR 87
Cdd:COG4148 3 LEVDFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKT----TLLRAiagLERPD----SGRIRLGGEVLQDSARGIFL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRGNKIAMIFQEPmvSLNPlHtlekqlYEVLS-LHRGMRREAARGEILNcLDRV----GIRQAAKRltdYPHQLSGGER 162
Cdd:COG4148 73 PPHRRRIGYVFQEA--RLFP-H------LSVRGnLLYGRKRAPRAERRIS-FDEVvellGIGHLLDR---RPATLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAA 242
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLA 219
|
....*.
gi 16130118 243 TLFASP 248
Cdd:COG4148 220 EVLSRP 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-238 |
1.22e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 131.40 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTA--LSILrLLPSppveylSGDIRFHGESLLhaSDQT 85
Cdd:TIGR04520 3 VENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAklLNGL-LLPT------SGKVTVDGLDTL--DEEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRgNKIAMIFQepmvslNPlhtlEKQLyeVLSL----------HRGMRREAARGEILNCLDRVGIRQAAKRltdYPH 155
Cdd:TIGR04520 72 LWEIR-KKVGMVFQ------NP----DNQF--VGATveddvafgleNLGVPREEMRKRVDEALKLVGMEDFRDR---EPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRkLAHRVAVMQNGRC 235
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
...
gi 16130118 236 VEQ 238
Cdd:TIGR04520 215 VAE 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
300-514 |
1.31e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 131.71 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPL--QNLNrrqLLPIRHRIQVVFQDPN 372
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKST----LIQHLNgllkpTSGKIIIDGVDItdKKVK---LSDIRKKVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SslnprlnvlQIIEEGLR---VHQPT---LSAAQREQQVIAVMHEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPS 445
Cdd:PRK13637 94 Y---------QLFEETIEkdiAFGPInlgLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 446 LIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVF 514
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-504 |
2.60e-34 |
|
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: 135.34 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPspPVEYLSGDIRFHGESLlhaSDQTLRGVRGNKIAMIFQEPM 102
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKS-TLMKILSGVY--PHGTWDGEIYWSGSPL---KASNIRDTERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 103 VSLNpLHTLEKQLYEVLSLHRGMRREAA----RGEILNCLDRVGIRQAAKRLTDYphqlSGGERQRVMIAMALLTRPELL 178
Cdd:TIGR02633 89 LVPE-LSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 179 IADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLfaSPTHPYTQKLLN 258
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM--SEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 259 SEPSGDPVPLPEPASTLLDVEQLQVAFPIRKGIlKRivdhnvvVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINS 338
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVINPHR-KR-------VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 339 Q--GSIIFDGQPLQNLNRRQllPIRHRIQVVFQD-PNSSLNPRLNVLQIIEegLRVHQP-----TLSAAQREQQVIAVMH 410
Cdd:TIGR02633 313 KfeGNVFINGKPVDIRNPAQ--AIRAGIAMVPEDrKRHGIVPILGVGKNIT--LSVLKSfcfkmRIDAAAELQIIGSAIQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 411 EVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVR 490
Cdd:TIGR02633 389 RLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVL 467
|
490
....*....|....
gi 16130118 491 ALCHQVIILRQGEV 504
Cdd:TIGR02633 468 GLSDRVLVIGEGKL 481
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
304-527 |
3.87e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPL---QNLNRRQLLPIRHRIQVVFQDPNssL 375
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSS----LLRVLNllempRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQYN--L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NPRLNVLQ-IIEEGLRVHQptLSAAQREQQVIAVMHEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK11124 94 WPHLTVQQnLIEAPCRVLG--LSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPcARVFATPQQEYTRQLLA 527
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
304-504 |
4.37e-34 |
|
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: 127.91 E-value: 4.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDpnSSLNPR 378
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKST----LLKLIykeelPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGLRVHQPTLSAAQReqQVIAVMHEVGLdpETRHR-YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRK--RVPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130118 458 KTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:cd03292 169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-234 |
1.07e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.05 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESLLHASDQTLR 87
Cdd:cd00267 2 IENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 gvrgNKIAMIFQepmvslnplhtlekqlyevlslhrgmrreaargeilncldrvgirqaakrltdyphqLSGGERQRVMI 167
Cdd:cd00267 73 ----RRIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-258 |
1.27e-33 |
|
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: 134.51 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppveYLSGDIRFHGESLLHA 81
Cdd:COG4987 330 GGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLHRGmrrEAARGEILNCLDRVGIRQAAKRLTD--------Y 153
Cdd:COG4987 403 DEDDLR----RRIAVVPQRP-------HLFDTTLRENLRLARP---DATDEELWAALERVGLGDWLAALPDgldtwlgeG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNG 233
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDG 545
|
250 260
....*....|....*....|....*
gi 16130118 234 RCVEQNYAATLFAspTHPYTQKLLN 258
Cdd:COG4987 546 RIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
297-509 |
1.51e-33 |
|
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: 127.35 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLnrrQLLPIRHRIQVVFQDpnssl 375
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSsGSILIDGQDIREV---TLDSLRRAIGVVPQD----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprlNVL--QIIEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDPETRhRYPAEF-----------SGGQRQRIAIARALIL 442
Cdd:cd03253 84 ----TVLfnDTIGYNIRYGRPDAT----DEEVIEAAKAAQIHDKIM-RFPDGYdtivgerglklSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 443 KPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVrALCHQVIILRQGEVVEQGP 509
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTI-VNADKIIVLKDGRIVERGT 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
298-518 |
1.68e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.97 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpIRHRiQVVFQdpN 372
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALSgelspDSGEVRLNGRPLADWSPAEL--ARRR-AVLPQ--H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALI------LKPSL 446
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGRAPH--GLSRAEDDALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFaTPQ 518
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-TPE 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-514 |
2.04e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.54 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVafpirkgilkrIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPL 349
Cdd:COG4559 1 MLEAENLSV-----------RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKST----LLKLLTgeltpSSGEVRLNGRPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 350 QNLNRRQLlpIRHRiQVVFQdpNSSLNPRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMHEVGLDPeTRHRYPAEFSGG 429
Cdd:COG4559 66 AAWSPWEL--ARRR-AVLPQ--HSSLAFPFTVEEVVALGRAPHGS--SAAQDRQIVREALALVGLAH-LAGRSYQTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 430 QRQRIAIARALI-------LKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQG 502
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQG 216
|
250
....*....|..
gi 16130118 503 EVVEQGPCARVF 514
Cdd:COG4559 217 RLVAQGTPEEVL 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
300-505 |
3.84e-33 |
|
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: 123.69 E-value: 3.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQllPIRHRIQVVFQdpnss 374
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKST----LMKILSglykpDSGEILVDGKEVSFASPRD--ARRAGIAMVYQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 lnprlnvlqiieeglrvhqptlsaaqreqqviavmhevgldpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03216 83 ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHqLAYLFISHDLHVVRALCHQVIILRQGEVV 505
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-239 |
1.51e-32 |
|
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: 124.58 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLHAS 82
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKT-TLLRMLagLLKPD------SGSILIDGEDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRgvrgnKIAMIFQEPMVSLNplHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGER 162
Cdd:COG4555 70 REARR-----QIGVLPDERGLYDR--LTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRV---GELSTGMK 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQN 239
Cdd:COG4555 139 KKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
3.30e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPPVEYLSGDIRFHGESLLH 80
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKS-TLLRCLnRMNDLIPGARVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 AS-DQT-LRgvRgnKIAMIFQEPmvslNPLhtlEKQLYE-V---LSLHrGMRREAARGEIL-NCLdrvgiRQAA-----K 148
Cdd:COG1117 83 PDvDVVeLR--R--RVGMVFQKP----NPF---PKSIYDnVaygLRLH-GIKSKSELDEIVeESL-----RKAAlwdevK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 149 -RLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVqAQILQLLRELQGElnMGMLFITHNLSIVRKLAHR 226
Cdd:COG1117 146 dRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|....*...
gi 16130118 227 VAVMQNGRCVEQNYAATLFASPTHPYTQ 254
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
4.96e-32 |
|
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: 122.93 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTqTLLAIENLSVGFR-HQQ--TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRL-----LPSppveylSGDIR 72
Cdd:COG4778 1 MT-TLLEVENLSKTFTlHLQggKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCiygnyLPD------SGSIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 73 FHGES----LLHASDQTLRGVRGNKIAMIFQ----EPMVSlnplhTLEkQLYEVLsLHRGMRREAARGEILNCLDRVGIR 144
Cdd:COG4778 70 VRHDGgwvdLAQASPREILALRRRTIGYVSQflrvIPRVS-----ALD-VVAEPL-LERGVDREEARARARELLARLNLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 145 QaakRLTD-YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKL 223
Cdd:COG4778 143 E---RLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAV 218
|
250
....*....|.
gi 16130118 224 AHRVAVMQNGR 234
Cdd:COG4778 219 ADRVVDVTPFS 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-504 |
7.36e-32 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 128.63 E-value: 7.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDqtlrgVRGNK--IAMIFQEP 101
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKS-TLMKIIAGIVPPD----SGTLEIGGNPCARLTP-----AKAHQlgIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVSLNpLHTLEKQLYEVLSLHRGMRREAARGEILNC---LDRvgirQAAkrltdyphQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK15439 96 LLFPN-LSVKENILFGLPKRQASMQKMKQLLAALGCqldLDS----SAG--------SLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 179 IADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVeqnyaatlFASPTHPY------ 252
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIA--------LSGKTADLstddii 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 253 --------------TQKLLNSEPSGDPVplPEPASTLLDVEQLQvafpiRKGIlkrivdhnvvvKNISFTLRAGETLGLV 318
Cdd:PRK15439 234 qaitpaarekslsaSQKLWLELPGNRRQ--QAAGAPVLTVEDLT-----GEGF-----------RNISLEVRAGEILGLA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 319 GESGSGKSTTGLAL--LRLINSqGSIIFDGQPLQNLNRRQ-------LLPIRHRIQVVFQDpnSSLnpRLNVLqiieeGL 389
Cdd:PRK15439 296 GVVGAGRTELAETLygLRPARG-GRIMLNGKEINALSTAQrlarglvYLPEDRQSSGLYLD--APL--AWNVC-----AL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 390 RVHQPTLSA-AQREQQVIAVMHEV------GLDPETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQA 462
Cdd:PRK15439 366 THNRRGFWIkPARENAVLERYRRAlnikfnHAEQAAR-----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 16130118 463 QILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
273-502 |
9.52e-32 |
|
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: 122.16 E-value: 9.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQvafpirkgilKRIVDHN------VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGS 341
Cdd:COG4778 2 TTLLEVENLS----------KTFTLHLqggkrlPVLDGVSFSVAAGECVALTGPSGAGKST----LLKCIYgnylpDSGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 342 IIF--DGQP--LQNLNRRQLLPIR-HRIQVVFQdpnsSLN--PRLNVLQIIEEGLRVHQPTLSAAQREQQviAVMHEVGL 414
Cdd:COG4778 68 ILVrhDGGWvdLAQASPREILALRrRTIGYVSQ----FLRviPRVSALDVVAEPLLERGVDREEARARAR--ELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 415 DPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCH 494
Cdd:COG4778 142 PERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVAD 220
|
....*...
gi 16130118 495 QVIILRQG 502
Cdd:COG4778 221 RVVDVTPF 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
301-509 |
1.11e-31 |
|
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: 121.83 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPN------- 372
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDL---RSRISIIPQDPVlfsgtir 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPrLN------VLQIIEeglRVHQPTLSAAQREqQVIAVMHEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSL 446
Cdd:cd03244 96 SNLDP-FGeysdeeLWQALE---RVGLKEFVESLPG-GLDTVVEEGGEN----------LSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSlqQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQGP 509
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDS 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
301-496 |
2.21e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.08 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLLPIRHRiQVVFQDPNSSL 375
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKST----LLHLLGgldtpTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NPRLNVLQIIEEGLRV-HQPTLSAAQREQQVIAVmheVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK11629 99 LPDFTALENVAMPLLIgKKKPAEINSRALEMLAA---VGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
301-505 |
2.50e-31 |
|
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: 120.05 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQNLNRRQllpirhRIQVVFQDPNSSLnprl 379
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERRK------SIGYVMQDVDYQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 nVLQIIEEGLRVHQPTLSAAQreQQVIAVMHEVGL-DPETRHryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:cd03226 85 -FTDSVREELLLGLKELDAGN--EQAETVLKDLDLyALKERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130118 459 TVQAQILTLLKSLQ-QKHqlAYLFISHDLHVVRALCHQVIILRQGEVV 505
Cdd:cd03226 160 KNMERVGELIRELAaQGK--AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-236 |
3.21e-31 |
|
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: 121.00 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSV---GFrhqqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLH 80
Cdd:cd03219 1 LEVRGLTKrfgGL-------VALDDVSFSVRPGEIHGLIGPNGAGKT-TLFNLIsgFLRPT------SGSVLFDGEDITG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQtLRGVRGnkIAMIFQEPmvslNPLHTL-----------EKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR 149
Cdd:cd03219 67 LPPH-EIARLG--IGRTFQIP----RLFPELtvlenvmvaaqARTGSGLLLARARREEREARERAEELLERVGLADLADR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 150 LTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAV 229
Cdd:cd03219 140 PAG---ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTV 215
|
....*..
gi 16130118 230 MQNGRCV 236
Cdd:cd03219 216 LDQGRVI 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
301-508 |
3.25e-31 |
|
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: 120.79 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRL-INSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSln 376
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSL---RSMIGVVLQDTflfSGT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnvlqiIEEGLRVHQPTlsaaQREQQVIAVMHEVGLDPETRHR------YPAE----FSGGQRQRIAIARALILKPSL 446
Cdd:cd03254 93 --------IMENIRLGRPN----ATDEEVIEAAKEAGAHDFIMKLpngydtVLGEnggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 447 IILDEPTSSLD----KTVQAQILTLLKslqqkhQLAYLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:cd03254 161 LILDEATSNIDteteKLIQEALEKLMK------GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
300-526 |
3.39e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 120.91 E-value: 3.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLnrrqllPIRHR-IQVVFQdpNS 373
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTT----LLRLIAglerpDSGTILFGGEDATDV------PVQERnVGFVFQ--HY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRLNVLQIIEEGLRVH--QPTLSAAQREQQVIAVMHEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03296 84 ALFRHMTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
302-485 |
3.47e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.89 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKST-----TGlALLRLINSQGSIIFDGQPLQNLNrrqllPIRHRIQVVFQDPnsSLN 376
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTllaaiAG-TLSPAFSASGEVLLNGRRLTALP-----AEQRRIGILFQDD--LLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLQIIEEGLRvhqPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:COG4136 89 PHLSVGENLAFALP---PTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180
....*....|....*....|....*....
gi 16130118 457 DKTVQAQILTLLKSLQQKHQLAYLFISHD 485
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-238 |
4.05e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.20 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPVeylSGDIRFHGESLLHASDQTLRgvr 90
Cdd:COG1132 345 VSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRfyDPT---SGRILIDGVDIRDLTLESLR--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 91 gNKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGmRREAARGEILNCLDRVGIRQAAKRLTD-YPHQ-------LSGGER 162
Cdd:COG1132 414 -RQIGVVPQDTFL-------FSGTIRENIRY--G-RPDATDEEVEEAAKAAQAHEFIEALPDgYDTVvgergvnLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQ 238
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-238 |
4.37e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 123.66 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppveYLSGDIRFHGE--SLLHASD 83
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKT-TLLRIIAGLEH----QTSGHIRFHGTdvSRLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QtlrgvrgnKIAMIFQE------PMVSLNPLHTLEkqlyeVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQL 157
Cdd:PRK10851 74 R--------KVGFVFQHyalfrhMTVFDNIAFGLT-----VLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGrCVE 237
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIE 216
|
.
gi 16130118 238 Q 238
Cdd:PRK10851 217 Q 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
279-526 |
4.67e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.38 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 279 EQLQVAFP-IRKGILKRIV----DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNL 352
Cdd:PRK10070 16 EHPQRAFKyIEQGLSKEQIlektGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 353 NRRQLLPIRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQR 431
Cdd:PRK10070 96 SDAELREVRRKkIAMVFQ--SFALMPHMTVLDNTAFGMEL--AGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCA 511
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
|
250
....*....|....*
gi 16130118 512 RVFATPQQEYTRQLL 526
Cdd:PRK10070 251 EILNNPANDYVRTFF 265
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-238 |
5.21e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 120.52 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGEsllhasDQTLRGVRGNKIAMIFQEpm 102
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKT-TLLRLIAGLERPD----SGTILFGGE------DATDVPVQERNVGFVFQH-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 103 VSLNPLHTLEKQLYEVLSLHRGMRREAA---RGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSERPPEaeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 180 ADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRcVEQ 238
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQ 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
299-528 |
7.09e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 7.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTTglalLRLIN-----SQGSIIFDGQPLQNLNrrqLLPIRHRIQVVFQDPNS 373
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDglleaESGQIIIDGDLLTEEN---VWDIRHKIGMVFQNPDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLnprlnVLQIIEE----GLRvhQPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK13650 93 QF-----VGATVEDdvafGLE--NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVveqgpcaRVFATPQQEYTR--QLLA 527
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV-------ESTSTPRELFSRgnDLLQ 236
|
.
gi 16130118 528 L 528
Cdd:PRK13650 237 L 237
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
302-515 |
7.31e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 121.28 E-value: 7.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqnlNRRQLLPIRHRIQVVFQDPNSSLn 376
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKST----LAKLLNglllpEAGTITVGGMVL---SEETVWDVRRQVGMVFQNPDNQF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnVLQIIEE----GLRVHQ-PTLSAAQREQQVIavmHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK13635 95 ----VGATVQDdvafGLENIGvPREEMVERVDQAL---RQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-247 |
7.55e-31 |
|
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: 126.03 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSvgFRHQQTvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESLLHASDQT 85
Cdd:COG4988 337 IELEDVS--FSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-----YSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRgvrgNKIAMIFQEPmvslnplHTLEKQLYEVLSLHRgmrREAARGEILNCLDRVGIRQAAKRLT---DYP-----HQL 157
Cdd:COG4988 409 WR----RQIAWVPQNP-------YLFAGTIRENLRLGR---PDASDEELEAALEAAGLDEFVAALPdglDTPlgeggRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL-QGELnmgMLFITHNLSIVRkLAHRVAVMQNGRCV 236
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGRT---VILITHRLALLA-QADRILVLDDGRIV 550
|
250
....*....|.
gi 16130118 237 EQNYAATLFAS 247
Cdd:COG4988 551 EQGTHEELLAK 561
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-248 |
7.56e-31 |
|
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: 119.75 E-value: 7.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvrtvVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGEsllhasDQT 85
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-----SGKILLNGK------DIT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKRltdYPHQLSGGERQRV 165
Cdd:cd03299 65 NLPPEKRDISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGIDHLLNR---KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLF 245
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
...
gi 16130118 246 ASP 248
Cdd:cd03299 219 KKP 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
301-508 |
8.03e-31 |
|
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: 119.95 E-value: 8.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSln 376
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWL---RSQIGLVSQEPvlfDGT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnvlqiIEEGLRVHQPTLSAAQREQQV-IAVMHEV------GLDPETRHRYpAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:cd03249 93 --------IAENIRYGKPDATDEEVEEAAkKANIHDFimslpdGYDTLVGERG-SQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 450 DEPTSSLDKTVQAQIltllkslQQKHQLAY-----LFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:cd03249 164 DEATSALDAESEKLV-------QEALDRAMkgrttIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
254-515 |
1.02e-30 |
|
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: 125.63 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 254 QKLLNSEPS-GDPVPLPEPASTLlDVEQLQVAFPIRKgilkrivdhNVVVKNISFTLRAGETLGLVGESGSGKSTtglaL 332
Cdd:COG4618 309 NELLAAVPAePERMPLPRPKGRL-SVENLTVVPPGSK---------RPILRGVSFSLEPGEVLGVIGPSGSGKST----L 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 333 LRLI-----NSQGSIIFDGQPLQNLNRRQL------LPirhriQVV-------------FQDPNSSlnprlnvlQIIEeg 388
Cdd:COG4618 375 ARLLvgvwpPTAGSVRLDGADLSQWDREELgrhigyLP-----QDVelfdgtiaeniarFGDADPE--------KVVA-- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 389 lrvhqptlsAAQReqqviAVMHEV------GLDpeTR-----HRypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:COG4618 440 ---------AAKL-----AGVHEMilrlpdGYD--TRigeggAR----LSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 458 KTVQAQILTLLKSLQQkHQLAYLFISHDLHVVRAlCHQVIILRQGEVVEQGPCARVFA 515
Cdd:COG4618 500 DEGEAALAAAIRALKA-RGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-252 |
1.39e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 122.14 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 11 LSVGFRHQQTVRTVvnDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVeylsGDIRFHGESLLHASDQTLRGVR 90
Cdd:TIGR02142 1 LSARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKT-TLIRLIAGLTRPDE----GEIVLNGRTLFDSRKGIFLPPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 91 GNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLdrvGIRQAAKRltdYPHQLSGGERQRVMIAMA 170
Cdd:TIGR02142 74 KRRIGYVFQE--ARLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGR---LPGRLSGGEKQRVAIGRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTH 250
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
..
gi 16130118 251 PY 252
Cdd:TIGR02142 226 PW 227
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
300-517 |
1.62e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 119.13 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRqllpiRHRIQVVFQdpNSS 374
Cdd:TIGR00968 14 QALDDVNLEVPTGSLVALLGPSGSGKST----LLRIIagleqPDSGRIRLNGQDATRVHAR-----DRKIGFVFQ--HYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHP--KAKIKARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHP 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
299-512 |
2.94e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 117.61 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTTgLALL--RLINSQGSIIFDGQPLqnlnRRQLLPIRHRIQVVFQDpnSSLN 376
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtgELRPTSGTAYINGYSI----RTDRKAARQSLGYCPQF--DALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDPEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:cd03263 88 DELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 457 DKTVQAQILTLLKSLQQKHqlAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCAR 512
Cdd:cd03263 165 DPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
301-518 |
3.46e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.13 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKST-----TGLaLLRLINSQGSIIFDGQplqNLNRRQLLPIRHRIQVVFQDPNSSL 375
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskliNGL-LLPDDNPNSKITVDGI---TLTAKTVWDIREKVGIVFQNPDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprlnVLQIIEE----GLRVHQptLSAAQREQQVIAVMHEVGL----DPEtrhryPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:PRK13640 98 -----VGATVGDdvafGLENRA--VPRPEMIKIVRDVLADVGMldyiDSE-----PANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
23-236 |
3.61e-30 |
|
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: 117.47 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASdqtlRGVRgNKIAMIFQEPm 102
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKT-TTIKMLTTLLKPT----SGRATVAGHDVVREP----REVR-RRIGIVFQDL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 103 vslnplhTLEKQL--YEVLSLH---RGMRREAARGEILNCLDRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03265 83 -------SVDDELtgWENLYIHarlYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
289-517 |
3.87e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 121.21 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIvDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLnrrqllPIRHR 363
Cdd:PRK09452 18 RGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIMLDGQDITHV------PAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 -IQVVFQdpNSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALIL 442
Cdd:PRK09452 87 hVNTVFQ--SYALFPHMTVFENVAFGLRMQK--TPAAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 443 KPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-264 |
6.64e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 118.27 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFrhqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLHASDqT 85
Cdd:PRK14271 22 MAAVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRD-V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRgnKIAMIFQEPmvSLNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQAAK-RLTDYPHQLSGGERQR 164
Cdd:PRK14271 97 LEFRR--RVGMLFQRP--NPFPMSIMDNVLAGVRA-HKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNmgMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
250 260
....*....|....*....|
gi 16130118 245 FASPTHPYTQKLLnSEPSGD 264
Cdd:PRK14271 250 FSSPKHAETARYV-AGLSGD 268
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
275-501 |
7.63e-30 |
|
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: 116.04 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPL 349
Cdd:COG4133 2 MLEAENLSCRR-----------GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILagllpPSAGEVLWNGEPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 350 QNLnrrqllPIRHRIQVVFQDPNSSLNPRLNVLqiieEGLRVHQPTLSAAQREQQVIAVMHEVGLDPEtRHRYPAEFSGG 429
Cdd:COG4133 67 RDA------REDYRRRLAYLGHADGLKPELTVR----ENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAyLFISHDLhvVRALCHQVIILRQ 501
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQP--LELAAARVLDLGD 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
273-515 |
1.31e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 117.64 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFPirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLqN 351
Cdd:PRK13636 3 DYILKVEELNYNYS----------DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPI-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 352 LNRRQLLPIRHRIQVVFQDPNSSLNPRlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMHEVGLDPeTRHRYPAEFSGGQR 431
Cdd:PRK13636 72 YSRKGLMKLRESVGMVFQDPDNQLFSA-SVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCA 511
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
....
gi 16130118 512 RVFA 515
Cdd:PRK13636 228 EVFA 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-234 |
1.64e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.07 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLH 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPT----SGDVIFNGQPMSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLRGVRGNKIAMIFQ--EPMVSLNPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLS 158
Cdd:PRK11629 76 LSSAAKAELRNQKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLaHRVAVMQNGR 234
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
2.43e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.04 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFrhqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLH 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPT----KGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 AsDQTLRGVRGnkIAMIFQEPMVsLNPLHTLEkQLY-------EVLSL----HRGMRREAArgeILncLDRVGIRqaaKR 149
Cdd:PRK09700 72 L-DHKLAAQLG--IGIIYQELSV-IDELTVLE-NLYigrhltkKVCGVniidWREMRVRAA---MM--LLRVGLK---VD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 150 LTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAV 229
Cdd:PRK09700 139 LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 230 MQNGRCVeqnyaatlfaspthpYTQKLlnSEPSGDPVplpepaSTLLDVEQLQVAFPIRKGILKRiVDHNVV-------- 301
Cdd:PRK09700 218 MKDGSSV---------------CSGMV--SDVSNDDI------VRLMVGRELQNRFNAMKENVSN-LAHETVfevrnvts 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 -----VKNISFTLRAGETLGLVGESGSGKSTTGLALLRL-INSQGSIIFDGQPLQnlNRRQLLPIRHRIQVVFQD----- 370
Cdd:PRK09700 274 rdrkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVdKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYITESrrdng 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 371 --PNSSLNPRLNVLQIIEE-------GLRVHQPTLSAAQREQQVIAvmhevgLDPETRHRYPAEFSGGQRQRIAIARALI 441
Cdd:PRK09700 352 ffPNFSIAQNMAISRSLKDggykgamGLFHEVDEQRTAENQRELLA------LKCHSVNQNITELSGGNQQKVLISKWLC 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVE 506
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-244 |
3.41e-29 |
|
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: 114.84 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESLLH-ASDQ 84
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP-----RSGSIRFDGRDITGlPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRgvRGnkIAMIFQEPMVSlnPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgirqaAKRLTDYPHQLSGGERQR 164
Cdd:cd03224 72 RAR--AG--IGYVPEGRRIF--PELTVEENLLLGAYARRRAKRKARLERVYELFPRL-----KERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-507 |
4.59e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 115.73 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 274 TLLDVEQLQVAFPIRKGilkrivdHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQP 348
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQ-------PQPALQDVSLTIESGEFVVALGASGCGKTT----LLNLIAgflapSSGEITLDGVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 349 LQNlnrrqllPIRHRiQVVFQDpnSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSG 428
Cdd:COG4525 71 VTG-------PGADR-GVVFQK--DALLPWLNVLDNVAFGLRLRG--VPKAERRARAEELLALVGLA-DFARRRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIIL--RQGEVVE 506
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
.
gi 16130118 507 Q 507
Cdd:COG4525 218 R 218
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
256-516 |
7.11e-29 |
|
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: 120.58 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 256 LLNSEPS----GDPVPLPEPASTLLDVEQLQVAFPIRKGILkrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLA 331
Cdd:TIGR02204 314 LLQAEPDikapAHPKTLPVPLRGEIEFEQVNFAYPARPDQP--------ALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 332 LLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPN---SSlnprlnvlqiIEEGLRVHQPTLSAAQ-REQQVI 406
Cdd:TIGR02204 386 LLRFYDpQSGRILLDGVDLRQLDPAEL---RARMALVPQDPVlfaAS----------VMENIRYGRPDATDEEvEAAARA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 407 AVMHE-VGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHqlAYLF 481
Cdd:TIGR02204 453 AHAHEfISALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLI 530
|
250 260 270
....*....|....*....|....*....|....*
gi 16130118 482 ISHDLHVVRAlCHQVIILRQGEVVEQGPCARVFAT 516
Cdd:TIGR02204 531 IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-238 |
7.23e-29 |
|
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: 113.50 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLL-----PSppveylSGDIRFHGEsllhasDQTLRGVRGNKIAM 96
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleePT------SGRIYIGGR------DVTDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 97 IFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgeilncldRVgiRQAAKRL------TDYPHQLSGGERQRVMIAMA 170
Cdd:cd03301 77 VFQN--YALYPHMTVYDNIAFGLKLRKVPKDEIDE--------RV--REVAELLqiehllDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRcVEQ 238
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-238 |
7.52e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 114.26 E-value: 7.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLH 80
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIagfetPT------SGEILLDGKDITN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 asdqtlrgVRGNK--IAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLS 158
Cdd:cd03300 67 --------LPPHKrpVNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRcVEQ 238
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK-IQQ 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-236 |
9.42e-29 |
|
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: 111.75 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDqtlRGVRGNKIAMIfqepm 102
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKS-TLMKILSGLYKPD----SGEILVDGKEVSFASP---RDARRAGIAMV----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 103 vslnplhtlekqlyevlslhrgmrreaargeilncldrvgirqaakrltdypHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:cd03216 81 ----------------------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 183 PTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
301-508 |
9.61e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.60 E-value: 9.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpirHR-IQVVFQDPnssLNPR 378
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYL----HRqVALVGQEP---VLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGLRVHQptlsaaqrEQQVIAVMHEVGLDP---ETRHRYPAE-------FSGGQRQRIAIARALILKPSLII 448
Cdd:TIGR00958 569 GSVRENIAYGLTDTP--------DEEIMAAAKAANAHDfimEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 449 LDEPTSSLDktvqAQILTLLKSLQQKHQLAYLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:TIGR00958 641 LDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-238 |
9.82e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.44 E-value: 9.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLL 79
Cdd:COG4559 1 MLEAENLSVRLGG----RTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 HASDQTLRGVRgnkiAMIFQEpmVSLN-PLHTLEkqlyeVLSLHR---GMRREAARGEILNCLDRVGIRQAAKRltDYPh 155
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFTVEE-----VVALGRaphGSSAAQDRQIVREALALVGLAHLAGR--SYQ- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALL-------TRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVA 228
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRIL 211
|
250
....*....|
gi 16130118 229 VMQNGRCVEQ 238
Cdd:COG4559 212 LLHQGRLVAQ 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-521 |
1.03e-28 |
|
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: 116.05 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 317 LVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNrrqllPIRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRV 391
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAgfeqpDSGSIMLDGEDVTNVP-----PHLRHINMVFQ--SYALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 392 HQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSL 471
Cdd:TIGR01187 70 RK--VPRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130118 472 QQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEY 521
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-508 |
1.16e-28 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 113.23 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLqnlnRRQLLPIRHRIQVVFQD 370
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGHDV----VREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 371 PnsSLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:cd03265 82 L--SVDDELTGWENLYIHARLY--GVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-238 |
1.92e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.94 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLL-----PSppveylSGDIRFHGESL-- 78
Cdd:COG3839 4 LELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagledPT------SGEILIGGRDVtd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 LHASDqtlrgvRGnkIAMIFQEPMvslnplhtlekqLYEVLSLH---------RGMRREAARGEILNCLDRVGIRQAAKR 149
Cdd:COG3839 70 LPPKD------RN--IAMVFQSYA------------LYPHMTVYeniafplklRKVPKAEIDRRVREAAELLGLEDLLDR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 150 ltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAV 229
Cdd:COG3839 130 ---KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAV 206
|
....*....
gi 16130118 230 MQNGRcVEQ 238
Cdd:COG3839 207 MNDGR-IQQ 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-523 |
2.78e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.21 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 269 PEPASTLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN----------S 338
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY-----------GDKQALKDINLDIPENKVTALIGPSGCGKST----LLRCLNrmndlipgarV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 339 QGSIIFDGQplqNLNRRQLLPIRHRIQV--VFQDPN---SSlnprlnvlqiIEE----GLRVHQpTLSAAQREQQVIAVM 409
Cdd:COG1117 70 EGEILLDGE---DIYDPDVDVVELRRRVgmVFQKPNpfpKS----------IYDnvayGLRLHG-IKSKSELDEIVEESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 410 HEVGLDPETRHR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLqqKHQLAYLFISHDL 486
Cdd:COG1117 136 RKAALWDEVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNM 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130118 487 HVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTR 523
Cdd:COG1117 214 QQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
299-514 |
3.74e-28 |
|
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: 112.49 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN------SQGSIIFDGQPLQNLNrrqLLPIRHRIQVVFQDPN 372
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITgdlpptYGNDVRLFGERRGGED---VWELRKRIGLVSPALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPRLNVLQIIEEGL-----RVHQPTlsAAQREQqVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:COG1119 89 LRFPRDETVLDVVLSGFfdsigLYREPT--DEQRER-ARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVF 514
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-524 |
5.34e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.31 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN------SQGSIIFDGQplqNLNRRQLLPIRHRIQVVFQDPNSS 374
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQ---DIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 lnPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPA---EFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK14247 95 --PNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 452 PTSSLDKTVQAQILTLLksLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQ 524
Cdd:PRK14247 173 PTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
26-234 |
5.42e-28 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 111.19 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLHASDQTLRGVRgNKIAMIFQE 100
Cdd:TIGR02673 19 HDVSLHIRKGEFLFLTGPSGAGKT----TLLKLLygaltPS------RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 101 PMVSLNplhtleKQLYE--VLSLH-RGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:TIGR02673 88 FRLLPD------RTVYEnvALPLEvRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
285-521 |
6.13e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.43 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 285 FPIRKGILKRIVDhNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQplqNLNRRQllp 359
Cdd:PRK11432 6 FVVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDGE---DVTHRS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 360 IRHR-IQVVFQdpNSSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIAR 438
Cdd:PRK11432 75 IQQRdICMVFQ--SYALFPHMSLGENVGYGLKMLG--VPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 439 ALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
...
gi 16130118 519 QEY 521
Cdd:PRK11432 230 SRF 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-238 |
8.20e-28 |
|
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: 110.38 E-value: 8.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTlrgvrgNKIAMIFQEP 101
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKT-TTMKIILGLIKPD----SGEITFDGKSYQKNIEAL------RRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 mvSLNPLHTLEKQLYeVLSLHRGMRREaargEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:cd03268 82 --GFYPNLTARENLR-LLARLLGIRKK----RIDEVLDVVGLKDSAKKKVK---GFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 182 EPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-238 |
8.43e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESL 78
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALsgelsPD------SGEVRLNGRPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 LHASDQTLRGVRgnkiAMIFQEPMVSLnPLhTLEkqlyEVLSL----HRGMRREAARgEILNCLDRVGIRQAAKRltDYP 154
Cdd:PRK13548 67 ADWSPAELARRR----AVLPQHSSLSF-PF-TVE----EVVAMgrapHGLSRAEDDA-LVAAALAQVDLAHLAGR--DYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 hQLSGGERQRVMIAMAL--LTRPE----LLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVA 228
Cdd:PRK13548 134 -QLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
250
....*....|
gi 16130118 229 VMQNGRCVEQ 238
Cdd:PRK13548 213 LLHQGRLVAD 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-246 |
8.86e-28 |
|
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: 111.17 E-value: 8.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 12 SVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpVEYLSGDIRFHGESLlhaSDQTLRGVRg 91
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRF-YDVDSGRILIDGHDV---RDYTLASLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 92 NKIAMIFQEPMVSLNPLHtlEKQLYEvlslhrgmRREAARGEILNCLDRVGIRQAAKRLTDYPH--------QLSGGERQ 163
Cdd:cd03251 76 RQIGLVSQDVFLFNDTVA--ENIAYG--------RPGATREEVEEAARAANAHEFIMELPEGYDtvigergvKLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQNYAAT 243
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
...
gi 16130118 244 LFA 246
Cdd:cd03251 223 LLA 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
297-509 |
1.03e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 117.36 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-----QGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQdp 371
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKST----LLRLLLGfetpeSGSVFYDGQDLAGLDVQAV---RRQLGVVLQ-- 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NSSLNPRlNVLQIIEEGLRVhqpTLSAAQreqqviAVMHEVGLDPETR------HRYPAE----FSGGQRQRIAIARALI 441
Cdd:TIGR03797 535 NGRLMSG-SIFENIAGGAPL---TLDEAW------EAARMAGLAEDIRampmgmHTVISEgggtLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILTLLKSLqqkhQLAYLFISHDLHVVRAlCHQVIILRQGEVVEQGP 509
Cdd:TIGR03797 605 RKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-238 |
1.11e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.06 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESLLHASdqt 85
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLFDGKPLDIAA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 lrgvrGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRV 165
Cdd:cd03269 69 -----RNRIGYLPEER--GLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
306-510 |
1.46e-27 |
|
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: 109.95 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 306 SFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQplqnlNRRQLLPIRHRIQVVFQDPNssLNPRLN 380
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKST----LLNLIAgfiepASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENN--LFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 381 VLQIIEEGLRvhqPTLS-AAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
Cdd:TIGR01277 87 VRQNIGLGLH---PGLKlNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 460 VQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPC 510
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
302-508 |
1.64e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 116.60 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTgLALL-RLINSQ-GSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSln 376
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL-INLLqRVFDPQsGRILIDGTDIRTVTRASL---RRNIAVVFQDAglfNRS-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnvlqiIEEGLRVHQPTLSAAQ-REQQVIAVMHEV------GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK13657 425 --------IEDNIRVGRPDATDEEmRAAAERAQAHDFierkpdGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLqqKHQLAYLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-248 |
1.68e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.46 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESLLH-AS 82
Cdd:COG0410 2 PMLEVENLHAGYGGIH----VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP-----RSGSIRFDGEDITGlPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRgvRGnkIAM------IFqepmvslnPLHTLEkqlyEVLSLhrGMRREAARGEILNCLDRVG---------IRQAA 147
Cdd:COG0410 73 HRIAR--LG--IGYvpegrrIF--------PSLTVE----ENLLL--GAYARRDRAEVRADLERVYelfprlkerRRQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 148 krltdypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRV 227
Cdd:COG0410 135 -------GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRA 206
|
250 260
....*....|....*....|.
gi 16130118 228 AVMQNGRCVEQNYAATLFASP 248
Cdd:COG0410 207 YVLERGRIVLEGTAAELLADP 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
297-514 |
1.78e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.38 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtgLALLRL---INSQGSIIFDGQPLQNLNRRQllpIRHRIQVVFQDPNS 373
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKST--IAKLMIgieKVKSGEIFYNNQAITDDNFEK---LRKHIGIVFQNPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLnprlnVLQIIEE----GLRVHQPTLSAAQREqqVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK13648 95 QF-----VGSIVKYdvafGLENHAVPYDEMHRR--VSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLhvVRAL-CHQVIILRQGEVVEQGPCARVF 514
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDL--SEAMeADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
297-518 |
1.78e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.32 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQnLNRRQLLPIRHRIQVVFQDPNSSL 375
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 -NPRlnVLQIIEEGlrvhqPT---LSAAQREQQVIAVMHEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK13639 92 fAPT--VEEDVAFG-----PLnlgLSKEEVEKRVKEALKAVGMEGFEN-KPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 452 PTSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
261-498 |
2.62e-27 |
|
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: 115.46 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 261 PSGDPVPLPEPASTLLDVEQLQVAFPirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQ 339
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYP----------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 340 GSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPnsslnprLNVLQIIEEGLRVHQPTLSAAQreqqVIAVMHEVGLD---- 415
Cdd:TIGR02857 377 GSIAVNGVPLADADADSW---RDQIAWVPQHP-------FLFAGTIAENIRLARPDASDAE----IREALERAGLDefva 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 416 --PETRH----RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVV 489
Cdd:TIGR02857 443 alPQGLDtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV--LLVTHRLALA 520
|
....*....
gi 16130118 490 RALCHQVII 498
Cdd:TIGR02857 521 ALADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
3.33e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.25 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVrtvvNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLH 80
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKAL----NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQT--LRgvrgNKIAMIFQEPmvslNPLhtlEKQLYEvlSLHRGMRREAARG-EILNCLDRVGIRQAA------KRLT 151
Cdd:PRK14239 77 PRTDTvdLR----KEIGMVFQQP----NPF---PMSIYE--NVVYGLRLKGIKDkQVLDEAVEKSLKGASiwdevkDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNmgMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFL 221
|
250 260
....*....|....*....|...
gi 16130118 232 NGRCVEQNYAATLFASPTHPYTQ 254
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKETE 244
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-289 |
4.81e-27 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 112.09 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQtvrtvVNDVSLQIEAGETLALVGESGSGKSVTaLSILRLLPSPPveylSGDIRFHGEsllhasDQ 84
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVL-LELIAGIWPPD----SGKIYLDGK------DI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGNKIAMIFQEPMvsLNPLHTLEKQLYEVLSLHRGMRREAAR--GEILNCLdrvGIRQAAKRltdYPHQLSGGER 162
Cdd:NF040840 65 TNLPPEKRGIAYVYQNYM--LFPHKTVFENIAFGLKLRKVPKEEIERkvKEIMELL---GISHLLHR---KPRTLSGGEQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAA 242
Cdd:NF040840 137 QRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVR 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16130118 243 TLFASPTHPYTQKLLNSEPSGDPVPLPEPASTLLDVEQLQVAFPIRK 289
Cdd:NF040840 217 EVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNIKIELPEEK 263
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
302-502 |
5.53e-27 |
|
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: 108.71 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNlnrrqllPIRHRIqVVFQdpNSSLN 376
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST----LLNLISglaqpTSGGVILEGKQITE-------PGPDRM-VVFQ--NYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:TIGR01184 67 PWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130118 457 DKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQG 502
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-258 |
6.35e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.67 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVEYLSGD----IRFHGESLLHASDQTLRGVRgNKIAMI 97
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLekPSEGSIVVNGQtinlVRDKDGQLKVADKNQLRLLR-TRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 98 FQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKrlTDYPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK10619 98 FQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELqGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLL 257
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
.
gi 16130118 258 N 258
Cdd:PRK10619 253 K 253
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
301-509 |
7.42e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 108.29 E-value: 7.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpIRHRIQVVFQDPNssLNPRL 379
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRR--IFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 NVlqiiEEGLRVHQPTLSAAQREQQVIAVmheVGLDP---ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:cd03224 91 TV----EENLLLGAYARRRAKRKARLERV---YELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 457 DKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:cd03224 164 APKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-201 |
7.55e-27 |
|
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: 107.56 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPVEylsGDIRFHGESLLHAS 82
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKT----TLLRILAglLPPSA---GEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRgvrgnKIAMIFQEPMV--SLNPLhtlekqlyEVLSLHRGMR-REAARGEILNCLDRVGIRQAAKRLtdyPHQLSG 159
Cdd:COG4133 71 EDYRR-----RLAYLGHADGLkpELTVR--------ENLRFWAALYgLRADREAIDEALEAVGLAGLADLP---VRQLSA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
298-508 |
9.28e-27 |
|
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: 107.84 E-value: 9.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVVVKNISFTLRAGETLGLVGESGSGKSTTglalLRLIN-----SQGSIIFDG-----QPLQnlnrrqllpIRHRIQVV 367
Cdd:cd03266 17 TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDGfdvvkEPAE---------ARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 368 FQdpNSSLNPRLNVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:cd03266 84 SD--STGLYDRLTARENLEYFAGLY--GLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-512 |
1.11e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 306 SFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQplqnlNRRQLLPIRHRIQVVFQDPNssLNPRLN 380
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKST----LLNLIAgfltpASGSLTLNGQ-----DHTTTPPSRRPVSMLFQENN--LFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 381 VLQIIeeGLRVHqP--TLSAAQReQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:PRK10771 88 VAQNI--GLGLN-PglKLNAAQR-EKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 459 TVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCAR 512
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-238 |
1.13e-26 |
|
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: 108.01 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppveY--LSGDIRFHGESLlhaSDQTLRGVRgNKIAMIFQEP 101
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-------YdpTSGEILLDGVDI---RDLNLRWLR-SQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVSLNPLhtLEKQLYEVLSLHRGMRREAARgeILNCLD-----------RVGIRQAakrltdyphQLSGGERQRVMIAMA 170
Cdd:cd03249 87 VLFDGTI--AENIRYGKPDATDEEVEEAAK--KANIHDfimslpdgydtLVGERGS---------QLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQ 238
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
292-508 |
1.14e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 107.30 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNrrqllPIRHRIQVVFQD 370
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpDSGEITFDGKSYQKNI-----EALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 371 PnsSLNPRLNVlqiiEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:cd03268 81 P--GFYPNLTA----RENLRLLA--RLLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
306-508 |
1.15e-26 |
|
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: 107.58 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 306 SFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNrrqllPIRHRIQVVFQDPNssLNPRLN 380
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKST----LLNLIAgfetpQSGRVLINGVDVTAAP-----PADRPVSMLFQENN--LFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 381 VLQIIEEGLrvhQPTLS-AAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
Cdd:cd03298 87 VEQNVGLGL---SPGLKlTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130118 460 VQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-238 |
1.26e-26 |
|
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: 107.19 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIrfhgesLLHASDQTLRGVRGNKIAMIFQEPmvSLN 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS-TLLNLIAGFETPQ----SGRV------LINGVDVTAAPPADRPVSMLFQEN--NLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 107 PLHTLEKQLyeVLSLHRGMR-REAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:cd03298 83 AHLTVEQNV--GLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 186 ALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
282-508 |
1.43e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.92 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 282 QVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQllpI 360
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITISKENLKE---I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 361 RHRIQVVFQDPNSSL--------------NPRLN---VLQIIEEglrvhqptlsaaqreqqviaVMHEVGLDpETRHRYP 423
Cdd:PRK13632 82 RKKIGIIFQNPDNQFigatveddiafgleNKKVPpkkMKDIIDD--------------------LAKKVGME-DYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGE 503
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGK 219
|
....*
gi 16130118 504 VVEQG 508
Cdd:PRK13632 220 LIAQG 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
300-525 |
1.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNR-RQLLPIRHRIQVVFQDPNS 373
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKST----LIQNINallkpTTGTVTVDDITITHKTKdKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRlNVLQIIEEGLRVHQPTLSAAQreQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK13646 97 QLFED-TVEREIIFGPKNFKMNLDEVK--NYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFAtpQQEYTRQL 525
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADW 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
296-524 |
1.68e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 296 VDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSII-FDGQPL---QNLNRRQLLPIRHRIQVVFQDP 371
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NSSlnPRLNVLQIIEEGLRVHqptlsAAQREQQVIAVMHE----VGLDPETRHRY--PA-EFSGGQRQRIAIARALILKP 444
Cdd:PRK14246 100 NPF--PHLSIYDNIAYPLKSH-----GIKEKREIKKIVEEclrkVGLWKEVYDRLnsPAsQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 445 SLIILDEPTSSLDKTVQAQILTLLKSLqqKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQ 524
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
300-514 |
1.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTGL---ALLrlINSQGSIIFDGqpLQNLNRRQLLPIRHRIQVVFQDPNSSLn 376
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALL--IPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK13633 99 ----VATIVEEDVAFGPENLGIPPEEirERVDESLKKVGMYEYRRHA-PHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDL-HVVRAlcHQVIILRQGEVVEQGPCARVF 514
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-257 |
1.91e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.28 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEpmVS 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL-----IEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 185 TALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLL 257
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-238 |
2.18e-26 |
|
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: 106.81 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVgfRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQTLR 87
Cdd:cd03244 5 FKNVSL--RYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL-----VELSSGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 gvrgNKIAMIFQEPMV-------SLNPLHtlekqlyevlslhrgmrrEAARGEILNCLDRVGIRQAAK--------RLTD 152
Cdd:cd03244 78 ----SRISIIPQDPVLfsgtirsNLDPFG------------------EYSDEELWQALERVGLKEFVEslpggldtVVEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqgEL-NMGMLFITHNLSIVRKlAHRVAVMQ 231
Cdd:cd03244 136 GGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE---AFkDCTVLTIAHRLDTIID-SDRILVLD 211
|
....*..
gi 16130118 232 NGRCVEQ 238
Cdd:cd03244 212 KGRVVEF 218
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
8-257 |
2.26e-26 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 110.47 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRhqqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvEYLSGDIRFHGESLLHASDQTlr 87
Cdd:TIGR03258 8 IDHLRVAYG----ANTVLDDLSLEIEAGELLALIGKSGCGKT-TLLRAIAGFVKA--AGLTGRIAIADRDLTHAPPHK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 gvRGnkIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMI 167
Cdd:TIGR03258 79 --RG--LALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAE-RVADALKLVGLGDAAAH---LPAQLSGGMQQRIAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGEL-NMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFA 246
Cdd:TIGR03258 149 ARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYD 228
|
250
....*....|.
gi 16130118 247 SPTHPYTQKLL 257
Cdd:TIGR03258 229 APADGFAAEFL 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
292-519 |
2.28e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.17 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQllpirHRIQV 366
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIaglehQTSGHIRFHGTDVSRLHARD-----RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQdpNSSLNPRLNVLQIIEEGLRV--HQPTLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:PRK10851 79 VFQ--HYALFRHMTVFDNIAFGLTVlpRRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 445 SLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGeVVEQgpcarvFATPQQ 519
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ------AGTPDQ 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
289-508 |
2.50e-26 |
|
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: 106.51 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIvDHNVVVKNISFTLRAGeTLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLqnlnRRQLLPIRHR 363
Cdd:cd03264 4 ENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTT----LMRILAtltppSSGTIRIDGQDV----LKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDPNssLNPRLNVlqiiEEGLRvHQPTL---SAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARAL 440
Cdd:cd03264 74 IGYLPQEFG--VYPNFTV----REFLD-YIAWLkgiPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 441 ILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
303-518 |
2.68e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.57 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQN-LNRRQLLPIRHRIQVVFQDPNSSLN 376
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKST----LLQHLNgllqpTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRlNVLQIIEEGlrvhqPT---LSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK13634 100 EE-TVEKDICFG-----PMnfgVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
302-518 |
3.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.26 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTGlallRLINS-----QGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPNSSLn 376
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTA----RLIDGlfeefEGKVKIDGELLTAENVWNL---RRKIGMVFQNPDNQF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVG-LDPETRHryPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK13642 95 ----VGATVEDDVAFGMENQGIPREEmiKRVDEALLAVNmLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
276-515 |
4.41e-26 |
|
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: 112.65 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 276 LDVEQLQVAFPIRKGILK-RIVDHNV----------VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQ 339
Cdd:TIGR03375 444 LPVERPEGTRFLHRPRLQgEIEFRNVsfaypgqetpALDNVSLTIRPGEKVAIIGRIGSGKST----LLKLLLglyqpTE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 340 GSIIFDGqplqnLNRRQLLP--IRHRIQVVFQDP---NSSLnpRLNVlqiieeglrvhqpTLSAAQ-REQQVIAVMHEVG 413
Cdd:TIGR03375 520 GSVLLDG-----VDIRQIDPadLRRNIGYVPQDPrlfYGTL--RDNI-------------ALGAPYaDDEEILRAAELAG 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 414 LDPETRhRYPAEF-----------SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFI 482
Cdd:TIGR03375 580 VTEFVR-RHPDGLdmqigergrslSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLV 656
|
250 260 270
....*....|....*....|....*....|...
gi 16130118 483 SHDLHVVRaLCHQVIILRQGEVVEQGPCARVFA 515
Cdd:TIGR03375 657 THRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
6.28e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpveyLSGDIRFHGESLlhaS 82
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKS-TISKILTGLLKP----QSGEIKIDGITI---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRGVRgNKIAMIFQEP---MVSLnplhTLEKQLyeVLSL-HRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLS 158
Cdd:PRK13632 75 KENLKEIR-KKIGIIFQNPdnqFIGA----TVEDDI--AFGLeNKKVPPKKMKDIIDDLAKKVGMEDYLDK---EPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVrKLAHRVAVMQNGRCVEQ 238
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQ 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-233 |
6.34e-26 |
|
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: 105.03 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVrtvVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGesllhasDQTLR 87
Cdd:cd03226 2 IENISFSYKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKT-TLAKILAGLIKES----SGSILLNG-------KPIKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRGNKIAMIFQEPmvslnplhtlEKQLYE--VLS-LHRGMRREAARGEILNC-LDRVGIRQAAKRltdYPHQLSGGERQ 163
Cdd:cd03226 67 KERRKSIGYVMQDV----------DYQLFTdsVREeLLLGLKELDAGNEQAETvLKDLDLYALKER---HPLSLSGGQKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMgMLFITHNLSIVRKLAHRVAVMQNG 233
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-238 |
7.09e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 105.78 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 9 ENLSVGFrhqQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLlhaSD 83
Cdd:cd03253 4 ENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLfrfydVS------SGSILIDGQDI---RE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRgNKIAMIFQEpMVSLNP----------LHTLEKQLYEVlslhrgmrREAAR--GEILNCLD----RVGIRQAa 147
Cdd:cd03253 68 VTLDSLR-RAIGVVPQD-TVLFNDtigynirygrPDATDEEVIEA--------AKAAQihDKIMRFPDgydtIVGERGL- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 148 krltdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRV 227
Cdd:cd03253 137 --------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKI 205
|
250
....*....|.
gi 16130118 228 AVMQNGRCVEQ 238
Cdd:cd03253 206 IVLKDGRIVER 216
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
275-499 |
7.91e-26 |
|
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: 105.55 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAFPI-RKGILKRivdhnVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLR---------LINSQGSIIf 344
Cdd:TIGR02324 1 LLEVEDLSKTFTLhQQGGVRL-----PVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnylpdsgriLVRHEGAWV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 345 dgqPLQNLNRRQLLPIR-HRIQVVFQdpnsSLN--PRLNVLQIIEEGLRVHQPTLSAAQREQQviAVMHEVGLDPETRHR 421
Cdd:TIGR02324 75 ---DLAQASPREVLEVRrKTIGYVSQ----FLRviPRVSALEVVAEPLLERGVPREAARARAR--ELLARLNIPERLWHL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLqqKHQ-LAYLFISHDLHVVRALCHQVIIL 499
Cdd:TIGR02324 146 PPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEA--KARgAALIGIFHDEEVRELVADRVMDV 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
303-508 |
9.05e-26 |
|
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: 111.07 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSlnpr 378
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDvTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTvlfNDT---- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 lnvlqiIEEGLRVHQPTLSAAQREQQV-IAVMH---------------EVGLdpetrhrypaEFSGGQRQRIAIARALIL 442
Cdd:COG5265 448 ------IAYNIAYGRPDASEEEVEAAArAAQIHdfieslpdgydtrvgERGL----------KLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 443 KPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHqlAYLFISHDLH-VVRAlcHQVIILRQGEVVEQG 508
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-508 |
9.73e-26 |
|
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: 105.39 E-value: 9.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---N 372
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASL---RRQIGLVSQDVflfN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSlnprlnvlqiIEEGLRVHQPTLSAAQ-REQQVIAVMHEV------GLDPETRHRyPAEFSGGQRQRIAIARALILKPS 445
Cdd:cd03251 90 DT----------VAENIAYGRPGATREEvEEAARAANAHEFimelpeGYDTVIGER-GVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 446 LIILDEPTSSLDKTVQAQILTLLKSLqQKHQLAyLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERL-MKNRTT-FVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
297-508 |
1.39e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.59 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRL-INSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---N 372
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVtlfY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLnpRLNvlqiIEEGLRVHQptlsaaqrEQQVIAVMHEVGLDPETRhRYPAEF-----------SGGQRQRIAIARALI 441
Cdd:cd03245 92 GTL--RDN----ITLGAPLAD--------DERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVrALCHQVIILRQGEVVEQG 508
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-246 |
1.69e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFR-HQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGESLlhaSDQTL 86
Cdd:PRK13650 5 IEVKNLTFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL-----EAESGQIIIDGDLL---TEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RGVRgNKIAMIFQEP-------MVSLNPLHTLEKQlyevlslhrGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSG 159
Cdd:PRK13650 77 WDIR-HKIGMVFQNPdnqfvgaTVEDDVAFGLENK---------GIPHEEMKERVNEALELVGMQDFKER---EPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVrKLAHRVAVMQNGRCVEQN 239
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTS 222
|
....*..
gi 16130118 240 YAATLFA 246
Cdd:PRK13650 223 TPRELFS 229
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
254-509 |
1.70e-25 |
|
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: 110.13 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 254 QKLLNSEPSGDP-VPLPEPASTLlDVEQLQVAFPIRKgilkrivdhNVVVKNISFTLRAGETLGLVGESGSGKSTtglaL 332
Cdd:TIGR01842 295 NELLANYPSRDPaMPLPEPEGHL-SVENVTIVPPGGK---------KPTLRGISFSLQAGEALAIIGPSGSGKST----L 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 333 LRLI-----NSQGSIIFDGQPLQNLNRRQLLPirhRIQVVFQD----PNSslnprlnvlqIIEEGLRVHQPTLSAAQREQ 403
Cdd:TIGR01842 361 ARLIvgiwpPTSGSVRLDGADLKQWDRETFGK---HIGYLPQDvelfPGT----------VAENIARFGENADPEKIIEA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 404 QVIAVMHEVGLdpetrhRYP-----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLq 472
Cdd:TIGR01842 428 AKLAGVHELIL------RLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL- 500
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130118 473 QKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQGP 509
Cdd:TIGR01842 501 KARGITVVVITHRPSLL-GCVDKILVLQDGRIARFGE 536
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-257 |
2.16e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.92 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLHASDQTLRgVRgNKIAMIFQEPmv 103
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIE-VR-REVGMVFQYP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 slNPLHTLekQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAA------KRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK14267 95 --NPFPHL--TIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQGELNmgMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLL 257
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
301-515 |
2.30e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.47 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLqNLNRRQLLPIRHRIQVVFQDP-------- 371
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPeqqifytd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 -NSSLNPRLNVLQIIEEGL--RVHQP-TLSAAQReqqviavmhevgldpeTRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:PRK13638 95 iDSDIAFSLRNLGVPEAEItrRVDEAlTLVDAQH----------------FRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSL--QQKHqlaYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIvaQGNH---VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-245 |
2.97e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.51 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLlhaSDQ--TLRGVRgNKIAMIF 98
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT------SGKIIIDGVDI---TDKkvKLSDIR-KKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 99 QEPmvslnplhtlEKQLYEVL--------SLHRGMRREAARGEILNCLDRVGIrqaakrltDY-------PHQLSGGERQ 163
Cdd:PRK13637 90 QYP----------EYQLFEETiekdiafgPINLGLSEEEIENRVKRAMNIVGL--------DYedykdksPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAAT 243
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
..
gi 16130118 244 LF 245
Cdd:PRK13637 232 VF 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-518 |
3.05e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.91 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQN 351
Cdd:COG0410 1 MPMLEVENLHAGY-----------GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 352 LNRRQLlpIRHRI-QV-----VFqdpnsslnPRLNVlqiiEEGLRVHQPTLSAAQREQQVIAVMHEvgLDP---ETRHRY 422
Cdd:COG0410 70 LPPHRI--ARLGIgYVpegrrIF--------PSLTV----EENLLLGAYARRDRAEVRADLERVYE--LFPrlkERRRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQG 502
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 16130118 503 EVVEQGPCARVFATPQ 518
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
298-504 |
3.06e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 103.70 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPnsSLN 376
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYL---HSKVSLVGQEP--VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRlNVLQIIEEGLR-VHQPTLSAAQREQQV---IAVMhEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03248 101 AR-SLQDNIAYGLQsCSFECVKEAAQKAHAhsfISEL-ASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKHqlAYLFISHDLHVV-RAlcHQVIILRQGEV 504
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVeRA--DQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
297-508 |
3.92e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.14 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP 371
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTrawdpQQGEILLNGQPIADYSEAAL---RQAISVVSQRV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 ---NSSLnprlnvlqiiEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDP--ETRHRYPA-------EFSGGQRQRIAIARA 439
Cdd:PRK11160 424 hlfSATL----------RDNLLLAAPNAS----DEALIEVLQQVGLEKllEDDKGLNAwlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 440 LILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLhvvRALCH--QVIILRQGEVVEQG 508
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRL---TGLEQfdRICVMDNGQIIEQG 555
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
299-526 |
4.36e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.15 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPL---QNLNRRQLLPIRHRIQV--VFQDPNS 373
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRlfgRNIYSPDVDPIEVRREVgmVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SlnPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHR---YPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:PRK14267 97 F--PHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 451 EPTSSLDKTVQAQILTLLksLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK14267 175 EPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-508 |
4.74e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQdpnsslNPRL 379
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESW---RKHLSWVGQ------NPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 nVLQIIEEGLRVHQPTLSAAQReQQVIA--------VMHEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK11174 435 -PHGTLRDNVLLGNPDASDEQL-QQALEnawvseflPLLPQGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHqlAYLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-238 |
5.58e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.90 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLlhaSDQTLRGVRGNkIAMIFQEP 101
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPQ----SGRILIDGTDI---RTVTRASLRRN-IAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVslnplhtLEKQLYEVLSLHRG------MRREAARGEILNCLDR--------VGIRQaakrltdypHQLSGGERQRVMI 167
Cdd:PRK13657 419 GL-------FNRSIEDNIRVGRPdatdeeMRAAAERAQAHDFIERkpdgydtvVGERG---------RQLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQ 238
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
264-526 |
7.35e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.07 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 264 DPVPLPEPAST-----LLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN- 337
Cdd:PRK11607 3 DAIPRPQAKTRkaltpLLEIRNLTKSF-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 338 ----SQGSIIFDGQPLQnlnrrQLLPIRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVHQ-PTLSAAQREQQVIAVMHEv 412
Cdd:PRK11607 68 feqpTAGQIMLDGVDLS-----HVPPYQRPINMMFQ--SYALFPHMTVEQNIAFGLKQDKlPKAEIASRVNEMLGLVHM- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 413 gldPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRAL 492
Cdd:PRK11607 140 ---QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTM 216
|
250 260 270
....*....|....*....|....*....|....
gi 16130118 493 CHQVIILRQGEVVEQGPCARVFATPQQEYTRQLL 526
Cdd:PRK11607 217 AGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
297-508 |
8.25e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 102.95 E-value: 8.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRL-INSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDpnssl 375
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprlNVL--QIIEEGLRVHQPTLSAAQREQQV-IAVMHEVGLD-PETRHRYPAE----FSGGQRQRIAIARALILKPSLI 447
Cdd:cd03252 85 ----NVLfnRSIRDNIALADPGMSMERVIEAAkLAGAHDFISElPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTV--IIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
301-507 |
9.57e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.55 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTgLALLRLIN--SQGSIIFDGQPLQNLNRRQLLPIRHR-IQVVFQdpNSSLNP 377
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTL-LAILAGLDdgSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQ--SFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RLNVLQiieeglRVHQPTL----SAAQREQQVIAVMHEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK10584 102 TLNALE------NVELPALlrgeSSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVrALCHQVIILRQGEVVEQ 507
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-238 |
1.09e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 101.89 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvrtVVNDVSLQIEAGeTLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLhASDQT 85
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKT-TLMRILATLTPPS----SGTIRIDGQDVL-KQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVrgnkIAMIFQEPMVSlnPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRV 165
Cdd:cd03264 70 LRRR----IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL-GE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
301-506 |
1.11e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.86 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNlnrrqllPIRHRiQVVFQdpNSSL 375
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAgfvpyQHGSITLDGKPVEG-------PGAER-GVVFQ--NEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PRK11248 82 LPWRNVQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 456 LDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILR--QGEVVE 506
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-216 |
1.29e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.16 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENL--SVGFRHQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLl 79
Cdd:PRK10584 3 AENIVEVHHLkkSVGQGEHEL--SILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 HASDQTLRG-VRGNKIAMIFQEPMVsLNPLHTLEKqlYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLS 158
Cdd:PRK10584 75 HQMDEEARAkLRAKHVGFVFQSFML-IPTLNALEN--VELPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHN 216
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-273 |
1.78e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPpveyLSGDIRFHGESLLHASD 83
Cdd:PRK11231 1 MTLRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL-TP----QSGTVFLGDKPISMLSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLrgvrGNKIAMIFQEPMVslnPLHTLEKQLYEV-----LSLHrGMRREAARGEILNCLDRVGIRQ-AAKRLTDyphqL 157
Cdd:PRK11231 72 RQL----ARRLALLPQHHLT---PEGITVRELVAYgrspwLSLW-GRLSAEDNARVNQAMEQTRINHlADRRLTD----L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElnmGMLFIT--HNLSIVRKLAHRVAVMQNGRC 235
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ---GKTVVTvlHDLNQASRYCDHLVVLANGHV 216
|
250 260 270
....*....|....*....|....*....|....*...
gi 16130118 236 VEQnyaatlfASPTHPYTQKLLNSEPSGDPVPLPEPAS 273
Cdd:PRK11231 217 MAQ-------GTPEEVMTPGLLRTVFDVEAEIHPEPVS 247
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
297-508 |
1.88e-24 |
|
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: 107.52 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDpnssl 375
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQhGQVLVDGVDLAIADPAWL---RRQMGVVLQE----- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprlNVL--QIIEEGLRVHQPTLSaaqrEQQVIAVMHEVGLDP---ETRHRYPAE-------FSGGQRQRIAIARALILK 443
Cdd:TIGR01846 540 ----NVLfsRSIRDNIALCNPGAP----FEHVIHAAKLAGAHDfisELPQGYNTEvgekganLSGGQRQRIAIARALVGN 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-519 |
2.02e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.53 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHAS--DQTLRGvrgnkIAMIFQEpmvs 104
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPD----AGSILIDGQEMRFASttAALAAG-----VAIIYQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 lnpLHTL-EKQLYEVLSL----HRG--MRREAARGEILNCLDRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLtRPEL 177
Cdd:PRK11288 88 ---LHLVpEMTVAENLYLgqlpHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKY---LSIGQRQMVEIAKALA-RNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 178 LIA-DEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEqnyaatlfaspTHPYTQKL 256
Cdd:PRK11288 161 VIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA-----------TFDDMAQV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 257 ----LNSEPSG---------DPVPLPEPASTLLDVEQLQVAFPirkgilkrivdhnvvvknISFTLRAGETLGLVGESGS 323
Cdd:PRK11288 229 drdqLVQAMVGreigdiygyRPRPLGEVRLRLDGLKGPGLREP------------------ISFSVRAGEIVGLFGLVGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 324 GKSttglALLRLI-----NSQGSIIFDGQPLQNLNRRQllPIRHRIQVVFQD-------PNSSLNPRLNVlqiieeGLRV 391
Cdd:PRK11288 291 GRS----ELMKLLygatrRTAGQVYLDGKPIDIRSPRD--AIRAGIMLCPEDrkaegiiPVHSVADNINI------SARR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 392 HQPTLSA---AQREQQvIAVMHEVGLDPETRHRYPA--EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILT 466
Cdd:PRK11288 359 HHLRAGClinNRWEAE-NADRFIRSLNIKTPSREQLimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYN 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 467 LLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVeqGPCARVFATPQQ 519
Cdd:PRK11288 438 VIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAREQATERQ 487
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
299-504 |
2.09e-24 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 99.98 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQLlpirhriqvvfqdpns 373
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKST----LARLIlgllrPTSGRVRLDGADISQWDPNEL---------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 slnprlnvlqiieeglrvhqptlsaaqrEQQVIAVMHEVGLDPETrhryPAE--FSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03246 75 ----------------------------GDHVGYLPQDDELFSGS----IAEniLSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 452 PTSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVrALCHQVIILRQGEV 504
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
301-517 |
3.84e-24 |
|
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: 100.70 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQllpiRHRIQVVFQDPNSSLNPRL 379
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGKILLDGQDITKLPMHK----RARLGIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 NVLQIIEEGLRVHqpTLSAAQREQQVIAVMHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
Cdd:cd03218 91 TVEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 460 VQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:cd03218 168 AVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-234 |
3.91e-24 |
|
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: 100.17 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLHASDQTLRGVRgNKIAMIFQE 100
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKS-TLLKLIykEELPT------SGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 101 pmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKrltDYPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03292 87 --FRLLPDRNVYENVAFALEVTGVPPREIRK-RVPAALELVGLSHKHR---ALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 181 DEPTTALDVSVQAQILQLLRELQgelNMG--MLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKIN---KAGttVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
289-504 |
3.98e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.68 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIvDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNlnrrqllpIRHR 363
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLagletPSAGELLAGTAPLAE--------ARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDpnSSLNPRLNVLQIIEEGLRVHQptlsaaqrEQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:PRK11247 83 TRLMFQD--ARLLPWKKVIDNVGLGLKGQW--------RDAALQALAAVGLA-DRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-252 |
4.17e-24 |
|
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: 102.96 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 40 LVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQtLRGvrgnkIAMIFQEpmVSLNPLHTLEKQLYEVL 119
Cdd:TIGR01187 1 LLGPSGCGKT-TLLRLLAGFEQPD----SGSIMLDGEDVTNVPPH-LRH-----INMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 120 SLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLL 199
Cdd:TIGR01187 68 KM-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 200 RELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPY 252
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-234 |
4.33e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.49 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLlhaSDQTLRGV------RGnki 94
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPD------SGEVLWDGEPL---DPEDRRRIgylpeeRG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 95 amifqepmvsLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTR 174
Cdd:COG4152 82 ----------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKVE---ELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 175 PELLIADEPTTALD-VSVQAqILQLLRELQGElnmG--MLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:COG4152 148 PELLILDEPFSGLDpVNVEL-LKDVIRELAAK---GttVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-234 |
5.03e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 100.27 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLlhasd 83
Cdd:cd03263 1 LQIRNLTK--TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLtgELRPT------SGTAYINGYSI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMIFQEPMvsLNPLHTLEKQLYeVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQ 163
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDA--LFDELTVREHLR-FYARLKGLPKSEIKEEVELLLRVLGLTDKANKRA---RTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-236 |
5.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSPPVEYLSGdirfhgeslLHASD-QTLRGVRgNKIA 95
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDG---------LDTSDeENLWDIR-NKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 96 MIFQEPM-----------VSLNPlhtlekqlyEVLslhrGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQR 164
Cdd:PRK13633 89 MVFQNPDnqivativeedVAFGP---------ENL----GIPPEEIRERVDESLKKVGMYEYRRHA---PHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKlAHRVAVMQNGRCV 236
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
289-518 |
5.23e-24 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 105.29 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIvDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-------QGSIIFDGQPLQNLNRRQLLpiR 361
Cdd:TIGR02633 5 KGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKST----LMKILSGvyphgtwDGEIYWSGSPLKASNIRDTE--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 362 HRIQVVFQDpnSSLNPRLNVLQ-------IIEEGLRVHQPTLSaaQREQqviAVMHEVGLDPETRHRYPAEFSGGQRQRI 434
Cdd:TIGR02633 78 AGIVIIHQE--LTLVPELSVAEniflgneITLPGGRMAYNAMY--LRAK---NLLRELQLDADNVTRPVGDYGGGQQQLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 435 AIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQkHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPcARVF 514
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKD-MSTM 228
|
....
gi 16130118 515 ATPQ 518
Cdd:TIGR02633 229 SEDD 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
297-521 |
5.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQllPIRHRIQVVFQDPNSSL 375
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSKLQ--GIRKLVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprlnVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK13644 91 -----VGRTVEEDLAFGPENLCLPPIEirKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRAlCHQVIILRQGEVVEQGPCARVFATPQQEY 521
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-238 |
5.96e-24 |
|
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: 100.93 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVgfRHQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPVEylSGDIRFHGESLLH 80
Cdd:COG1119 1 DPLLELRNVTV--RRGG--KTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGdlPPTY--GNDVRLFGERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 ASDQTLR---GVRGNKIAMIFQepmVSLNPLHTLEKQLYEVLSLHRG----MRREAARgeilnCLDRVGIRQAAKRLTdy 153
Cdd:COG1119 71 EDVWELRkriGLVSPALQLRFP---RDETVLDVVLSGFFDSIGLYREptdeQRERARE-----LLELLGLAHLADRPF-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 154 pHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNG 233
Cdd:COG1119 141 -GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
....*
gi 16130118 234 RCVEQ 238
Cdd:COG1119 220 RVVAA 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-238 |
6.71e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 99.99 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLLHASDQTL 86
Cdd:cd03254 5 FENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQ------KGQILIDGIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHrgmRREAARGEILNCLDRVGIRQAAKRLTD-YPHQ-------LS 158
Cdd:cd03254 76 R----SMIGVVLQDTFL-------FSGTIMENIRLG---RPNATDEEVIEAAKEAGAHDFIMKLPNgYDTVlgenggnLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQ 238
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
289-509 |
7.15e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHnVVVKNISFTLRAGETLGLVGESGSGKSTTglalLRLIN-----SQGSIIFDGQPLQNLNRRQL--LPiR 361
Cdd:COG4152 5 KGLTKRFGDK-TAVDDVSFTVPKGEIFGLLGPNGAGKTTT----IRIILgilapDSGEVLWDGEPLDPEDRRRIgyLP-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 362 HRiqvvfqdpnsSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALI 441
Cdd:COG4152 79 ER----------GLYPKMKVGEQLVYLARLKG--LSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 442 LKPSLIILDEPTSSLDkTVQAQIL-TLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:COG4152 146 HDPELLILDEPFSGLD-PVNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-504 |
8.00e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 104.70 E-value: 8.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSVGFrhqQTVRTVvNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLlha 81
Cdd:PRK10762 1 MQALLQLKGIDKAF---PGVKAL-SGAALNVYPGRVMALVGENGAGKS-TMMKVLTGIYTRD----AGSILYLGKEV--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 sdqTLRGVRGNK---IAMIFQEpmVSLNPLHTLEKQLY---EVLS-----LHRGMRREAARgeilnCLDRVGIRQAAKRL 150
Cdd:PRK10762 69 ---TFNGPKSSQeagIGIIHQE--LNLIPQLTIAENIFlgrEFVNrfgriDWKKMYAEADK-----LLARLNLRFSSDKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 151 TDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVM 230
Cdd:PRK10762 139 VG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 231 QNGRCVEQNYAATLfaspthpyTQ----------KLLNSEPSGDpvplPEPASTLLDVEQLQVAfpirkGilkrivdhnv 300
Cdd:PRK10762 215 RDGQFIAEREVADL--------TEdsliemmvgrKLEDQYPRLD----KAPGEVRLKVDNLSGP-----G---------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 vVKNISFTLRAGETLGLVGESGSGKSttglALLRLI-----NSQGSIIFDGQPLQNLNRRQLLpiRHRIQVVFQD----- 370
Cdd:PRK10762 268 -VNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLygalpRTSGYVTLDGHEVVTRSPQDGL--ANGIVYISEDrkrdg 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 371 --------PNSSLnPRLNvlQIIEEGLRVHQptlsaaQREQQviAVMHEVGL----DPeTRHRYPAEFSGGQRQRIAIAR 438
Cdd:PRK10762 341 lvlgmsvkENMSL-TALR--YFSRAGGSLKH------ADEQQ--AVSDFIRLfnikTP-SMEQAIGLLSGGNQQKVAIAR 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 439 ALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-505 |
8.97e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 104.49 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 26 NDVSLQIEAGETLALVGESGSGKSvTALSILrllpS---PPVEYlSGDIRFHGE----SLLHASDQtlrgvRGnkIAMIF 98
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKS-TLMKVL----SgvyPHGSY-EGEILFDGEvcrfKDIRDSEA-----LG--IVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 99 QE----PMVSL--NPLHTLEKQLYEVLSLHRGMRREAArgeilnCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALL 172
Cdd:NF040905 85 QElaliPYLSIaeNIFLGNERAKRGVIDWNETNRRARE------LLAKVGLDESPDTLVT---DIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 173 TRPELLIADEPTTALDVSVQAQILQLLRELQGElnmGM--LFITHNLSIVRKLAHRVAVMQNGRCVEqnyaaTLFA---- 246
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQ---GItsIIISHKLNEIRRVADSITVLRDGRTIE-----TLDCrade 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 247 -------------SPTHPYtqkllnsepsgdPVPLPEPASTLLDVEQLQVAFPIRKgilkrivdHNVVVKNISFTLRAGE 313
Cdd:NF040905 228 vtedriirgmvgrDLEDRY------------PERTPKIGEVVFEVKNWTVYHPLHP--------ERKVVDDVSLNVRRGE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 314 TLGLVGESGSGKstTGLALLRLINS-----QGSIIFDGQPLQNLNRRQllPIRHRIQVVFQDpnsslnpR----LNVLQI 384
Cdd:NF040905 288 IVGIAGLMGAGR--TELAMSVFGRSygrniSGTVFKDGKEVDVSTVSD--AIDAGLAYVTED-------RkgygLNLIDD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 385 IEEGLrvhqpTLSAAQR--EQQVIAVMHEVGLDPETRH----RYPAEF------SGGQRQRIAIARALILKPSLIILDEP 452
Cdd:NF040905 357 IKRNI-----TLANLGKvsRRGVIDENEEIKVAEEYRKkmniKTPSVFqkvgnlSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 453 TSSLDKTVQAQILTLLKSL--QQKhqlAYLFISHDLHVVRALCHQVIILRQGEVV 505
Cdd:NF040905 432 TRGIDVGAKYEIYTIINELaaEGK---GVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-255 |
1.06e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.99 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPPVEYLSGDIRFHGESLLHA 81
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKS-TLLRVFnRLIELYPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLRgvrgNKIAMIFQEPmvslNPLHTLekQLYEVLSLHRGMRREA-ARGEILN----CLDRVGIRQAAKRLTDYPH- 155
Cdd:PRK14247 76 DVIELR----RRVQMVFQIP----NPIPNL--SIFENVALGLKLNRLVkSKKELQErvrwALEKAQLWDEVKDRLDAPAg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElnMGMLFITHNLSIVRKLAHRVAVMQNGRC 235
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250 260
....*....|....*....|
gi 16130118 236 VEQNYAATLFASPTHPYTQK 255
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTEK 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
301-517 |
1.33e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.00 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQllpIRHRIQVVFQDpnSSL 375
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTT----LLRAINgtltpTAGTVLVAGDDVEALSARA---ASRRVASVPQD--TSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NPRLNVLQIIEEGLRVHQPTLSAAQR--EQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK09536 89 SFEFDVRQVVEMGRTPHRSRFDTWTEtdRAAVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFIsHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-238 |
1.60e-23 |
|
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: 104.03 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpVEYLSGDIRFHGESLLHASDQTLR 87
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPRF-YEPDSGQILLDGHDLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 gvrgNKIAMIFQEpmvslnpLHTLEKQLYEvlSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQ--------LSG 159
Cdd:TIGR02203 406 ----RQVALVSQD-------VVLFNDTIAN--NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLSG 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQ 238
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVER 548
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-234 |
1.66e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFrHQQTV--RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIRFHGESLLHA 81
Cdd:COG1101 2 LELKNLSKTF-NPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIagSLPPD------SGSILIDGKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQtlrgVRGNKIAMIFQEPMVSLNPLHTLEKQLyeVLSLHRGMRREAARG----------EILNCLDRvGIrqaAKRLT 151
Cdd:COG1101 74 PEY----KRAKYIGRVFQDPMMGTAPSMTIEENL--ALAYRRGKRRGLRRGltkkrrelfrELLATLGL-GL---ENRLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:COG1101 144 TKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMH 223
|
...
gi 16130118 232 NGR 234
Cdd:COG1101 224 EGR 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
1.75e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.86 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSVGFRHQQTVRtvvnDVSLQIEAGETLALVGESGSGKSvtalSILR-------LLPSPPVEylsGDIRFH 74
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVK----NVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRVE---GKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 75 GESLlHASDQTLRGVRgNKIAMIFQEPmvslNPLhtlEKQLYEVLSLhrGMRREAARGEILNCLDRvGIRQAA------K 148
Cdd:PRK14243 76 GKNL-YAPDVDPVEVR-RRIGMVFQKP----NPF---PKSIYDNIAY--GARINGYKGDMDELVER-SLRQAAlwdevkD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 149 RLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNmgMLFITHNLsivrKLAHRVA 228
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT--IIIVTHNM----QQAARVS 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 16130118 229 VM-------------QNGRCVEQNYAATLFASPTHPYTQ 254
Cdd:PRK14243 218 DMtaffnveltegggRYGYLVEFDRTEKIFNSPQQQATR 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-234 |
1.80e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 99.75 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVEYLSGDIRFHGESLLHASD 83
Cdd:PRK11247 11 TPLLLNAVSKRYGE----RTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAG--LETPSAGELLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRgvrgnkiaMIFQEpmVSLNPLhtleKQLYEVLSLH-RGMRREAArgeiLNCLDRVGIrqaAKRLTDYPHQLSGGER 162
Cdd:PRK11247 81 EDTR--------LMFQD--ARLLPW----KKVIDNVGLGlKGQWRDAA----LQALAAVGL---ADRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-255 |
1.84e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.74 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppVEYLSGDIRFHGESLLHASDQ-TLRGVRGNK-IAMIFQ 99
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKS-TLLKVLNRL----IEIYDSKIKVDGKVLYFGKDIfQIDAIKLRKeVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EPmvslNPLHTLE--KQLYEVLSLHRGMRREAARGEILNCLDRVGI-RQAAKRLTDYPHQLSGGERQRVMIAMALLTRPE 176
Cdd:PRK14246 98 QP----NPFPHLSiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 177 LLIADEPTTALDVSVQAQILQLLRELQGElnMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQK 255
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-259 |
1.89e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQ 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQPT----AGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TlrgvrgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRRE-AARGEILncLDRVGIRQAAKRltdYPHQLSGGERQ 163
Cdd:PRK11607 90 Q------RPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEiASRVNEM--LGLVHMQEFAKR---KPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSV----QAQILQLLRELQGELNMgmlfITHNLSIVRKLAHRVAVMQNGRCVEQN 239
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERVGVTCVM----VTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250 260
....*....|....*....|
gi 16130118 240 YAATLFASPTHPYTQKLLNS 259
Cdd:PRK11607 233 EPEEIYEHPTTRYSAEFIGS 252
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-527 |
1.94e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 100.17 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKsTTGLALLRLINSQ-------GSIIFDGQPLqnLNRRQLLPIRHRIQVVFQDPNS 373
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGK-TTFLRTLNRMNDKvsgyrysGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SlnpRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETRHRY---PAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:PRK14271 113 F---PMSIMDNVLAGVRAHK-LVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKhqLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLA 527
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
296-508 |
2.30e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 296 VDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALL---RLINSQGSIIFDGQPLQNLnrrqllPIRHR----IQVVF 368
Cdd:COG0396 10 VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKYEVTSGSILLDGEDILEL------SPDERaragIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 369 QDP-------NSSLnprlnvLQIIEEGLRvhQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAE-FSGGQRQRIAIARAL 440
Cdd:COG0396 84 QYPveipgvsVSNF------LRTALNARR--GEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 441 ILKPSLIILDEPTSSLD----KTVQAQIltllKSLQQKHQlAYLFISHD---LHVVRAlcHQVIILRQGEVVEQG 508
Cdd:COG0396 156 LLEPKLAILDETDSGLDidalRIVAEGV----NKLRSPDR-GILIITHYqriLDYIKP--DFVHVLVDGRIVKSG 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
300-508 |
2.56e-23 |
|
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: 97.00 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTgLALLR--LINSQGSIIFDGQPLQNLNRRqllpIRHRIQVVFQDP---NSS 374
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTgdLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPylfDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LnpRLNVlqiieeGLRvhqptlsaaqreqqviavmhevgldpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03247 91 L--RNNL------GRR-----------------------------------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRALcHQVIILRQGEVVEQG 508
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-258 |
3.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 7 AIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVEYLSGDIRFHGESLlhaSDQTL 86
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL--PDDNPNSKITVDGITL---TAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RGVRgNKIAMIFQEP-------MVSLNPLHTLEkqlyevlslHRGMRREAARGEILNCLDRVGirqaakrLTDY----PH 155
Cdd:PRK13640 80 WDIR-EKVGIVFQNPdnqfvgaTVGDDVAFGLE---------NRAVPRPEMIKIVRDVLADVG-------MLDYidsePA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVrKLAHRVAVMQNGRC 235
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
250 260 270
....*....|....*....|....*....|.
gi 16130118 236 VEQNYAATLFASPTH--------PYTQKLLN 258
Cdd:PRK13640 222 LAQGSPVEIFSKVEMlkeigldiPFVYKLKN 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-238 |
3.57e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.78 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpveyLSGDIRFHGESLLHASD 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIAGFLAP----SSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QtlRGVrgnkiamIFQEP--MVSLNPLHTLEkqlyevLSLH-RGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGG 160
Cdd:COG4525 77 D--RGV-------VFQKDalLPWLNVLDNVA------FGLRlRGVPKAERRARAEELLALVGLADFARR---RIWQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQN--GRCVEQ 238
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
274-526 |
4.02e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 274 TLLDVEQLQVAFPIrkgilKRIVDhnvvvkNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNL 352
Cdd:PRK11231 1 MTLRTENLTVGYGT-----KRILN------DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 353 NRRQL------LPIRHriqvvfqdpnssLNPrlnvlqiieEGLRVHQ-------PTLS-----AAQREQQVIAVMHEVGL 414
Cdd:PRK11231 70 SSRQLarrlalLPQHH------------LTP---------EGITVRElvaygrsPWLSlwgrlSAEDNARVNQAMEQTRI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 415 DpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQ--KHQLAYLfisHDLHVVRAL 492
Cdd:PRK11231 129 N-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgKTVVTVL---HDLNQASRY 204
|
250 260 270
....*....|....*....|....*....|....
gi 16130118 493 CHQVIILRQGEVVEQGpcarvfaTPQQEYTRQLL 526
Cdd:PRK11231 205 CDHLVVLANGHVMAQG-------TPEEVMTPGLL 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
289-508 |
5.42e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 97.79 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQ-PLQNlnRRQLLpirHRIQV 366
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGLvPWKR--RKKFL---RRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPNS---SLNPRlnvlqiieEGLRVHQPT--LSAAQREQQV--IAVMHEVG--LDPETRhrypaEFSGGQRQRIAIA 437
Cdd:cd03267 99 VFGQKTQlwwDLPVI--------DSFYLLAAIydLPPARFKKRLdeLSELLDLEelLDTPVR-----QLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 438 RALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-246 |
6.94e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLLHaSDQTLRGVRGNkIAMIFQEPMV 103
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPS------SGRILFDGKPIDY-SRKGLMKLRES-VGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 SLNPLHTLEKQLYEVLSLhrGMRREAARGEILNCLDRVGIrqaaKRLTDYP-HQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:PRK13636 94 QLFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 183 PTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFA 246
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
301-508 |
6.97e-23 |
|
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: 96.71 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPN-SSLNPR 378
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL---RSSLTIIPQDPTlFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNvLQIIEEglrvhqptlsaaQREQQVIAVMH--EVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:cd03369 100 SN-LDPFDE------------YSDEEIYGALRvsEGGLN----------LSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 457 DKTVQAQILTLLKSLQQKHQLayLFISHDLHVVrALCHQVIILRQGEVVEQG 508
Cdd:cd03369 157 DYATDALIQKTIREEFTNSTI--LTIAHRLRTI-IDYDKILVMDAGEVKEYD 205
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
301-509 |
7.60e-23 |
|
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: 102.71 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGlallRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDpnssl 375
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIPREEIPREVL---ANSVAMVDQD----- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nprLNVLQ-IIEEGLRVHQPTLSAAQREQQVI-AVMHEV------GLDPETrhrypAE----FSGGQRQRIAIARALILK 443
Cdd:TIGR03796 562 ---IFLFEgTVRDNLTLWDPTIPDADLVRACKdAAIHDVitsrpgGYDAEL-----AEgganLSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKslqqKHQLAYLFISHDLHVVRAlCHQVIILRQGEVVEQGP 509
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGT 694
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-524 |
7.84e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRL------INSQGSIIFDGQPLQ----NLNRrqllpIRHRIQV 366
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneleseVRVEGRVEFFNQNIYerrvNLNR-----LRRQVSM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPN----------------SSLNPRLNVLQIIEEGLRvhqptlsAAQREQQVIAVMHEVGLDpetrhrypaeFSGGQ 430
Cdd:PRK14258 93 VHPKPNlfpmsvydnvaygvkiVGWRPKLEIDDIVESALK-------DADLWDEIKHKIHKSALD----------LSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIIL-----RQGEVV 505
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLV 235
|
250
....*....|....*....
gi 16130118 506 EQGPCARVFATPQQEYTRQ 524
Cdd:PRK14258 236 EFGLTKKIFNSPHDSRTRE 254
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
289-508 |
8.35e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 96.58 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHNVVvKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINS-QGSIIFDGQPLQNLnrrqllpIRHRIQVV 367
Cdd:cd03269 4 ENVTKRFGRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGKPLDIA-------ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 368 FQDpnSSLNPRLNVLQIIEEGLRVHQPTLSAAQReqQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:cd03269 76 PEE--RGLYPKMKVIDQLVYLAQLKGLKKEEARR--RIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-237 |
9.01e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 9.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfrhqqTV--RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILrllPSPPVEYLSGDIRFHGESLLHAS- 82
Cdd:COG0396 1 LEIKNLHV------SVegKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM---GHPKYEVTSGSILLDGEDILELSp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQtlRGVRGnkIAMIFQEPM----VSL-NPLHT-LEKQLYEVLSLhrgmrrEAARGEILNCLDRVGIRQA-AKRltDYPH 155
Cdd:COG0396 72 DE--RARAG--IFLAFQYPVeipgVSVsNFLRTaLNARRGEELSA------REFLKLLKEKMKELGLDEDfLDR--YVNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIA-MALLtRPELLIADEPTTALDV-SVQAqILQLLRELQGElNMGMLFITHNLSIVRKL-AHRVAVMQN 232
Cdd:COG0396 140 GFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRILDYIkPDFVHVLVD 216
|
....*
gi 16130118 233 GRCVE 237
Cdd:COG0396 217 GRIVK 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-286 |
1.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVEYLS-GDIRFHGESllhaSDQTLRGVRgNKIAMIFQEPmv 103
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKS-TLIQNINALLKPTTGTVTvDDITITHKT----KDKYIRPVR-KRIGMVFQFP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 slnplhtlEKQLYEVlSLHR---------GMRREAARGEILNCLDRVGIRQAAKRLTdyPHQLSGGERQRVMIAMALLTR 174
Cdd:PRK13646 95 --------ESQLFED-TVEReiifgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQS--PFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 175 PELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASpthpyTQ 254
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD-----KK 238
|
250 260 270
....*....|....*....|....*....|...
gi 16130118 255 KLLNSEpsgdpVPLPEPASTLLDVEQ-LQVAFP 286
Cdd:PRK13646 239 KLADWH-----IGLPEIVQLQYDFEQkYQTKLK 266
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-273 |
1.56e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQ 84
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPT----SGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRGNKIAMIFQEpmVSLNPlHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164
Cdd:PRK10535 79 ALAQLRREHFGFIFQR--YHLLS-HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQnyaatl 244
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN------ 224
|
250 260
....*....|....*....|....*....
gi 16130118 245 faSPTHPytqkllNSEPSGDPVPLPEPAS 273
Cdd:PRK10535 225 --PPAQE------KVNVAGGTEPVVNTAS 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-244 |
1.61e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 29 SLQIEAGETLALVGESGSGKSvTALSILR--LLPSppveylSGDIRFHGEsllhasDQTLRGVRGNKIAMIFQEPmvSLN 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIAgfLTPA------SGSLTLNGQ------DHTTTPPSRRPVSMLFQEN--NLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 107 PLHTLEKQLyeVLSLHRGMRREAA-RGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK10771 84 SHLTVAQNI--GLGLNPGLKLNAAqREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 186 ALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
260-502 |
1.63e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 260 EPSGDPVPLPEPASTLLDVEQLQVAFPirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-- 337
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRTP----------DGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRAIAgl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 338 ---SQGSIIF-DGQ-----------PLQNLnRRQLLPirhriqvvfqdpnsslnprlnvlqiieeglrvhqPTLSAAQRE 402
Cdd:COG4178 413 wpyGSGRIARpAGArvlflpqrpylPLGTL-REALLY----------------------------------PATAEAFSD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 403 QQVIAVMHEVGLDP-----ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKslQQKHQL 477
Cdd:COG4178 458 AELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGT 535
|
250 260
....*....|....*....|....*
gi 16130118 478 AYLFISHDlHVVRALCHQVIILRQG 502
Cdd:COG4178 536 TVISVGHR-STLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
304-518 |
1.72e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKST-----TGLallrLINSQGSI-IFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNP 377
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPSSGTItIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RlNVLQIIEEGLRvhqpTLSAAQREQQVIAV--MHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PRK13641 101 N-TVLKDVEFGPK----NFGFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 456 LDKTVQAQILTLLKSLQQKHQLAYLfISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-246 |
1.85e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.05 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSVGFRHQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGE 76
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLtrawdPQ------QGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 77 SLLHASDQTLRgvrgNKIAMIFQEPMVsLNplHTLEKQLyeVLSLHrgmrrEAARGEILNCLDRVGIR---QAAKRLT-- 151
Cdd:PRK11160 403 PIADYSEAALR----QAISVVSQRVHL-FS--ATLRDNL--LLAAP-----NASDEALIEVLQQVGLEkllEDDKGLNaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 --DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLsivRKLAH--RV 227
Cdd:PRK11160 469 lgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRL---TGLEQfdRI 543
|
250
....*....|....*....
gi 16130118 228 AVMQNGRCVEQNYAATLFA 246
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLA 562
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-262 |
1.99e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSV-----TALsilrLLPSppveylSGDIRFHGESL-LHASDQTLRGVRgNKIAMIF 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPS------SGTITIAGYHItPETGNKNLKKLR-KKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 99 QEPmvslnplhtlEKQLYE--VLS------LHRGMRREAARGEILNCLDRVGIRQAAkrLTDYPHQLSGGERQRVMIAMA 170
Cdd:PRK13641 92 QFP----------EAQLFEntVLKdvefgpKNFGFSEDEAKEKALKWLKKVGLSEDL--ISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLfITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTh 250
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE- 237
|
250
....*....|..
gi 16130118 251 pYTQKLLNSEPS 262
Cdd:PRK13641 238 -WLKKHYLDEPA 248
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-233 |
2.27e-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: 95.61 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHAsdqtlrgvrGNKIAMIFQEpmVS 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQPT----SGGVILEGKQITEP---------GPDRMVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKQLY-EVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:TIGR01184 65 LLPWLTVRENIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130118 184 TTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNG 233
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-247 |
2.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGESLLHASDQ 84
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF-----EEFEGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRgvrgNKIAMIFQEPMVSLNPLhTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164
Cdd:PRK13642 78 NLR----RKIGMVFQNPDNQFVGA-TVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
...
gi 16130118 245 FAS 247
Cdd:PRK13642 228 FAT 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
301-509 |
3.37e-22 |
|
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: 100.18 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSL- 375
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEpDSGQILLDGHDLADYTLASL---RRQVALVSQDVvlfNDTIa 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 ------NPRLNVLQIIEEGLrvhqptlsAAQREQQVIAVMHEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:TIGR02203 424 nniaygRTEQADRAEIERAL--------AAAYAQDFVDKLPL-GLDTPIGEN-GVLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHqlAYLFISHDLHVVRAlCHQVIILRQGEVVEQGP 509
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-249 |
3.94e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.63 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTV---RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFhGESLLHA--SDQTLR 87
Cdd:PRK13634 8 VEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKS-TLLQHLNGLLQPT----SGTVTI-GERVITAgkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQEPmvslnplhtlEKQLYE--VLS------LHRGMRREAARGEILNCLDRVGIRQAAkrLTDYPHQLSG 159
Cdd:PRK13634 82 PLR-KKVGIVFQFP----------EHQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGLPEEL--LARSPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQN 239
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
250
....*....|
gi 16130118 240 YAATLFASPT 249
Cdd:PRK13634 229 TPREIFADPD 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-201 |
5.17e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.50 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILR----LLPsppveYLSGDIRFHgesllha 81
Cdd:COG4178 363 LALEDLTLRTPDG---RPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWP-----YGSGRIARP------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 sdqtlrgvRGNKIAMIFQEPMVslnPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIRQAAKRL---TDYPHQLS 158
Cdd:COG4178 424 --------AGARVLFLPQRPYL---PLGTLREAL-----LYPATAEAFSDAELREALEAVGLGHLAERLdeeADWDQVLS 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
304-514 |
5.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNR-RQLLPIRHRIQVVFQDPNSSLNP 377
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKST----IMQLLNglhvpTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RlNVLQIIEEGLR---VHQPTLSAAQREQqviavMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK13649 101 E-TVLKDVAFGPQnfgVSQEEAEALAREK-----LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 455 SLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVF 514
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-247 |
6.33e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.86 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESLLHASDQTLRgvrgN 92
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-----NGRVLVDGHDLALADPAWLR----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 93 KIAMIFQEPMVslnplhtLEKQLYEVLSLHR-GMRREaargEILNCLDRVGIRQAAKRLTDYPHQ--------LSGGERQ 163
Cdd:cd03252 77 QVGVVLQENVL-------FNRSIRDNIALADpGMSME----RVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQNYAAT 243
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDE 222
|
....
gi 16130118 244 LFAS 247
Cdd:cd03252 223 LLAE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
7.49e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.88 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGfrhqqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppveYLSGDIRFHGESLLHASd 83
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPVTRRS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 qtLRGVRGNKIAMIFQEPMVS-LNPLHTLekqlYEVLSLhrgmrreaargeilncldrvgirqaakrltdyPHQLSGGER 162
Cdd:cd03215 69 --PRDAIRAGIAYVPEDRKREgLVLDLSV----AENIAL--------------------------------SSLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-248 |
7.90e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.14 E-value: 7.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSVTAL---SILRllPSppveylSGDIRFHGESLLHaSDQTLRGVRgNKIAMIFQE 100
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLhfnGILK--PT------SGEVLIKGEPIKY-DKKSLLEVR-KTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 101 PMVSLNPLHTLEKQLYEVLSLhrGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK13639 87 PDDQLFAPTVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 181 DEPTTALDVSVQAQILQLLRELQGElnmGMLFI--THNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASP 248
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKE---GITIIisTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-236 |
8.61e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 93.59 E-value: 8.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQ 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKT-TTLRMLAGLLEPD----AGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLR--GVRGNKIAmifqepmvsLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGER 162
Cdd:cd03266 76 ARRrlGFVSDSTG---------LYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
301-527 |
8.65e-22 |
|
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: 94.13 E-value: 8.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNL--NRRqllpIRHRIQVVFQdpNSSLNP 377
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPvKSGSIRLDGEDITKLppHER----ARAGIAYVPQ--GREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RLNVLQIIEEGLRVHqptlsaAQREQQVIAVMHEvgLDP---ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:TIGR03410 89 RLTVEENLLTGLAAL------PRRSRKIPDEIYE--LFPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVfatpQQEYTRQLLA 527
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-220 |
8.99e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 8.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILrllpsppveylsgdirfhgeSLLHASD 83
Cdd:PRK09544 3 SLVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL--------------------GLVAPDE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMIFQEpmVSLNPlhTLEKQLYEVLSLHRGMRReaarGEILNCLDRVgirQAAKrLTDYPHQ-LSGGER 162
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPGTKK----EDILPALKRV---QAGH-LIDAPMQkLSGGET 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIV 220
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
273-522 |
1.05e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.46 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFPIRKGIlkrivdhnvvvKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ----------GSI 342
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKAL-----------NSVSLDFYPNEITALIGPSGSGKST----LLRSINRMndlnpevtitGSI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 343 IFDGQPLQNlNRRQLLPIRHRIQVVFQDPNSSlnPrLNVLQIIEEGLRVH----QPTLSAA-QREQQVIAVMHEVgldPE 417
Cdd:PRK14239 68 VYNGHNIYS-PRTDTVDLRKEIGMVFQQPNPF--P-MSIYENVVYGLRLKgikdKQVLDEAvEKSLKGASIWDEV---KD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 418 TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRALCHQVI 497
Cdd:PRK14239 141 RLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|....*
gi 16130118 498 ILRQGEVVEQGPCARVFATPQQEYT 522
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
304-514 |
1.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSI-IFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNP 377
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKST----LLQHLNgllqpTEGKVtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RlNVLQIIEEGLRvhqpTLSAAQREQQVIAV--MHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PRK13643 100 E-TVLKDVAFGPQ----NFGIPKEKAEKIAAekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 456 LDKTVQAQILTLLKSLQQKHQLAYLfISHDLHVVRALCHQVIILRQGEVVEQGPCARVF 514
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
256-486 |
1.16e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.20 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 256 LLNSEPSGDPVPLPEPASTLLDVEQLQVafpirKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRL 335
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKPTLEL-----RDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 336 IN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPN---SSlnprlnvlqiIEEGLRVHQPTLSaaqrEQQVIAVMHE 411
Cdd:TIGR02868 385 LDpLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAHlfdTT----------VRENLRLARPDAT----DEELWAALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 412 VGLDPETR----------HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL-TLLKSLQQKhqlAYL 480
Cdd:TIGR02868 448 VGLADWLRalpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSGR---TVV 524
|
....*.
gi 16130118 481 FISHDL 486
Cdd:TIGR02868 525 LITHHL 530
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-245 |
1.18e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.82 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGESLlhaSDQTLR 87
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE-----KVKSGEIFYNNQAI---TDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQEP-------MVSLNPLHTLEKQLYEvlslHRGMRREAARgeilnCLDRVGIRQAAkrltDY-PHQLSG 159
Cdd:PRK13648 80 KLR-KHIGIVFQNPdnqfvgsIVKYDVAFGLENHAVP----YDEMHRRVSE-----ALKQVDMLERA----DYePNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHrVAVMQNGRCVEQN 239
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEG 224
|
....*.
gi 16130118 240 YAATLF 245
Cdd:PRK13648 225 TPTEIF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-515 |
1.45e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFPIRKGI---LKRIV--------DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN---- 337
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPsrsLKELLlrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKST----LLKLIAgile 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 338 -SQGSIIFDGqplqnlnrrqllpirhRIqvvfqdpnSSLnprlnvlqiIEEGLRVHqPTLSAaqREQ-QVIAVMHevGLD 415
Cdd:COG1134 78 pTSGRVEVNG----------------RV--------SAL---------LELGAGFH-PELTG--RENiYLNGRLL--GLS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 416 P-ETRHRYP--AEFSG--------------GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlA 478
Cdd:COG1134 120 RkEIDEKFDeiVEFAElgdfidqpvktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-T 198
|
250 260 270
....*....|....*....|....*....|....*..
gi 16130118 479 YLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:COG1134 199 VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-227 |
1.53e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpveyLSGdirfhgesllhasdqTLRGVRGNKIAMIFQEP 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKS-TLLKVLAGVLRP----TSG---------------TVRRAGGARVAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVSlnplHTLEKQLYEVLSL----HRGMRRE---AARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTR 174
Cdd:NF040873 65 EVP----DSLPLTVRDLVAMgrwaRRGLWRRltrDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 175 PELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRV 227
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-238 |
1.77e-21 |
|
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: 97.97 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGESLLHASDQTLR 87
Cdd:COG5265 363 VSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVT------SGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVrgnkIAMIFQEPmVSLNplHTLEkqlYEVlslhRGMRREAARGEIlncldrvgiRQAAK--RLTDY----PHQ----- 156
Cdd:COG5265 432 AA----IGIVPQDT-VLFN--DTIA---YNI----AYGRPDASEEEV---------EAAARaaQIHDFieslPDGydtrv 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqgELNMGMLFITHNLS-IVRklAHRVAV 229
Cdd:COG5265 489 gerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLStIVD--ADEILV 564
|
....*....
gi 16130118 230 MQNGRCVEQ 238
Cdd:COG5265 565 LEAGRIVER 573
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-229 |
2.50e-21 |
|
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: 97.36 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALS-ILRLLPSPpveylSGDIRFHGESLLHASDQ 84
Cdd:TIGR02857 322 LEFSGVSVAYPGR---RPALRPVSFTVPPGERVALVGPSGAGKS-TLLNlLLGFVDPT-----EGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGvrgnKIAMIFQEPmvslnplHTLEKQLYEVLSLHRgmrREAARGEILNCLDRVGIRQAAK--------RLTDYPHQ 156
Cdd:TIGR02857 393 SWRD----QIAWVPQHP-------FLFAGTIAENIRLAR---PDASDAEIREALERAGLDEFVAalpqgldtPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKLAHRVAV 229
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
301-517 |
2.58e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQllpIRHRIQVVFQDPNSSL 375
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKST----LFRHFNgilkpTSGSVLIRGEPITKENIRE---VRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 -NPrlNVLQIIEEGlrvhqPT---LSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK13652 92 fSP--TVEQDIAFG-----PInlgLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
302-505 |
2.74e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.63 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLN 376
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKST----LLKLIcgierPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRL--NV-LQIIEEGLrvhqptlSAAQREQQVIAVMHEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK10908 94 RTVydNVaIPLIIAGA-------SGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 454 SSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVRALCHQVIILRQGEVV 505
Cdd:PRK10908 166 GNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-519 |
3.77e-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: 92.22 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 307 FTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQnlnrrqllPIRHRIQVVFQDPNSSLNPRLNVLQII 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIpPAKGTVKVAGASPG--------KGWRHIGYVPQRHEFAWDFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 386 EEGLRVHQPTLSAAQREQ--QVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ 463
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADfaAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 464 ILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILrQGEVVEQGpcarvfaTPQQ 519
Cdd:TIGR03771 152 LTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADG-------TPQQ 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-248 |
3.98e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRL---LPSPPveylSGDIRFHGEsllhasDQTLRGVRGNKIAMIFQ 99
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLvagLEKPT----EGQIFIDGE------DVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 E----PMVSL--NPLHTLEKQlyevlslhrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLT 173
Cdd:PRK11432 86 SyalfPHMSLgeNVGYGLKML---------GVPKEERKQRVKEALELVDLAGFEDRYVD---QISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 174 RPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASP 248
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
301-517 |
4.65e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.71 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLnrrQLLPIRHRIQVVFQDP---- 371
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKST----LLSLIQrhfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPflfs 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 -----NSSLNPRLNVLQIIEEGLR---VHQPTLSAAQreqqviavmhevGLDPETRHRyPAEFSGGQRQRIAIARALILK 443
Cdd:PRK10789 403 dtvanNIALGRPDATQQEIEHVARlasVHDDILRLPQ------------GYDTEVGER-GVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 444 PSLIILDEPTSSLDKTVQAQIltlLKSLQQKHQLAYLFIShdLHVVRAL--CHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIIS--AHRLSALteASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-215 |
5.02e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.39 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppVEYLSGDIRFHGESLLHASDQT 85
Cdd:COG4136 2 LSLENLTI-TLGG---RPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAI-------AGTLSPAFSASGEVLLNGRRLT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGNKIAMIFQEPMvsLNPLHTLEKQLyeVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRV 165
Cdd:COG4136 70 ALPAEQRRIGILFQDDL--LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQRARV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITH 215
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
301-523 |
6.78e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNrrqllPIRHRIQVVFQdpNSSL 375
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAgleriTSGEIWIGGRVVNELE-----PADRDIAMVFQ--NYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PRK11650 88 YPHMSVRENMAYGLKIRG--MPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 456 LDKTVQAQILTLLKSLQQKHQLAYLFISHDLhvVRA--LCHQVIILRQGeVVEQgpcarvFATPQQEYTR 523
Cdd:PRK11650 165 LDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQ--VEAmtLADRVVVMNGG-VAEQ------IGTPVEVYEK 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-236 |
8.85e-21 |
|
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: 90.30 E-value: 8.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQT--VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLlpspPVEYLSGDIRFHGESLlha 81
Cdd:cd03213 4 LSFRNLTVTVKSSPSksGKQLLKNVSGKAKPGELTAIMGPSGAGKS-TLLNALagRR----TGLGVSGEVLINGRPL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLRGvrgnKIAMIFQEPMVslnpLHTLekQLYEVLSLHRGMRreaargeilncldrvgirqaakrltdyphQLSGGE 161
Cdd:cd03213 76 DKRSFRK----IIGYVPQDDIL----HPTL--TVRETLMFAAKLR-----------------------------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqGELNMGMLFITHNLSI-VRKLAHRVAVMQNGRCV 236
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSeIFELFDKLLLLSQGRVI 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-234 |
9.78e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLRGVRgNKIAMIFQEP 101
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERPS----AGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVslnplhTLEKQLYEVLSLH---RGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK10908 89 HL------LMDRTVYDNVAIPliiAGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 179 IADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-249 |
1.46e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGESLLHASDQTLRgvrgNKIAMIFQEPmv 103
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-----QPTGGQVLLDGVPLVQYDHHYLH----RQVALVGQEP-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 slnplhtlekQLYEvlslhRGMRREAARGeiLNCLDRVGIRQAAKR------LTDYPH-----------QLSGGERQRVM 166
Cdd:TIGR00958 565 ----------VLFS-----GSVRENIAYG--LTDTPDEEIMAAAKAanahdfIMEFPNgydtevgekgsQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 167 IAMALLTRPELLIADEPTTALDVSVQaQILQLLRELQGelnMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQNYAATLFA 246
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECE-QLLQESRSRAS---RTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
...
gi 16130118 247 SPT 249
Cdd:TIGR00958 703 DQG 705
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
301-508 |
1.81e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.19 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP----NSSL 375
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDIDRHTL---RQFINYLPQEPyifsGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NprlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMHEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:TIGR01193 566 E---NLLLGAKEN--VSQDEIWAACEIAEIKDDIENMPLGYQTElSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 455 SLDKTVQAQILTLLKSLQQKhqlAYLFISHDLHVVRaLCHQVIILRQGEVVEQG 508
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
300-526 |
1.91e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ-----GSIIFDGQPLQNLNRRQLLPIRHRIQVVFQdpNSS 374
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQiapdhGEILFDGENIPAMSRSRLYTVRKRMSMLFQ--SGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHT-QLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEyTRQLL 526
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-234 |
2.62e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 90.08 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLR 87
Cdd:cd03267 20 IGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKT-TTLKILSGLLQPT----SGEVRVAGLVPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 gvrgnKIAMIF-QEPMVS--LNPLHTLE--KQLYEVLSLHRGMRREAArGEILNCldrvgirqaaKRLTDYP-HQLSGGE 161
Cdd:cd03267 95 -----RIGVVFgQKTQLWwdLPVIDSFYllAAIYDLPPARFKKRLDEL-SELLDL----------EELLDTPvRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
299-524 |
2.88e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLR-------LINS---QGSIIFDGQplqNLNRRQLLP--IRHRIQV 366
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKST----ILRcfnrlndLIPGfrvEGKVTFHGK---NLYAPDVDPveVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 VFQDPNS---------SLNPRLNVLQ-----IIEEGLRvhqptlsAAQREQQVIAVMHEVGLdpetrhrypaEFSGGQRQ 432
Cdd:PRK14243 96 VFQKPNPfpksiydniAYGARINGYKgdmdeLVERSLR-------QAALWDEVKDKLKQSGL----------SLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLqqKHQLAYLFISHDLHVVRALCHQVIIL---------RQGE 503
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGY 236
|
250 260
....*....|....*....|.
gi 16130118 504 VVEQGPCARVFATPQQEYTRQ 524
Cdd:PRK14243 237 LVEFDRTEKIFNSPQQQATRD 257
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
289-508 |
2.91e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIVDHnVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQllpiRHRIQVV 367
Cdd:PRK13537 11 RNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARHA----RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 368 FQDPNssLNPRLNVlqiiEEGLRVHQP--TLSAAQREQQVIAVMHEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPS 445
Cdd:PRK13537 86 PQFDN--LDPDFTV----RENLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 446 LIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
301-508 |
3.05e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 88.76 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ-------GSIIFDGQPlqnlnrRQLLPIRHRIQVVFQDpnS 373
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKST----LLNALAGRrtglgvsGEVLINGRP------LDKRSFRKIIGYVPQD--D 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRLNVlqiiEEGLRVhqptlSAAQReqqviavmhevGLdpetrhrypaefSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03213 92 ILHPTLTV----RETLMF-----AAKLR-----------GL------------SGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 454 SSLDKTVQAQILTLLKSLQQK--------HQLAYLFIShdlhvvraLCHQVIILRQGEVVEQG 508
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTgrtiicsiHQPSSEIFE--------LFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
300-517 |
3.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKST-----TGLallrLINSQGSI-----------IFDGQPLQNLNRR--QLLPIR 361
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTlvthfNGL----IKSKYGTIqvgdiyigdkkNNHELITNPYSKKikNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 362 HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMhevGLDPETRHRYPAEFSGGQRQRIAIARALI 441
Cdd:PRK13631 116 RRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKM---GLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLfISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
303-508 |
3.71e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQplqNLNRRQLLPIRHRIQVVFQD--------PNS 373
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGH---DLRDYTLASLRNQVALVSQNvhlfndtiANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRLNVLQI--IEEGLRVHQPTLSAAQREQQVIAVMHEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK11176 437 IAYARTEQYSReqIEEAARMAYAMDFINKMDNGLDTVIGENG----------VLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVRAlCHQVIILRQGEVVEQG 508
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-237 |
4.04e-20 |
|
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: 88.62 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQT 85
Cdd:cd03369 7 IEVENLSV--RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRF-----LEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRgvrgNKIAMIFQEPMV-------SLNPL-HTLEKQLYEVLSLHRGmrreaarGEilncldrvgirqaakrltdyphQL 157
Cdd:cd03369 80 LR----SSLTIIPQDPTLfsgtirsNLDPFdEYSDEEIYGALRVSEG-------GL----------------------NL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKLAhRVAVMQNGRCVE 237
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYD-KILVMDAGEVKE 203
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-234 |
4.61e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 87.66 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVeylSGDIRFHGESLlhasDQT 85
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PT---SGRVRLDGADI----SQW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGNKIAMIFQEpmvslnplhtleKQLYEvlslhrgmrreaarGEILNCLdrvgirqaakrltdyphqLSGGERQRV 165
Cdd:cd03246 70 DPNELGDHVGYLPQD------------DELFS--------------GSIAENI------------------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMgMLFITHNLSIVRkLAHRVAVMQNGR 234
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLA-SADRILVLEDGR 172
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-234 |
5.63e-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: 88.38 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 29 SLQIEAGETLALVGESGSGKSvTALSILRLLPSPpveyLSGDIRFHGESLLHASDQTlrgvrgNKIAMIFQEPmvSLNPL 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEP----ASGSIKVNDQSHTGLAPYQ------RPVSMLFQEN--NLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 109 HTLEKQLyeVLSLHRGMRREAARGE-ILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
Cdd:TIGR01277 85 LTVRQNI--GLGLHPGLKLNAEQQEkVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130118 188 DVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
301-508 |
7.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKST-----TGLallrLINSQGSIIF---DGQPLQNLNR------------------ 354
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlNAL----LLPDTGTIEWifkDEKNKKKTKEkekvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 355 RQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVmheVGLDPETRHRYPAEFSGGQRQRI 434
Cdd:PRK13651 98 KKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIEL---VGLDESYLQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 435 AIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLfISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-249 |
8.04e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQT 85
Cdd:PRK09536 4 IDVSDLSVEFGDT----TVLDGVDLSVREGSLVGLVGPNGAGKT-TLLRAINGTLTPT----AGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LrgvrGNKIAMIFQEPMVSLNplHTLEKQLYEVLSLHRG---MRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGER 162
Cdd:PRK09536 75 A----SRRVASVPQDTSLSFE--FDVRQVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQFADRPVT---SLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFItHNLSIVRKLAHRVAVMQNGRCVEQNYAA 242
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPA 224
|
....*..
gi 16130118 243 TLFASPT 249
Cdd:PRK09536 225 DVLTADT 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-485 |
8.62e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 92.71 E-value: 8.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 30 LQIEAGETLALVGESGSGKSvTALSIL--------------------RLLPSPP-------VEYLSGDIRFHGEsLLHAS 82
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKS-TLMKILngevllddgriiyeqdlivaRLQQDPPrnvegtvYDFVAEGIEEQAE-YLKRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRgvrgnkiaMIFQEPMVS-LNPLhtleKQLYEVLSLHRGMRREAargEILNCLDRVGIrQAAKRLTDyphqLSGGE 161
Cdd:PRK11147 102 HDISH--------LVETDPSEKnLNEL----AKLQEQLDHHNLWQLEN---RINEVLAQLGL-DPDAALSS----LSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELnmgmLFITHNLSIVRKLAHRVAVMQNGRCVE--QN 239
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRIVDLDRGKLVSypGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 240 YAATLfaspthpyTQKllnsepsgdpvplpEPAstlLDVEQLQVA-FP---------IRKGI-------------LK--- 293
Cdd:PRK11147 238 YDQYL--------LEK--------------EEA---LRVEELQNAeFDrklaqeevwIRQGIkarrtrnegrvraLKalr 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 294 ------------------------RIV----------DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ 339
Cdd:PRK11147 293 rerserrevmgtakmqveeasrsgKIVfemenvnyqiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTT----LLKLMLGQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 340 gsiifdgqplqnlnrrqLLPIRHRIQV-------VFQDPNSSLNPRLNVLQIIEEGlrvhQPTLSAAQREQQVIAVMHEV 412
Cdd:PRK11147 369 -----------------LQADSGRIHCgtklevaYFDQHRAELDPEKTVMDNLAEG----KQEVMVNGRPRHVLGYLQDF 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 413 gLDPETRHRYPAE-FSGGQRQRIAIARaLILKPS-LIILDEPTSSLDktvqAQILTLLKSLQQKHQLAYLFISHD 485
Cdd:PRK11147 428 -LFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-236 |
1.06e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 15 FRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSppveylSGDIRFHGeslLHASDQTLRGVRgn 92
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgiLVPT------SGEVRVLG---YVPFKRRKEFAR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 93 KIAMIF---QEPMVSLNPLHTLE--KQLY---------------EVLSLhrgmrreaarGEILNcldrVGIRQaakrltd 152
Cdd:COG4586 96 RIGVVFgqrSQLWWDLPAIDSFRllKAIYripdaeykkrldelvELLDL----------GELLD----TPVRQ------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 153 yphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQN 232
Cdd:COG4586 155 ----LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
....
gi 16130118 233 GRCV 236
Cdd:COG4586 231 GRII 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
289-509 |
1.29e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRivDHNVV--VKNISFTLRAGETLGLVGESGSGKSTT-----GLallrLINSQGSIIFDG-QPLQNlnRRQLLpi 360
Cdd:COG4586 25 KGLFRR--EYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTikmltGI----LVPTSGEVRVLGyVPFKR--RKEFA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 361 rHRIQVVF-QdpNSSLNPRLNVLqiieEGLRVHQ-----PTLSAAQREQQVIAVMhEVG--LDPETRhrypaEFSGGQRQ 432
Cdd:COG4586 95 -RRIGVVFgQ--RSQLWWDLPAI----DSFRLLKaiyriPDAEYKKRLDELVELL-DLGelLDTPVR-----QLSLGQRM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:COG4586 162 RCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-236 |
1.48e-19 |
|
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: 87.26 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 7 AIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESL--LHASDq 84
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS-TLLKLLAGLYKPT----SGSVLLDGTDIrqLDPAD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 tlrgVRGNkIAMIFQEPmvslnplHTLEKQLYEVLSLHRGmrrEAARGEILNCLDRVGIRQAAKRltdYPH--------- 155
Cdd:cd03245 76 ----LRRN-IGYVPQDV-------TLFYGTLRDNITLGAP---LADDERILRAAELAGVTDFVNK---HPNgldlqiger 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNmgMLFITHNLSIVrKLAHRVAVMQNG 233
Cdd:cd03245 138 grGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT--LIIITHRPSLL-DLVDRIIVMDSG 214
|
...
gi 16130118 234 RCV 236
Cdd:cd03245 215 RIV 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-505 |
1.55e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 276 LDVEQLQVAFPirkgilKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQ 350
Cdd:COG1101 2 LELKNLSKTFN------PGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAgslppDSGSILIDGKDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 351 NLN--RRQLLPIRhriqvVFQDPNSSLNPRLNvlqiIEE------------GLRvhqPTLSAAQRE--QQVIAvmhEVGL 414
Cdd:COG1101 72 KLPeyKRAKYIGR-----VFQDPMMGTAPSMT----IEEnlalayrrgkrrGLR---RGLTKKRRElfRELLA---TLGL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 415 DPETRHRYPAEF-SGGQRQRIAIARALILKPSLIILDEPTSSLD-KTvQAQILTLLKSLQQKHQLAYLFISHDLHVVRAL 492
Cdd:COG1101 137 GLENRLDTKVGLlSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKT-AALVLELTEKIVEENNLTTLMVTHNMEQALDY 215
|
250
....*....|...
gi 16130118 493 CHQVIILRQGEVV 505
Cdd:COG1101 216 GNRLIMMHEGRII 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-217 |
2.12e-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: 91.27 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQTVrtvVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESLLHASDQT 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPPV---LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP-----LQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVrgnkIAMIFQEPmvslnplHTLEKQLYEVLSLHRGmrrEAARGEILNCLDRVGIRQAAKRLTDYPH--------QL 157
Cdd:TIGR02868 407 VRRR----VSVCAQDA-------HLFDTTVRENLRLARP---DATDEELWAALERVGLADWLRALPDGLDtvlgeggaRL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQGELNMGMLFITHNL 217
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
300-508 |
2.16e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQ-GSIIFDGQPLQNLNRRQllpIRHRIQVVFQdpNSSLNPR 378
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAhGHVWLDGEHIQHYASKE---VARRIGLLAQ--NATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGLRVHQPTLSAAQREQQ--VIAVMHEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRWRKEDEeaVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 457 DKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
296-485 |
2.29e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 296 VDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-----QGSIIFDGQPLQNLNrrqllPIRHRIQV--VF 368
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKST----LLKIVASlisptSGTLLFEGEDISTLK-----PEIYRQQVsyCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 369 QDP---NSSLNPRLnvlqIIEEGLRVHQPtlsaaqREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPS 445
Cdd:PRK10247 88 QTPtlfGDTVYDNL----IFPWQIRNQQP------DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130118 446 LIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHD 485
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-236 |
2.36e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 15 FRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVEYlSGDIRFHGESLlHASDQTLRGvrgnki 94
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKT-TLMNALAFRSPKGVKG-SGSVLLNGMPI-DAKEMRAIS------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 95 AMIFQEPMvsLNPLHTLEKQLY--EVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQ---LSGGERQRVMIAM 169
Cdd:TIGR00955 102 AYVQQDDL--FIPTLTVREHLMfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQgelNMGMLFIT--HNLSI-VRKLAHRVAVMQNGRCV 236
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA---QKGKTIICtiHQPSSeLFELFDKIILMAEGRVA 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
301-508 |
2.41e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.39 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINS-QGSIIFDGQPLQNL--NRR-QL----LPirhriqvvfQDPn 372
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEDITHLpmHKRaRLgigyLP---------QEA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 sSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:COG1137 88 -SIFRKLTVEDNILAVLELRK--LSKKEREERLEELLEEFGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 453 TSSLD-KTVqAQILTLLKSLQQKhQLAYLfIShDlHVVR---ALCHQVIILRQGEVVEQG 508
Cdd:COG1137 164 FAGVDpIAV-ADIQKIIRHLKER-GIGVL-IT-D-HNVRetlGICDRAYIISEGKVLAEG 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-508 |
2.49e-19 |
|
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: 86.82 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 276 LDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPlq 350
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAgiyppDSGTVTVRGRV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 351 nlnrRQLLpirhriqvvfqDPNSSLNPRLNVLQIIEEGLRVHqptlsaAQREQQVIAVMHEVgldpetrhrypAEFSG-- 428
Cdd:cd03220 86 ----SSLL-----------GLGGGFNPELTGRENIYLNGRLL------GLSRKEIDEKIDEI-----------IEFSElg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 429 ------------GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQV 496
Cdd:cd03220 134 dfidlpvktyssGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRA 212
|
250
....*....|..
gi 16130118 497 IILRQGEVVEQG 508
Cdd:cd03220 213 LVLEKGKIRFDG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-234 |
2.69e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.86 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSILRllpspPVEylSGDIRFHGESLLHA 81
Cdd:COG3845 256 VVLEVENLSVRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSelAEALAGLR-----PPA--SGSIRLDGEDITGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SdqtLRGVRGNKIAMIFQEPM-VSLNPLHTLEKQLyeVLSLHRgmRREAARGEILnclDRVGIRQAAKRL-TDY------ 153
Cdd:COG3845 326 S---PRERRRLGVAYIPEDRLgRGLVPDMSVAENL--ILGRYR--RPPFSRGGFL---DRKAIRAFAEELiEEFdvrtpg 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 154 PHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL--QGelnMGMLFITHNLSIVRKLAHRV 227
Cdd:COG3845 396 PDTparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAG---AAVLLISEDLDEILALSDRI 472
|
....*..
gi 16130118 228 AVMQNGR 234
Cdd:COG3845 473 AVMYEGR 479
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
301-518 |
2.73e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.26 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLI-NSQGSIIFDGQPLQnlnrrqLLPI--RHRIQVVFQDPNSSLNP 377
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVpRDAGNIIIDDEDIS------LLPLhaRARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK10895 92 RLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 458 KTVQAQILTLLKSLQQkHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK10895 170 PISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-484 |
3.23e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 90.46 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 15 FRHQQTvRTVVNDvSLQIEAGETLALVGESGSGKSVTALSILRLLPsppveYLSGDIRFHGESLLHASDQTLRGVrgnkI 94
Cdd:PRK10938 11 FRLSDT-KTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELP-----LLSGERQSQFSHITRLSFEQLQKL----V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 95 AMIFQE---PMVSLNPLHTlEKQLYEVLSLHRgmrREAARGEILNCLdrVGIRQAAKRLTDYphqLSGGERQRVMIAMAL 171
Cdd:PRK10938 80 SDEWQRnntDMLSPGEDDT-GRTTAEIIQDEV---KDPARCEQLAQQ--FGITALLDRRFKY---LSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFAsptHP 251
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ---QA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 252 YTQKLLNSEPSGDpVPLPEPASTLLDvEQLQVAFPirkgilkRIVDHNVVVK--------NISFTLRAGETLGLVGESGS 323
Cdd:PRK10938 227 LVAQLAHSEQLEG-VQLPEPDEPSAR-HALPANEP-------RIVLNNGVVSyndrpilhNLSWQVNPGEHWQIVGPNGA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 324 GKSTtglaLLRLI---NSQG---SIIFDGQplqnlnRR----QLLPIRHRIQVVfqdpNSSL--NPRLN--VLQIIEEG- 388
Cdd:PRK10938 298 GKST----LLSLItgdHPQGysnDLTLFGR------RRgsgeTIWDIKKHIGYV----SSSLhlDYRVStsVRNVILSGf 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 389 ---LRVHQpTLSAAQRE--QQVIAVMhevGLDPETRHRYPAEFSGGQrQRIA-IARALILKPSLIILDEPTSSLDKTVQA 462
Cdd:PRK10938 364 fdsIGIYQ-AVSDRQQKlaQQWLDIL---GIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQ 438
|
490 500
....*....|....*....|..
gi 16130118 463 QILTLLKSLQQKHQLAYLFISH 484
Cdd:PRK10938 439 LVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
305-517 |
3.30e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.91 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 305 ISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLlpIRHRIQVVFQDPNSSLNPrlnVLQI 384
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAEL--ARHRAYLSQQQTPPFAMP---VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 385 ieegLRVHQPTLSAAQREQQVIA-VMHEVGLDPETrHRYPAEFSGGQRQRIAIArALILK--PS------LIILDEPTSS 455
Cdd:PRK03695 90 ----LTLHQPDKTRTEAVASALNeVAEALGLDDKL-GRSVNQLSGGEWQRVRLA-AVVLQvwPDinpagqLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 456 LDKTVQAQILTLLKSLQQKhQLAYLFISHDL-HVVRAlCHQVIILRQGEVVEQGP---------CARVFATP 517
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQ-GIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRrdevltpenLAQVFGVN 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
303-509 |
3.40e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKST--TGLALLRLINS--QGSIIFDGQPLqnlNRRQllpIRHRIQVVFQDpnsSLN-P 377
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTlmNALAFRSPKGVkgSGSVLLNGMPI---DAKE---MRAISAYVQQD---DLFiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RLNVLQ--IIEEGLRVHQpTLSAAQREQQVIAVMHEVGLDP--ETRHRYPAE---FSGGQRQRIAIARALILKPSLIILD 450
Cdd:TIGR00955 113 TLTVREhlMFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 451 EPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
301-509 |
3.83e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglallrLIN--------SQGSIIFDGQPLQNLNRRQLLPIRHR-IQVVFQdp 371
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKST-------LMNilgcldkpTSGTYRVAGQDVATLDADALAQLRREhFGFIFQ-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 nsslnpRLNVLQIIEEGLRVHQPTLSA----AQREQQVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:PRK10535 94 ------RYHLLSHLTAAQNVEVPAVYAglerKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 448 ILDEPTSSLDKTVQAQILTLLKSLQQK-HQLayLFISHDLHVVrALCHQVIILRQGEVVEQGP 509
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRgHTV--IIVTHDPQVA-AQAERVIEIRDGEIVRNPP 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
297-508 |
4.24e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNrrqllPIRHRIQVVFQdp 371
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAglediTSGDLFIGEKRMNDVP-----PAERGVGMVFQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMHEVGLDpetrH---RYPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKL--AGAKKEEINQRVNQVAEVLQLA----HlldRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 449 LDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
301-504 |
4.92e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.79 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpIRHRIQVVFQDpnsslnpRL 379
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpASGEITLDGKPVTRRSPRDA--IRAGIAYVPED-------RK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 nvlqiiEEGLrvhQPTLSaaqreqqviaVMHEVGLdpetrhryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
Cdd:cd03215 86 ------REGL---VLDLS----------VAENIAL--------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16130118 460 VQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
297-508 |
4.97e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.10 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTglaLLRL--IN--SQGSIIFDGQPLQNLNRRQllpIRHRIQVVFQDPN 372
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLngIYlpQRGRVKVMGREVNAENEKW---VRSKVGLVFQDPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPrLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK13647 90 DQVFS-STVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
300-511 |
6.43e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQllpiRHR--IQVVFQDPN 372
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKST----LMKIIagivpPDSGTLEIGGNPCARLTPAK----AHQlgIYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 ssLNPRLNVLQIIEEGLRVHQptlSAAQREQQVIAVMhEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK15439 97 --LFPNLSVKENILFGLPKRQ---ASMQKMKQLLAAL-GCQLDLDSS---AGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCA 511
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-238 |
6.59e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.47 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVEYL-SGDIRFHGESLL 79
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIAG--FETPdSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 HASDQTlRGVRgnkiaMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKRltdYPHQLSG 159
Cdd:PRK09452 80 HVPAEN-RHVN-----TVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQLEEFAQR---KPHQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRcVEQ 238
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQ 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
305-509 |
8.61e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.38 E-value: 8.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 305 ISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpIRHRIQVVFQDPNSSlnpRL 379
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKST----LLKMLGrhqppSEGEILLDAQPLESWSSKAF--ARKVAYLPQQLPAAE---GM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 NVLQIIEEGLRVHQPTL---SAAQREQ--QVIAVmheVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK10575 101 TVRELVAIGRYPWHGALgrfGAADREKveEAISL---VGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 455 SLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
9.36e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.50 E-value: 9.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfrhqqTV--RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsPPVEYLSGDIRFHGESLLHASd 83
Cdd:cd03217 1 LEIKDLHV------SVggKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH---PKYEVTEGEILFKGEDITDLP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGnkIAMIFQEPMvslnplhtlEKQLYEVLSLHRGmrreaargeiLNcldrVGirqaakrltdyphqLSGGERQ 163
Cdd:cd03217 71 PEERARLG--IFLAFQYPP---------EIPGVKNADFLRY----------VN----EG--------------FSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKL-AHRVAVMQNGRCVE 237
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-238 |
9.87e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.90 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsppveylsGDIR-FHGESLLHASD- 83
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKS-TLLQLLT-----------GDLKpQQGEITLDGVPv 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMIFQEPmvslnplHTLEKQLYEvlslhrgmrreaargeilncldRVGIRqaakrltdyphqLSGGERQ 163
Cdd:cd03247 67 SDLEKALSSLISVLNQRP-------YLFDTTLRN----------------------NLGRR------------FSGGERQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQ 238
Cdd:cd03247 106 RLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-234 |
9.96e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 85.22 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLRgvrgNKIAMIFQEP 101
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKS-TVVALLENFYQPQ----GGQVLLDGKPISQYEHKYLH----SKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVSLNPLHtlEKQLYEVLSLHRGMRREAARGEilncldrvgirQAAKRLTDYPH-----------QLSGGERQRVMIAMA 170
Cdd:cd03248 98 VLFARSLQ--DNIAYGLQSCSFECVKEAAQKA-----------HAHSFISELASgydtevgekgsQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 171 LLTRPELLIADEPTTALDVSVQAQILQLLRelQGELNMGMLFITHNLSIVRKlAHRVAVMQNGR 234
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALY--DWPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-248 |
1.24e-18 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 85.02 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESLLHASdQT 85
Cdd:TIGR04406 2 LVAENLIKSYKK----RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILIDGQDITHLP-MH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGnkIAMIFQEPmvSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaaKRLTDYPHQ-LSGGERQR 164
Cdd:TIGR04406 72 ERARLG--IGYLPQEA--SIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMsLSGGERRR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:TIGR04406 144 VEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLK-ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
....
gi 16130118 245 FASP 248
Cdd:TIGR04406 223 VANE 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-202 |
1.25e-18 |
|
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: 85.02 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVeyLSGDIRFHGESLlhAS 82
Cdd:cd03234 1 QRVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT--TSGQILFNGQPR--KP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRgvrgnKIAMIFQEPMvsLNPLHTLEKQLY--EVLSLHRGM--RREAARGEILNcLDRVGIRQAAKRLTDYphqLS 158
Cdd:cd03234 77 DQFQK-----CVAYVRQDDI--LLPGLTVRETLTytAILRLPRKSsdAIRKKRVEDVL-LRDLALTRIGGNLVKG---IS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130118 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
Cdd:cd03234 146 GGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-234 |
1.40e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.51 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppveylSGDIRFHGesllhasdqtlrgvrgnKIA 95
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLagiypPD------SGTVTVRG-----------------RVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 96 MIFqEPMVSLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAkrltDYP-HQLSGGERQRVMIAMALLTR 174
Cdd:cd03220 87 SLL-GLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELGDFI----DLPvKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 175 PELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-234 |
2.10e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.47 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEAGETLALVGESGSGKS--VTALSILrllpSPPVEylsGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEpmVS 104
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTslINAISGL----TRPQK---GRIVLNGRVLFDAEKGICLPPEKRRIGYVFQD--AR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKqlyevlSLHRGMRREaARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK11144 87 LFPHYKVRG------NLRYGMAKS-MVAQFDKIVALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130118 185 TALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
297-484 |
2.82e-18 |
|
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: 82.20 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIfdgqplqnlnrrqlLPIRHRIQVVFQdp 371
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALAglwpwGSGRIG--------------MPEGEDLLFLPQ-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 nsslnprlnvlqiieeglrvhQPTLSAAQREQQVIavmhevgldpetrhrYP--AEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:cd03223 72 ---------------------RPYLPLGTLREQLI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 16130118 450 DEPTSSLDKTVQAQILTLLKslqqKHQLAYLFISH 484
Cdd:cd03223 116 DEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
287-508 |
2.90e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 287 IRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN----SQGSIIFDGQPLQNLNR--RQLLPI 360
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTVQREGRlaRDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 361 RHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQP------TLSAAQREQQVIAVMHEVGLdPETRHRYPAEFSGGQRQRI 434
Cdd:PRK09984 85 RANTGYIFQQFN--LVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 435 AIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
302-515 |
2.91e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKST-----TGLallrLINSQG-SIIFDGQPLQNLNR-RQLLPIRHRIQVVFQDPNSS 374
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqltNGL----IISETGqTIVGDYAIPANLKKiKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LnprlnVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK13645 103 L-----FQETIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
3.11e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.85 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRhqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLlhaSDQ 84
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKS-TLFRHFNGILKPT----SGSVLIRGEPI---TKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRgNKIAMIFQEPMVSLnpLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQR 164
Cdd:PRK13652 72 NIREVR-KFVGLVFQNPDDQI--FSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATL 244
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 16130118 245 FASP 248
Cdd:PRK13652 226 FLQP 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-238 |
3.12e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRhqqtvrtvVNDVSLQIEAGETLALVGESGSGKSvTALSILR-LLPSppveylSGDIRFHGESLLHASDQ 84
Cdd:COG4138 1 LQLNDVAVAGR--------LGPISAQVNAGELIHLIGPNGAGKS-TLLARMAgLLPG------QGEILLNGRPLSDWSAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVRgnkiAMIFQEPMvslnPLHTLekQLYEVLSLHR--GMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGER 162
Cdd:COG4138 66 ELARHR----AYLSQQQS----PPFAM--PVFQYLALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 163 QRVMIAMALLT-------RPELLIADEPTTALDVSVQAQILQLLREL--QGelnMGMLFITHNLSIVRKLAHRVAVMQNG 233
Cdd:COG4138 133 QRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELcqQG---ITVVMSSHDLNHTLRHADRVWLLKQG 209
|
....*
gi 16130118 234 RCVEQ 238
Cdd:COG4138 210 KLVAS 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
300-468 |
3.30e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPlqnlnrrQLLPiRHRIQVVFQDPNSS 374
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLIAgllppAAGTIKLDGGD-------IDDP-DVAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRLNVLQIIEEGLRVHqptlsaAQREQQVIAVMHEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK13539 84 MKPALTVAENLEFWAAFL------GGEELDIAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....
gi 16130118 455 SLDKTVQAQILTLL 468
Cdd:PRK13539 157 ALDAAAVALFAELI 170
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
300-491 |
5.33e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.41 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPL---QNLNRRQLLPIRHRiqvvfqdp 371
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTT----LLRILAgllrpDSGEVRWNGTPLaeqRDEPHENILYLGHL-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 372 nSSLNPRLNVLqiieEGLRVHQPTLSAAQREqqVIAVMHEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:TIGR01189 82 -PGLKPELSAL----ENLHFWAAIHGGAQRT--IEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130118 452 PTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRA 491
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
319-518 |
5.44e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 319 GESGSGKSTtglallrLIN--------SQGSIIFDGQPLQNLNRRQLLPI-RHRIQVVFQDpnSSLNPRLNVLQIIEEGL 389
Cdd:PRK11144 31 GRSGAGKTS-------LINaisgltrpQKGRIVLNGRVLFDAEKGICLPPeKRRIGYVFQD--ARLFPHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 390 rvhqptlsAAQREQQVIAVMHEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLK 469
Cdd:PRK11144 102 --------AKSMVAQFDKIVALLGIEPLLD-RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130118 470 SLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQ 518
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-217 |
7.35e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVEYLSGDIRFHGESLLHASDQ 84
Cdd:PRK11248 1 MLQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKT----TLLNLI-AGFVPYQHGSITLDGKPVEGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 tlRGVrgnkiamIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164
Cdd:PRK11248 72 --RGV-------VFQNE--GLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNL 217
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
289-513 |
7.76e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.21 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 289 KGILKRIvDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLL----RLIN-SQGSIIFDGQPLQNLNRRQLlpiRHR 363
Cdd:COG4604 5 KNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKST----LLsmisRLLPpDSGEVLVDGLDVATTPSREL---AKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDPNssLNPRLNVLQIIEEGlRV--HQPTLSAAQRE--QQVIAVMhevGLDPeTRHRYPAEFSGGQRQRIAIARA 439
Cdd:COG4604 77 LAILRQENH--INSRLTVRELVAFG-RFpySKGRLTAEDREiiDEAIAYL---DLED-LADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 440 LILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARV 513
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-236 |
8.51e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 82.21 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 30 LQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESllhasdqtlRGVRGNKIAMIFQEPMVSLNPLH 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPA-----KGTVKVAGAS---------PGKGWRHIGYVPQRHEFAWDFPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 110 TLEKQLYEVLSLHRGMRREAARGE---ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:TIGR03771 67 SVAHTVMSGRTGHIGWLRRPCVADfaaVRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16130118 187 LDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVaVMQNGRCV 236
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVI 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-238 |
1.12e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.82 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSvgFRHQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPpveylSGDIRFHGESLLHASDQTL 86
Cdd:COG4604 4 IKNVS--KRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD-----SGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 rgvrGNKIAMIFQEPMVSLNpLhTLEkqlyEVLSL-----HRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGE 161
Cdd:COG4604 74 ----AKRLAILRQENHINSR-L-TVR----ELVAFgrfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLD---ELSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
301-508 |
1.42e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 82.31 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALL---RLINSQGSIIFDGQPLQNLNRRQllpiRHR--IQVVFQDPNSSl 375
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGQDLLELEPDE----RARagLFLAFQYPEEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 nPRLNVLQIIEEGLRVH-----QPTLSAAQREQQVIAVMHEVGLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLIIL 449
Cdd:TIGR01978 90 -PGVSNLEFLRSALNARrsargEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVI-ILRQGEVVEQG 508
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKPDYVhVLLDGRIVKSG 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-246 |
1.47e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.84 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGESLlhaSDQTLR 87
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY-----DIDEGEILLDGHDL---RDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRgNKIAMIFQEpmVSL------NPLHTLEKQLYEVLSLHRGMRREAARGEIL---NCLDRV----GIrqaakrltdyp 154
Cdd:PRK11176 414 SLR-NQVALVSQN--VHLfndtiaNNIAYARTEQYSREQIEEAARMAYAMDFINkmdNGLDTVigenGV----------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGR 234
Cdd:PRK11176 480 -LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGE 555
|
250
....*....|..
gi 16130118 235 CVEQNYAATLFA 246
Cdd:PRK11176 556 IVERGTHAELLA 567
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
302-520 |
1.53e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpirhrIQVVFQDPNSSLNPRLN 380
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 381 VLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:PRK15056 97 VEDVVMMGRYGHMGWLRRAKKRdrQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 459 TVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRqGEVVEQGPCARVFATPQQE 520
Cdd:PRK15056 176 KTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLE 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
299-503 |
1.56e-17 |
|
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: 79.41 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQgsiifdgqplqnlnrrqllpirhriqvvfqdpnssLNPr 378
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIAGE-----------------------------------LEP- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 lnvlqiiEEGlrvhqptlsaaqreqqviavmhEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:cd03221 53 -------DEG----------------------IVTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16130118 459 TVQAQILTLLKSLQQkhqlAYLFISHDLHVVRALCHQVIILRQGE 503
Cdd:cd03221 104 ESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-457 |
1.86e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSIL---RLLPSPPVEYLSGDI--RFHGESLLHasdqtlr 87
Cdd:NF033858 7 VSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKS-SLLSLIagaRKIQQGRVEVLGGDMadARHRRAVCP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 gvrgnKIAMIFQepmvslnplhTLEKQLYEVLSLHR---------GMRREAARGEILNCLDRVGI-----RQAAKrltdy 153
Cdd:NF033858 77 -----RIAYMPQ----------GLGKNLYPTLSVFEnldffgrlfGQDAAERRRRIDELLRATGLapfadRPAGK----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 154 phqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMlfithnlSIVRKLAH-------- 225
Cdd:NF033858 137 ---LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE-RPGM-------SVLVATAYmeeaerfd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 226 RVAVMQNGRCVEQNYAATLFASpthpyTQ---------KLLNSEPSGDPVPLPEPASTLLDVEqlqvAFPIR-KGILKRI 295
Cdd:NF033858 206 WLVAMDAGRVLATGTPAELLAR-----TGadtleaafiALLPEEKRRGHQPVVIPPRPADDDD----EPAIEaRGLTMRF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 296 VDHnVVVKNISFTLRAGETLGLVGESGSGKST-----TGLallrLINSQGSIIFDGQPL--QNLNrrqllpIRHRI---- 364
Cdd:NF033858 277 GDF-TAVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmlTGL----LPASEGEAWLFGQPVdaGDIA------TRRRVgyms 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 365 QvVFqdpnsSLNPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMHEVGLDPETRHRyPAEFSGGQRQRIAIARALILKP 444
Cdd:NF033858 346 Q-AF-----SLYGELTVRQNLELHARLFH--LPAAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKP 416
|
490
....*....|...
gi 16130118 445 SLIILDEPTSSLD 457
Cdd:NF033858 417 ELLILDEPTSGVD 429
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-238 |
2.08e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTqTLLAIENLSVGFRHQQT------------------VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL--- 59
Cdd:COG1134 1 MS-SMIEVENVSKSYRLYHEpsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKS----TLLKLIagi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 60 --PSppveylSGDIRFHGesllhasdqtlrgvrgnKIAMIFqEPMVSLNPLHTLEKQLYEVLSLHrGMRREaargEILNC 137
Cdd:COG1134 76 lePT------SGRVEVNG-----------------RVSALL-ELGAGFHPELTGRENIYLNGRLL-GLSRK----EIDEK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 138 LDRV----GIRQAAkrltDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLF 212
Cdd:COG1134 127 FDEIvefaELGDFI----DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIF 201
|
250 260
....*....|....*....|....*.
gi 16130118 213 ITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:COG1134 202 VSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-248 |
3.53e-17 |
|
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: 80.66 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLLHAS-D 83
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPD------SGKILLDGQDITKLPmH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QtlRGVRGnkIAMIFQEPMV--SLnplhTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGE 161
Cdd:cd03218 71 K--RARLG--IGYLPQEASIfrKL----TVEENILAVLEIR-GLSKKEREEKLEELLEEFHITHLRKSKAS---SLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALD-VSVQaQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNY 240
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
....*...
gi 16130118 241 AATLFASP 248
Cdd:cd03218 217 PEEIAANE 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-234 |
3.91e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.84 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESL----LHa 81
Cdd:COG1137 4 LEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGRIFLDGEDIthlpMH- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 sdqtLRGVRGnkIAMIFQEPMV--SLnplhTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSG 159
Cdd:COG1137 74 ----KRARLG--IGYLPQEASIfrKL----TVEDNILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAY---SLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALD-VSVqAQILQLLRELQgELNMGMLfIT-HN----LSIVrklaHRVAVMQNG 233
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretLGIC----DRAYIISEG 212
|
.
gi 16130118 234 R 234
Cdd:COG1137 213 K 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
300-508 |
4.40e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQllpiRHRIQVVFQDPNssLNPR 378
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARLA----RARIGVVPQFDN--LDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVlqiiEEGLRVHQPTLSAAQRE-QQVIAVMHEVG-LDPETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK13536 129 FTV----RENLLVFGRYFGMSTREiEAVIPSLLEFArLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 457 DKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-245 |
6.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.94 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHAS-DQTLRGVRgNKIAMIFQEPmvsl 105
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKS-TIMQLLNGLHVPT----QGSVRVDDTLITSTSkNKDIKQIR-KKVGLVFQFP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 106 nplhtlEKQLYEVLSL--------HRGMRREAARGEILNCLDRVGIrqaAKRLTDY-PHQLSGGERQRVMIAMALLTRPE 176
Cdd:PRK13649 95 ------ESQLFEETVLkdvafgpqNFGVSQEEAEALAREKLALVGI---SESLFEKnPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 177 LLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLF 245
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-237 |
6.46e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVGFrhqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPsppveyLSGDIRfHGESLlha 81
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-TLLKLLagELEP------DSGTVK-LGETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 sdqtlrgvrgnKIAMIFQEPMvSLNPlhtlEKQLYEVLslhRGMRREAARGEILNCLDRVGIR--QAAKRLTDyphqLSG 159
Cdd:COG0488 379 -----------KIGYFDQHQE-ELDP----DKTVLDEL---RDGAPGGTEQEVRGYLGRFLFSgdDAFKPVGV----LSG 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelnmGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
6.99e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHQQTVR-TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSP----PVE--YLSGDIRFHGES 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKygtiQVGdiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 78 LLHASDQTLRGVRGNK-IAMIFQEPMVSLNPlHTLEKQL-YEVLSLhrGMRREAARGEILNCLDRVGIRQAAkrLTDYPH 155
Cdd:PRK13631 101 TNPYSKKIKNFKELRRrVSMVFQFPEYQLFK-DTIEKDImFGPVAL--GVKKSEAKKLAKFYLNKMGLDDSY--LERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRC 235
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
250
....*....|....
gi 16130118 236 VEQNYAATLFASPT 249
Cdd:PRK13631 255 LKTGTPYEIFTDQH 268
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-201 |
8.61e-17 |
|
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: 78.94 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfrhQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPveyLSGDIRFHGESLlhasd 83
Cdd:TIGR01189 1 LAARNLAC----SRGERMLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILAglLRP---DSGEVRWNGTPL----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLHRGMRREaargeILNCLDRVGIRQAAKRLTdypHQLSGGERQ 163
Cdd:TIGR01189 65 AEQRDEPHENILYLGHLP--GLKPELSALENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPA---AQLSAGQQR 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-234 |
1.96e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.33 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFrhqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppveylSGDIRFHGESLLHASdqt 85
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI--------AGELEPDEGIVTWGS--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 lrgvrGNKIAmifqepmvslnplhtlekqlyevlslhrgmrreaargeilncldrvgirqaakrltdYPHQLSGGERQRV 165
Cdd:cd03221 62 -----TVKIG---------------------------------------------------------YFEQLSGGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelnmGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-267 |
2.18e-16 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 82.24 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVEYLSGDirfhGESLLHASDQTLRgvrgNKIAMIFQEPMVs 104
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKT-TLINLLQRVYDPTVGQILID----GIDINTVTRESLR----KSIATVFQDAGL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 lnplhtLEKQLYEVLSLHRgmrREAARGEILNCLDRVGIRQ-AAKRLTDYP-------HQLSGGERQRVMIAMALLTRPE 176
Cdd:TIGR01192 421 ------FNRSIRENIRLGR---EGATDEEVYEAAKAAAAHDfILKRSNGYDtlvgergNRLSGGERQRLAIARAILKNAP 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 177 LLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQNYAATLFASPTHPY---- 252
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSFQELIQKDGRFYkllr 568
|
250
....*....|....*
gi 16130118 253 TQKLLNSEPSGDPVP 267
Cdd:TIGR01192 569 RSGLLTNQPATKPLR 583
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-247 |
2.20e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppveYLSGDIRFHGESLLHASDQT 85
Cdd:PRK10790 341 IDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRPLSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRGMRREAargeILNCLDRVGIRQAAKRLTDYPH--------QL 157
Cdd:PRK10790 413 LR----QGVAMVQQDPVV-------LADTFLANVTLGRDISEEQ----VWQALETVQLAELARSLPDGLYtplgeqgnNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGelNMGMLFITHNLSIVRKlAHRVAVMQNGRCVE 237
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
250
....*....|
gi 16130118 238 QNYAATLFAS 247
Cdd:PRK10790 555 QGTHQQLLAA 564
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
301-508 |
2.39e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.08 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLI--------NSQGSIIFDGQPLqnlnRRQLlpIRHRIQVVFQDPN 372
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTT----LLDAIsgrvegggTTSGQILFNGQPR----KPDQ--FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 ssLNPRLNVlqiiEEGL------RVHQPTLSAAQREQQVIAVMHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSL 446
Cdd:cd03234 92 --LLPGLTV----RETLtytailRLPRKSSDAIRKKRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 447 IILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFIshdlHVVRA----LCHQVIILRQGEVVEQG 508
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI----HQPRSdlfrLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-247 |
3.03e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.28 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRfhgeslLHASDQTLRGVRG--NKIAMIFQEPM 102
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYA------IPANLKKIKEVKRlrKEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 103 VSLNPlHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGI-RQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:PRK13645 101 YQLFQ-ETIEKDI-AFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 182 EPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFAS 247
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
297-515 |
3.29e-16 |
|
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: 82.30 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINS-QGSIIFDGqplQNLNRRQLLPIRHRIQVVFQDP---N 372
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDG---LNIAKIGLHDLRFKITIIPQDPvlfS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPRLNVL-QIIEEGL-----RVHQPTLSAAQREqqviavmhevGLDPETrhrypAE----FSGGQRQRIAIARALIL 442
Cdd:TIGR00957 1374 GSLRMNLDPFsQYSDEEVwwaleLAHLKTFVSALPD----------KLDHEC-----AEggenLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 443 KPSLIILDEPTSSL----DKTVQAQILTllkslqQKHQLAYLFISHDLHVVRALChQVIILRQGEVVEQGPCARVFA 515
Cdd:TIGR00957 1439 KTKILVLDEATAAVdletDNLIQSTIRT------QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-220 |
3.99e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQTVrtvVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESllh 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-----VRLASGKISILGQP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 asdqTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRG-MRREAARgeilnclDRVGIRQAAKR--LTDYPH-- 155
Cdd:PRK15056 71 ----TRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGwLRRAKKR-------DRQIVTAALARvdMVEFRHrq 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIV 220
Cdd:PRK15056 140 igELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSV 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-272 |
4.18e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.27 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPVeylSGDIRFHGESLLHASDQTLRGVRgNKIAMIFQ 99
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGqiAPD---HGEILFDGENIPAMSRSRLYTVR-KRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EP--MVSLNPLHTLEKQLYEvlslHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK11831 92 SGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPThPYTQKLL 257
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFL 243
|
250
....*....|....*
gi 16130118 258 NSEPSGdPVPLPEPA 272
Cdd:PRK11831 244 DGIADG-PVPFRYPA 257
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
297-508 |
4.87e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtgLALLRLIN---SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPns 373
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKST--LASLLMGYyplTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDP-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 slnprlnvlQIIEEGLRVHQpTLSAAQREQQVIAVMHEVGLD------PETRHRYPAE----FSGGQRQRIAIARALILK 443
Cdd:PRK10790 425 ---------VVLADTFLANV-TLGRDISEEQVWQALETVQLAelarslPDGLYTPLGEqgnnLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLH-VVRAlcHQVIILRQGEVVEQG 508
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLStIVEA--DTILVLHRGQAVEQG 556
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-234 |
5.05e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLS-VGFRHqqtvrtvvndVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGESllha 81
Cdd:PRK15439 266 APVLTVEDLTgEGFRN----------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA-----RGGRIMLNGKE---- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 sdqtlrgVRGNKIAMIFQEPMVSL------NPLHtLEKQLY-EVLSLHRGMR-------REAARgeilncLDR----VGI 143
Cdd:PRK15439 327 -------INALSTAQRLARGLVYLpedrqsSGLY-LDAPLAwNVCALTHNRRgfwikpaRENAV------LERyrraLNI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 144 R-----QAAKRLtdyphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqGELNMGMLFITHNLS 218
Cdd:PRK15439 393 KfnhaeQAARTL-------SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLE 464
|
250
....*....|....*.
gi 16130118 219 IVRKLAHRVAVMQNGR 234
Cdd:PRK15439 465 EIEQMADRVLVMHQGE 480
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-238 |
8.45e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 28 VSLQIEAGETLALVGESGSGKSvTALS-ILRLLPSppveylSGDIRFHGESLLHASDQTLRGVRGnkiAMIFQEPMVSLN 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLArMAGLLPG------SGSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 107 PLhtlekqlYEVLSLHRGMRREAARGEILncLDRVGIR-QAAKRLTDYPHQLSGGERQRVMIAMALL-----TRPE--LL 178
Cdd:PRK03695 85 PV-------FQYLTLHQPDKTRTEAVASA--LNEVAEAlGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 179 IADEPTTALDVSVQAQILQLLRELqGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-247 |
8.50e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.31 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLRgvrgnKIAMIFQep 101
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKT-TTLRMLLGLTHPD----AGSISLCGEPVPSRARHARQ-----RVGVVPQ-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVSLNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQAAkrltDYP-HQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK13537 88 FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKA----DAKvGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 181 DEPTTALDVSVQAQILQLLRELqgeLNMG--MLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFAS 247
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSL---LARGktILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
300-508 |
9.20e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.98 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINS-QGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP---NSSL 375
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLREL---RRQFSMIPQDPvlfDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 npRLNVlqiieeglrvhQPTLSAAQREqqVIAVMHEVGLdpetRHRYPAE--------------FSGGQRQRIAIARALI 441
Cdd:PTZ00243 1401 --RQNV-----------DPFLEASSAE--VWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 442 LKPS-LIILDEPTSSLDKTVQAQILTLLKSLQQKHQLayLFISHDLHVVrALCHQVIILRQGEVVEQG 508
Cdd:PTZ00243 1462 KKGSgFILMDEATANIDPALDRQIQATVMSAFSAYTV--ITIAHRLHTV-AQYDKIIVMDHGAVAEMG 1526
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
312-508 |
1.11e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 312 GETLGLVGESGSGKSTTGLALLRLINSQGsiiFDGQPLQNlNRRQLLPIRHRIQVVFQDpnSSLNPRLNVLQ--IIEEGL 389
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILAN-NRKPTKQILKRTGFVTQD--DILYPHLTVREtlVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 390 RVHQpTLSAAQREQQVIAVMHEVGL----DPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
Cdd:PLN03211 168 RLPK-SLTKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130118 466 TLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-254 |
1.28e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIE--NLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESL 78
Cdd:PRK14258 1 MSKLIPAIKvnNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 LHASDQTLRGVRgnKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhrGMRREAARGEIL-NCLDRVGIRQAAK-RLTDYPHQ 156
Cdd:PRK14258 77 YERRVNLNRLRR--QVSMVHPKP--NLFPMSVYDNVAYGVKIV--GWRPKLEIDDIVeSALKDADLWDEIKhKIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQN---- 232
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenr 230
|
250 260
....*....|....*....|...
gi 16130118 233 -GRCVEQNYAATLFASPTHPYTQ 254
Cdd:PRK14258 231 iGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
273-501 |
1.66e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFPIRKgilkrivdhnvVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQplqn 351
Cdd:PRK09544 2 TSLVSLENVSVSFGQRR-----------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGK---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 352 lnrrqlLPIRHRIQVVFQDPNSSLNprlnvlqiIEEGLRVHQPTlsaaqREQQVIAVMHEVglDPETRHRYPAE-FSGGQ 430
Cdd:PRK09544 67 ------LRIGYVPQKLYLDTTLPLT--------VNRFLRLRPGT-----KKEDILPALKRV--QAGHLIDAPMQkLSGGE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQ 501
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-462 |
1.84e-15 |
|
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: 79.21 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-----------RLLPSPPVEYL--------SGDIRFHGESLLHAS 82
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkdfngeaRPQPGIKVGYLpqepqldpTKTVRENVEEGVAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRgvRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLslhrgmrrEAARGEILNclDRVGIRQAAKRLT--DYP-HQLSG 159
Cdd:TIGR03719 97 KDALD--RFNEISAKYAEPDADFDKLAAEQAELQEII--------DAADAWDLD--SQLEIAMDALRCPpwDADvTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELnmgmLFITHNLSIVRKLAHRVAVMQNGRCV--E 237
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTV----VAVTHDRYFLDNVAGWILELDRGRGIpwE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 238 QNYAATLFA--------SPTHPYTQKLLNSE-------PSGD------------------------------PvPLPEPA 272
Cdd:TIGR03719 241 GNYSSWLEQkqkrleqeEKEESARQKTLKRElewvrqsPKGRqakskarlaryeellsqefqkrnetaeiyiP-PGPRLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ-----GSIIfdgq 347
Cdd:TIGR03719 320 DKVIEAENLTKAF-----------GDKLLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMITGQeqpdsGTIE---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 348 plqnlnrrqllpIRHRIQVVFQDPN-SSLNPRLNVLQIIEEGLRVhqptLSAAQREQQVIAVMHEVGLDPETRHRYPAEF 426
Cdd:TIGR03719 381 ------------IGETVKLAYVDQSrDALDPNKTVWEEISGGLDI----IKLGKREIPSRAYVGRFNFKGSDQQKKVGQL 444
|
490 500 510
....*....|....*....|....*....|....*..
gi 16130118 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQA 462
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDvETLRA 481
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-234 |
1.97e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPvEYLSGDIrFHGESLLHASDQTLRGVrgnkiAMIFQEpmvsl 105
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLE-DITSGDL-FIGEKRMNDVPPAERGV-----GMVFQS----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 106 nplhtleKQLYEVLSLHRGMR-----REAARGEILNCLDRVG-IRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK11000 84 -------YALYPHLSVAENMSfglklAGAKKEEINQRVNQVAeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 180 ADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-214 |
2.02e-15 |
|
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: 74.11 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfrHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL----PsppveYLSGDIRFHgesllha 81
Cdd:cd03223 1 IELENLSL---ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRALaglwP-----WGSGRIGMP------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 sdqtlrgvRGNKIAMIFQEPMVslnPLHTLEKQLYevlslhrgmrreaargeilncldrvgirqaakrltdYP--HQLSG 159
Cdd:cd03223 62 --------EGEDLLFLPQRPYL---PLGTLREQLI------------------------------------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqgelnMGMLFIT 214
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE------LGITVIS 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-227 |
2.10e-15 |
|
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: 74.84 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPveyLSGDIRFHGESLLHASDQTLRGvrgnkIAMIFQ 99
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAglSPP---LAGRVLLNGGPLDFQRDSIARG-----LLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EPMVslnplhtleKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQaakrLTDYP-HQLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03231 81 APGI---------KTTLSVLENLRFWHADHSDEQVEEALARVGLNG----FEDRPvAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130118 179 IADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRV 227
Cdd:cd03231 148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
302-508 |
2.66e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRqlLPIRHRIQVVFQDpnSSLN 376
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKST----LMKVLSgihepTKGTITINNINYNKLDHK--LAAQLGIGIIYQE--LSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLQIIEEG-LRVHQ----PTLSAAQREQQVIAVMHEVGL--DPETRhryPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK09700 93 DELTVLENLYIGrHLTKKvcgvNIIDWREMRVRAAMMLLRVGLkvDLDEK---VANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 450 DEPTSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-238 |
2.71e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTL--LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpveyLSGDIRFHGESL 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGYGK----YTVAENLTVEIPDGHFTAIIGPNGCGKS-TLLRTLSRLMTP----AHGHVWLDGEHI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 79 LH-ASDQTLRgvrgnKIAMIFQEPMV--SLNPLHTLEKQLYEVLSLHRGMRREAARGeILNCLDRVGIRQAAKRLTDyph 155
Cdd:PRK10253 72 QHyASKEVAR-----RIGLLAQNATTpgDITVQELVARGRYPHQPLFTRWRKEDEEA-VTKAMQATGITHLADQSVD--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRC 235
Cdd:PRK10253 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
...
gi 16130118 236 VEQ 238
Cdd:PRK10253 223 VAQ 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-238 |
2.89e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEY---LSGDIRFHGESLLHA 81
Cdd:PRK13547 1 MLTADHLHVARRH----RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarVTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLRGVRgnkiAMIFQ--EPMVSLNplhtlekqLYEVLSLHR-------GMRREAARGEILNCLDRVGIRQAAKRLTD 152
Cdd:PRK13547 77 DAPRLARLR----AVLPQaaQPAFAFS--------AREIVLLGRypharraGALTHRDGEIAWQALALAGATALVGRDVT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 153 yphQLSGGERQRVMIAMAL---------LTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKL 223
Cdd:PRK13547 145 ---TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARH 221
|
250
....*....|....*
gi 16130118 224 AHRVAVMQNGRCVEQ 238
Cdd:PRK13547 222 ADRIAMLADGAIVAH 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-249 |
3.23e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 2 TQTLLAIENLSvgFRHQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHA 81
Cdd:PRK10575 8 SDTTFALRNVS--FRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPPS----EGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 82 SDQTLrgvrGNKIAMIFQEpmvsLNPLHTLekQLYEVLSLHR-------GMRREAARGEILNCLDRVGIRQAAKRLTDyp 154
Cdd:PRK10575 79 SSKAF----ARKVAYLPQQ----LPAAEGM--TVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:PRK10575 147 -SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGE 225
|
250
....*....|....*
gi 16130118 235 CVEQNYAATLFASPT 249
Cdd:PRK10575 226 MIAQGTPAELMRGET 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-234 |
3.50e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLlh 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKT-TVFNCLTGFYKPT----GGTILLRGQHI-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 asdqtlRGVRGNKIAM-----------IFQEPMVSLNPL---HT-LEKQLYEVLSLHRGMRReaARGEILN----CLDRV 141
Cdd:PRK11300 70 ------EGLPGHQIARmgvvrtfqhvrLFREMTVIENLLvaqHQqLKTGLFSGLLKTPAFRR--AESEALDraatWLERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 142 GIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVR 221
Cdd:PRK11300 142 GLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVM 218
|
250
....*....|...
gi 16130118 222 KLAHRVAVMQNGR 234
Cdd:PRK11300 219 GISDRIYVVNQGT 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-233 |
5.01e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQQTVrtvvNDVSLQIEAGETLALVGESGSGKSvtalSILRLL---------PSPPVEYLSGDIRF 73
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQAL----HAVDLNIHHGEMVALLGPSGSGKS----TLLRHLsglitgdksAGSHIELLGRTVQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 74 HGesllhasdQTLRGVRGNK--IAMIFQEPMVsLNPLHTLEKQLYEVLSLHRGMR------REAARGEILNCLDRVGIRQ 145
Cdd:PRK09984 74 EG--------RLARDIRKSRanTGYIFQQFNL-VNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVGMVH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 146 -AAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLA 224
Cdd:PRK09984 145 fAHQRVS----TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYC 220
|
....*....
gi 16130118 225 HRVAVMQNG 233
Cdd:PRK09984 221 ERIVALRQG 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
265-492 |
6.32e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 265 PVPLPEPASTLLDveqlqvAFPIRKGILKRivdhnVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLInsqgsiif 344
Cdd:COG2401 20 VLDLSERVAIVLE------AFGVELRVVER-----YVLRDLNLEIEPGEIVLIVGASGSGKST----LLRLL-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 345 dgqplqnlnRRQLLPIRHRIQVVFQDPNSSlnprlNVLQIIEEGLRVHQPTlsaaqreqQVIAVMHEVGL-DPETRHRYP 423
Cdd:COG2401 77 ---------AGALKGTPVAGCVDVPDNQFG-----REASLIDAIGRKGDFK--------DAVELLNAVGLsDAVLWLRRF 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqAQILTL-LKSLQQKHQLAYLFISHDLHVVRAL 492
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
274-508 |
6.75e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 274 TLLDVEQLQVAFpirKGILkrivdhnvVVKNISFTLRAGETLGLVGESGSGKST-----TGLallrLINSQGSIIFDGQP 348
Cdd:PRK11300 4 PLLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTTvfnclTGF----YKPTGGTILLRGQH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 349 LQNLNRRQLlpIRHRIQVVFQdpNSSLNPRLNVLqiieEGLRVHQ---------------PTLSAAQREQQVIAV--MHE 411
Cdd:PRK11300 69 IEGLPGHQI--ARMGVVRTFQ--HVRLFREMTVI----ENLLVAQhqqlktglfsgllktPAFRRAESEALDRAAtwLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 412 VGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRA 491
Cdd:PRK11300 141 VGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMG 219
|
250
....*....|....*..
gi 16130118 492 LCHQVIILRQGEVVEQG 508
Cdd:PRK11300 220 ISDRIYVVNQGTPLANG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
292-509 |
6.89e-15 |
|
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: 73.33 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALL---RLINSQGSIIFDGQPLQNLnrrqllPIRHR----I 364
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDITDL------PPEERarlgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 365 QVVFQDPnsslnPRLnvlqiieEGLRVhqptlsaaqreqqviavmhevgldpETRHRYPAE-FSGGQRQRIAIARALILK 443
Cdd:cd03217 80 FLAFQYP-----PEI-------PGVKN-------------------------ADFLRYVNEgFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 444 PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVI-ILRQGEVVEQGP 509
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVhVLYDGRIVKSGD 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
304-506 |
7.95e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.75 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-------QGSIIFDGQPLQnlnrrqllpirhriqvvFQDPNSSln 376
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKST----LMKVLSGvyphgsyEGEILFDGEVCR-----------------FKDIRDS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLqIIeeglrvHQ-----PTLSAAQ-----REQQ---VI----------AVMHEVGLD--PETRhryPAEFSGGQR 431
Cdd:NF040905 76 EALGIV-II------HQelaliPYLSIAEniflgNERAkrgVIdwnetnrrarELLAKVGLDesPDTL---VTDIGVGKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVE 506
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
301-490 |
9.23e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 9.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIF-DGQPLQNLNRRQLlpiRHRIQVVFQDP----NSS 374
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIInDSHNLKDINLKWW---RSKIGVVSQDPllfsNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNP------RLNVLQIIEEGLR--------------------------VHQPTLSA----AQREQQVI-----------A 407
Cdd:PTZ00265 477 KNNikyslySLKDLEALSNYYNedgndsqenknkrnscrakcagdlndMSNTTDSNelieMRKNYQTIkdsevvdvskkV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 408 VMHE-VGLDPETRHRY----PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFI 482
Cdd:PTZ00265 557 LIHDfVSALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
....*...
gi 16130118 483 SHDLHVVR 490
Cdd:PTZ00265 637 AHRLSTIR 644
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
299-498 |
9.84e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLInsQGSIifdgQPLQNLNRRqllpiRHRIQVVFQDPNSSLNPR 378
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKST----LLKVL--AGVL----RPTSGTVRR-----AGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 L--NVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:NF040873 70 LplTVRDLVAMGRWARRGLWRRLTRDdrAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130118 455 SLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVII 498
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-245 |
1.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.38 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQT-LRGVRgNKIAMIFQEPmvsl 105
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKS-TLLQHLNGLLQPT----EGKVTVGDIVVSSTSKQKeIKPVR-KKVGVVFQFP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 106 nplhtlEKQLYEVLSL--------HRGMRREAARGEILNCLDRVGIRQaaKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK13643 94 ------ESQLFEETVLkdvafgpqNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLF 245
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
295-468 |
1.32e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 295 IVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-----QGSIIFDGQPLQNLN---RRQLLPIRHRiqv 366
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTS----LLRILAGlarpdAGEVLWQGEPIRRQRdeyHQDLLYLGHQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 367 vfqdpnSSLNPRLNVlqiiEEGLRVHQPtLSAAQREQQVIAVMHEVGLdpETRHRYPAE-FSGGQRQRIAIARALILKPS 445
Cdd:PRK13538 83 ------PGIKTELTA----LENLRFYQR-LHGPGDDEALWEALAQVGL--AGFEDVPVRqLSAGQQRRVALARLWLTRAP 149
|
170 180
....*....|....*....|...
gi 16130118 446 LIILDEPTSSLDKTVQAQILTLL 468
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALL 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-238 |
1.36e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.00 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSvgFRHQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppveylSGDIRFHGESLLHASDQTL 86
Cdd:PRK13647 7 VEDLH--FRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQ------RGRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RgvrgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLhrGMRREaargEILNcldRVGIRQAAKRLTDY----PHQLSGGER 162
Cdd:PRK13647 78 R----SKVGLVFQDPDDQVFSSTVWDDVAFGPVNM--GLDKD----EVER---RVEEALKAVRMWDFrdkpPYHLSYGQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQ 238
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-504 |
1.59e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESL-LHASDQTLRgvrgNKIAMIFQEpmv 103
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKS-TLLKCLFGIYQKD----SGSILFQGKEIdFKSSKEALE----NGISMVHQE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 sLNplHTLEKQLYEVLSL-----------HRGMRREAARgeILNCLDrVGIRQAAKRLTdyphqLSGGERQRVMIAMALL 172
Cdd:PRK10982 82 -LN--LVLQRSVMDNMWLgryptkgmfvdQDKMYRDTKA--IFDELD-IDIDPRAKVAT-----LSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 173 TRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV----------EQNYAA 242
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIatqplagltmDKIIAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 243 TLFASPTHPYTQKLlnsepsgdpvplPEPASTLLDVEQLQVAfpirkgilkrivdHNVVVKNISFTLRAGETLGLVGESG 322
Cdd:PRK10982 230 MVGRSLTQRFPDKE------------NKPGEVILEVRNLTSL-------------RQPSIRDVSFDLHKGEILGIAGLVG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 323 SgKSTTGLALLRLI--NSQGSIIFDGQPLQNlnRRQLLPIRHRIQVVFQDPNSS-----LNPRLNVLQIIEEGLRVHQPT 395
Cdd:PRK10982 285 A-KRTDIVETLFGIreKSAGTITLHGKKINN--HNANEAINHGFALVTEERRSTgiyayLDIGFNSLISNIRNYKNKVGL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 396 LSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKH 475
Cdd:PRK10982 362 LDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD 441
|
490 500
....*....|....*....|....*....
gi 16130118 476 QlAYLFISHDLHVVRALCHQVIILRQGEV 504
Cdd:PRK10982 442 K-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-486 |
1.94e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 35 GETLALVGESGSGKSvTALSIL--RLLP------SPP-----VEYLSGdirfhgeSLLHA-----SDQTLRGVRgnKIAM 96
Cdd:PRK13409 99 GKVTGILGPNGIGKT-TAVKILsgELIPnlgdyeEEPswdevLKRFRG-------TELQNyfkklYNGEIKVVH--KPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 97 IFQEPMVSLNPLHTLEKQLYEvlslhRGMRRE-AARGEILNCLDRvGIRQaakrltdyphqLSGGERQRVMIAMALLTRP 175
Cdd:PRK13409 169 VDLIPKVFKGKVRELLKKVDE-----RGKLDEvVERLGLENILDR-DISE-----------LSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 176 ELLIADEPTTALDVSVQAQILQLLRELQGELNmgMLFITHNLSIVRKLAHRVAVMqngrcveqnyaatlFASP------T 249
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKY--VLVVEHDLAVLDYLADNVHIA--------------YGEPgaygvvS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 250 HPY-TQKLLNSEPSG-----------DPVPLPEPASTLLDVEQLQVAFPirkGILKRIVDHNVVVKniSFTLRAGETLGL 317
Cdd:PRK13409 296 KPKgVRVGINEYLKGylpeenmrirpEPIEFEERPPRDESERETLVEYP---DLTKKLGDFSLEVE--GGEIYEGEVIGI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 318 VGESGSGKSTtglaLLRLIN-----SQGSIIFDgqplqnlnrrqlLPIRHRIQVVFQDPNSSlnprlnvlqiIEEGLRVH 392
Cdd:PRK13409 371 VGPNGIGKTT----FAKLLAgvlkpDEGEVDPE------------LKISYKPQYIKPDYDGT----------VEDLLRSI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 393 QPTLSAAQREQQVIavmHEVGLDP--EtrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQILT--LL 468
Cdd:PRK13409 425 TDDLGSSYYKSEII---KPLQLERllD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVakAI 496
|
490
....*....|....*...
gi 16130118 469 KSLQQKHQLAYLFISHDL 486
Cdd:PRK13409 497 RRIAEEREATALVVDHDI 514
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-238 |
2.42e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.49 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLlpsppVEYL----SGDIRFHGESL--LHASDqtlrgvRGnkIAMI 97
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRM-----VAGLeritSGEIWIGGRVVneLEPAD------RD--IAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 98 FQEpmVSLNPLHTLEKQLYEVLSLhRGM------RR--EAARG-EILNCLDRvgirqaakrltdYPHQLSGGERQRVMIA 168
Cdd:PRK11650 82 FQN--YALYPHMSVRENMAYGLKI-RGMpkaeieERvaEAARIlELEPLLDR------------KPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRcVEQ 238
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQ 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
297-491 |
2.56e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.76 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLN---RRQLLPIRHRiqvvf 368
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTT----LLRILAglsppLAGRVLLNGGPLDFQRdsiARGLLYLGHA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 369 qdpnSSLNPRLNVLqiieEGLRVHQPTLSAAQREQqviaVMHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:cd03231 82 ----PGIKTTLSVL----ENLRFWHADHSDEQVEE----ALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130118 449 LDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRA 491
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
228-529 |
4.31e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 228 AVMQNGRCVEQ-NYAAT--LFASPTHPYTQKL-------------LNS-EPSGDPVPLPEPASTLLDVEQLQVAFPIRKG 290
Cdd:PLN03232 1155 AVLRNGNAENQaGFASTmgLLLSYTLNITTLLsgvlrqaskaensLNSvERVGNYIDLPSEATAIIENNRPVSGWPSRGS 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 291 I------LKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQplqNLNRRQLLPIRHR 363
Cdd:PLN03232 1235 IkfedvhLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRIMIDDC---DVAKFGLTDLRRV 1311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDPN-SSLNPRLNVLQIIEEglrvHQPTLSAAQREQQVIAVM--HEVGLDPETRHRyPAEFSGGQRQRIAIARAL 440
Cdd:PLN03232 1312 LSIIPQSPVlFSGTVRFNIDPFSEH----NDADLWEALERAHIKDVIdrNPFGLDAEVSEG-GENFSVGQRQLLSLARAL 1386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 441 ILKPSLIILDEPTSSLDKTVQAQILTLLKslQQKHQLAYLFISHDLHVVRAlCHQVIILRQGEVVEqgpcarvFATPQQE 520
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQEL 1456
|
....*....
gi 16130118 521 YTRQLLALS 529
Cdd:PLN03232 1457 LSRDTSAFF 1465
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
297-513 |
4.90e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKST---------TGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRhriQVV 367
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTllkalagdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLR---AVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 368 FQDPNSSLnpRLNVLQIIEEGLRVHQPTLSAAQREQQVIA--VMHEVGLDPETRhRYPAEFSGGQRQRIAIARAL----- 440
Cdd:PRK13547 89 PQAAQPAF--AFSAREIVLLGRYPHARRAGALTHRDGEIAwqALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 441 ----ILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARV 513
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
304-509 |
5.45e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLI-----NSQGSIIFDGQPLQNLNRRQLLpiRHRIQVVFQDPNSSLnpR 378
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKST----LLKCLfgiyqKDSGSILFQGKEIDFKSSKEAL--ENGISMVHQELNLVL--Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQII------EEGLRVHQptlsaAQREQQVIAVMHEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK10982 88 RSVMDNMwlgrypTKGMFVDQ-----DKMYRDTKAIFDELDIDIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 453 TSSLDKTVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGP 509
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQP 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-249 |
5.68e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALsilrllpsppveYLSGDIRFH-GESLLHASD----QTLRGVRgNKIAMIFQ 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLAL------------HLNGLLRPQkGKVLVSGIDtgdfSKLQGIR-KLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EPmvslnplhtlEKQLyevlsLHRGMRREAARGEILNCLDRVGIRQAAKR------LTDY----PHQLSGGERQRVMIAM 169
Cdd:PRK13644 85 NP----------ETQF-----VGRTVEEDLAFGPENLCLPPIEIRKRVDRalaeigLEKYrhrsPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRkLAHRVAVMQNGRCVEQNYAATLFASPT 249
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
6.02e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.58 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGF-RHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveyLSGDIRFHGeSLLHASdQ 84
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK-----LSGSVSVPG-SIAYVS-Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 T---LRG-VRGNkiaMIFQEPMvslnplhtlEKQLYE-VL---SLHRGMrreaargEILNCLDR--VGIRQAAkrltdyp 154
Cdd:cd03250 74 EpwiQNGtIREN---ILFGKPF---------DEERYEkVIkacALEPDL-------EILPDGDLteIGEKGIN------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 hqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQGELNMG--MLFITHNLSIVRKlAHRVAVMQN 232
Cdd:cd03250 128 --LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLLNNktRILVTHQLQLLPH-ADQIVVLDN 202
|
..
gi 16130118 233 GR 234
Cdd:cd03250 203 GR 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
304-505 |
6.47e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ-----GSIIFDgqplQNL--NRRQLLPIR--------------- 361
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKST----LMKILNGEvllddGRIIYE----QDLivARLQQDPPRnvegtvydfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 362 ---------HRI-QVVFQDPNSSLnprLNVLQIIEEGLRvHQptlSAAQREQQVIAVMHEVGLDPETRHrypAEFSGGQR 431
Cdd:PRK11147 93 eqaeylkryHDIsHLVETDPSEKN---LNELAKLQEQLD-HH---NLWQLENRINEVLAQLGLDPDAAL---SSLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQkhqlAYLFISHDLHVVRALCHQVIILRQGEVV 505
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
273-484 |
9.31e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 273 STLLDVEQLQVAfpirkgilkriVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINS-------QGSIIFD 345
Cdd:CHL00131 5 KPILEIKNLHAS-----------VNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAGhpaykilEGDILFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 346 GQPLQNLN---RRQLlpirhRIQVVFQDP----------------NS--------SLNPrLNVLQIIEEGLRVhqptlsa 398
Cdd:CHL00131 70 GESILDLEpeeRAHL-----GIFLAFQYPieipgvsnadflrlayNSkrkfqglpELDP-LEFLEIINEKLKL------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 399 aqreqqviavmheVGLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILTLLKSLQq 473
Cdd:CHL00131 137 -------------VGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSEN- 202
|
250
....*....|.
gi 16130118 474 khqlAYLFISH 484
Cdd:CHL00131 203 ----SIILITH 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
301-506 |
1.07e-13 |
|
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: 71.09 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINS-QGSIIFDGQPLQNLnrrQLLPIRHRIQVVFQDP-------N 372
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKL---PLHTLRSRLSIILQDPilfsgsiR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPRLNVL-QIIEEGLRVHQPTLSAAQREQQVIAVMHEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03288 113 FNLDPECKCTdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 452 PTSSLDKTVQaqiltllKSLQQKHQLAY-----LFISHDLHVVRAlCHQVIILRQGEVVE 506
Cdd:cd03288 183 ATASIDMATE-------NILQKVVMTAFadrtvVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-236 |
1.33e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 23 TVVNDVSLQIEAGETLALVGESGSGKS--VTALSILrLLPSP-PVEYLSGDIRFHGESLLHASDQT-------------- 85
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPDTgTIEWIFKDEKNKKKTKEKEKVLEklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRgNKIAMIFQEPMVSLNPlHTLEKQL-YEVLSLhrGMRREAARGEILNCLDRVGIRQAAkrLTDYPHQLSGGERQR 164
Cdd:PRK13651 100 IKEIR-RRVGVVFQFAEYQLFE-QTIEKDIiFGPVSM--GVSKEEAKKRAAKYIELVGLDESY--LQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-237 |
1.39e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.83 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVeyLSGDIRFHGESLLH 80
Cdd:CHL00131 3 KNKPILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKS-TLSKVIAGHPAYKI--LEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 AsDQTLRGVRGnkIAMIFQEPM----VS--------------------LNPLhtlekQLYEVLSlhrgmrreaargeilN 136
Cdd:CHL00131 76 L-EPEERAHLG--IFLAFQYPIeipgVSnadflrlaynskrkfqglpeLDPL-----EFLEIIN---------------E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 137 CLDRVGIRQaaKRLTDYPHQ-LSGGERQRVMI-AMALLtRPELLIADEPTTALDVSVQAQILQLLRELQGELNmGMLFIT 214
Cdd:CHL00131 133 KLKLVGMDP--SFLSRNVNEgFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILIT 208
|
250 260
....*....|....*....|....*..
gi 16130118 215 H--NL--SIVRKLAHrvaVMQNGRCVE 237
Cdd:CHL00131 209 HyqRLldYIKPDYVH---VMQNGKIIK 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-236 |
1.85e-13 |
|
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: 69.21 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 10 NLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVEYLS--GDIRFHGesllHASDQTLR 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCS----TLLKALANRTEGNVSveGDIHYNG----IPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 88 GVRGNKIamifqepMVSLNPLH----TLEKQLYEVLSLhRGmrREAARGeilncldrvgirqaakrltdyphqLSGGERQ 163
Cdd:cd03233 80 KYPGEII-------YVSEEDVHfptlTVRETLDFALRC-KG--NEFVRG------------------------ISGGERK 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLS-IVRKLAHRVAVMQNGRCV 236
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-234 |
2.22e-13 |
|
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: 72.47 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPveyLSGDIRFHGESLlHASD 83
Cdd:COG4618 331 LSVENLTVVPPGSK--RPILRGVSFSLEPGEVLGVIGPSGSGKS----TLARLLVgvWPP---TAGSVRLDGADL-SQWD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRG----------------VRGNkIAMiFQEPmvslNPlhtlEKqlyeVLslhrgmrrEAARgeilncldRVGIRQAA 147
Cdd:COG4618 401 REELGrhigylpqdvelfdgtIAEN-IAR-FGDA----DP----EK----VV--------AAAK--------LAGVHEMI 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 148 KRLTD-Y-------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSI 219
Cdd:COG4618 451 LRLPDgYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSL 529
|
250
....*....|....*
gi 16130118 220 VRkLAHRVAVMQNGR 234
Cdd:COG4618 530 LA-AVDKLLVLRDGR 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-248 |
3.26e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 28 VSLQIEAGETLALVGESGSGKSVTALSILRLLPsppveYlSGDIRFHGESLLHASDQTLRgvrgNKIAMIFQEPmvslnp 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----Y-QGSLKINGIELRELDPESWR----KHLSWVGQNP------ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 108 lHTLEKQLYEVLSLHRGmrrEAARGEILNCLDRVGIRQAAKRLT---DYPHQ-----LSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK11174 433 -QLPHGTLRDNVLLGNP---DASDEQLQQALENAWVSEFLPLLPqglDTPIGdqaagLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 180 ADEPTTALDVSVQAQILQLLREL-QGELNmgmLFITHNLSivrKLAH--RVAVMQNGRCVEQNYAATLFASP 248
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAAsRRQTT---LMVTHQLE---DLAQwdQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-216 |
3.54e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENlsVGFRHQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQ 84
Cdd:PRK10247 7 LLQLQN--VGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPT----SGTLLFEGEDISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHRGMRREAA-RGEILNCLDRVGIRQAA--KRLTDyphqLSGGE 161
Cdd:PRK10247 78 IYR----QQVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPdPAIFLDDLERFALPDTIltKNIAE----LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHN 216
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
293-504 |
4.57e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 69.50 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 293 KRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDG-----QPLQNLnRRQLLPIRHRIQVV 367
Cdd:cd03289 11 KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswnsVPLQKW-RKAFGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 368 FQDPNSSLNPrlnvlqiieeglrvhqptlSAAQREQQVIAVMHEVGLDpETRHRYPAE-----------FSGGQRQRIAI 436
Cdd:cd03289 90 SGTFRKNLDP-------------------YGKWSDEEIWKVAEEVGLK-SVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 437 ARALILKPSLIILDEPTSSLDKtVQAQILTllKSLQQKHQLAYLFISHdlHVVRAL--CHQVIILRQGEV 504
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDP-ITYQVIR--KTLKQAFADCTVILSE--HRIEAMleCQRFLVIEENKV 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
297-504 |
5.61e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 71.87 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLN----RRQLLPIRHRIQVVFQDPN 372
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTlqtwRKAFGVIPQKVFIFSGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNPRlnvlqiieeglrvhqptlsAAQREQQVIAVMHEVGLDpETRHRYPAE-----------FSGGQRQRIAIARALI 441
Cdd:TIGR01271 1310 KNLDPY-------------------EQWSDEEIWKVAEEVGLK-SVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 442 LKPSLIILDEPTSSLDKtVQAQILTllKSLQQKHQLAYLFISHdlHVVRAL--CHQVIILRQGEV 504
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDP-VTLQIIR--KTLKQSFSNCTVILSE--HRVEALleCQQFLVIEGSSV 1429
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-232 |
7.27e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLhaSDQTLRGVRgNKIAMIFQEPMV 103
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPT----EGDIIINDSHNL--KDINLKWWR-SKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 --------------SLNPLHTLEKQL-------YEVLSLHRGMRREAAR--GEILNCLDRVGIRQAAKR----------- 149
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEALSNYYnedgndsQENKNKRNSCRAKCAGdlNDMSNTTDSNELIEMRKNyqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 150 ------LTDY---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNM 208
Cdd:PTZ00265 552 vskkvlIHDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|....
gi 16130118 209 GMLFITHNLSIVRkLAHRVAVMQN 232
Cdd:PTZ00265 632 ITIIIAHRLSTIR-YANTIFVLSN 654
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-248 |
7.54e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 15 FRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALS-ILRLLpsppvEYLSGDIRFHGESLLHASDQTLRGvrgnK 93
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSlIQRHF-----DVSEGDIRFHDIPLTKLQLDSWRS----R 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 94 IAMIFQEPM---------VSLNPLHTLEKQLYEV----------LSLHRGMRREaargeilncldrVGIRQAakrltdyp 154
Cdd:PRK10789 391 LAVVSQTPFlfsdtvannIALGRPDATQQEIEHVarlasvhddiLRLPQGYDTE------------VGERGV-------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqGElNMGMLFITHNLSIVRKlAHRVAVMQNGR 234
Cdd:PRK10789 451 -MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GE-GRTVIISAHRLSALTE-ASEILVMQHGH 526
|
250
....*....|....
gi 16130118 235 CVEQNYAATLFASP 248
Cdd:PRK10789 527 IAQRGNHDQLAQQS 540
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-234 |
7.58e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.86 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGESLlhasDQTLRGVRGnKIAMIFQep 101
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-----AGKITVLGVPV----PARARLARA-RIGVVPQ-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVSLNPLHTLEKQLYeVLSLHRGMRREAARGEILNCLDRVGI-RQAAKRLTDyphqLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK13536 122 FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLeSKADARVSD----LSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 181 DEPTTALDVSVQAQILQLLRELQGeLNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-489 |
8.89e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.58 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 33 EAGETLALVGESGSGKSvTALSIL--RLLP------SPP-----VEYLSG-DIRFHGESLlhaSDQTLRGVRgnKIAMIF 98
Cdd:COG1245 97 KKGKVTGILGPNGIGKS-TALKILsgELKPnlgdydEEPswdevLKRFRGtELQDYFKKL---ANGEIKVAH--KPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 99 QEPMVSLNPLHTLEKQLYEvlslhRGMRREAA-RGEILNCLDRvGIRQaakrltdyphqLSGGERQRVMIAMALLTRPEL 177
Cdd:COG1245 171 LIPKVFKGTVRELLEKVDE-----RGKLDELAeKLGLENILDR-DISE-----------LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMqngrcveqnyaatlFASP------THP 251
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL--------------YGEPgvygvvSKP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 252 Y-TQKLLNSEPSG-----------DPVPLPEPASTLLDVEQLQVAFPirkGILKRIVDHNVVVKniSFTLRAGETLGLVG 319
Cdd:COG1245 299 KsVRVGINQYLDGylpeenvrirdEPIEFEVHAPRREKEEETLVEYP---DLTKSYGGFSLEVE--GGEIREGEVLGIVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 320 ESGSGKSTtglaLLRLINS-----QGSIIFDgqplqnlnrrqlLPIRHRIQVVFQDPNSSlnprlnvlqiIEEGLR-VHQ 393
Cdd:COG1245 374 PNGIGKTT----FAKILAGvlkpdEGEVDED------------LKISYKPQYISPDYDGT----------VEEFLRsANT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 394 PTLSAAQREQQVIavmHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQILT--LLKSL 471
Cdd:COG1245 428 DDFGSSYYKTEII---KPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVakAIRRF 501
|
490
....*....|....*...
gi 16130118 472 QQKHQLAYLFISHDLHVV 489
Cdd:COG1245 502 AENRGKTAMVVDHDIYLI 519
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-215 |
9.20e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 3 QTLLAIENLSVGFRHQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppveylsgdirfhgesllhas 82
Cdd:COG2401 26 RVAIVLEAFGVELRVVE--RYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL----------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 dqtLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMrreaargEILNcldRVGIRQAAKRLTDYPHqLSGGER 162
Cdd:COG2401 77 ---AGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAV-------ELLN---AVGLSDAVLWLRRFKE-LSTGQK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALDVSVqAQILQL-LRELQGELNMGMLFITH 215
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATH 195
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-246 |
1.07e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLsvGFRHQQtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppveylSGDIRFHGESLLHaSD 83
Cdd:PRK13638 1 MLATSDL--WFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ------KGAVLWQGKPLDY-SK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRgNKIAMIFQEPmvslnplhtlEKQLYEV-------LSLhRGMrrEAARGEILNCLDRVGIRQAAKRLTDYPHQ 156
Cdd:PRK13638 70 RGLLALR-QQVATVFQDP----------EQQIFYTdidsdiaFSL-RNL--GVPEAEITRRVDEALTLVDAQHFRHQPIQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMgMLFITHNLSIVRKLAHRVAVMQNGRC 235
Cdd:PRK13638 136 cLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQI 214
|
250
....*....|.
gi 16130118 236 VEQNYAATLFA 246
Cdd:PRK13638 215 LTHGAPGEVFA 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-234 |
1.08e-12 |
|
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: 70.45 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSvgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppveYLSGDIRFHGESLlhasDQT 85
Cdd:TIGR01842 317 LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDGADL----KQW 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRGVRGNKIAMIFQEpmVSLNPlHTLEKQLYEvlslhrgMRREAARGEILNCLDRVGIRQAAKRLTD-YPHQ-------L 157
Cdd:TIGR01842 386 DRETFGKHIGYLPQD--VELFP-GTVAENIAR-------FGENADPEKIIEAAKLAGVHELILRLPDgYDTVigpggatL 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVrKLAHRVAVMQNGR 234
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGR 530
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-236 |
1.17e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpveylSGDIRFHGE--SLLHAS 82
Cdd:PRK10895 3 TLTAKNLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-----AGNIIIDDEdiSLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRGvrgnkIAMIFQEPmvSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGER 162
Cdd:PRK10895 74 ARARRG-----IGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGGER 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 163 QRVMIAMALLTRPELLIADEPTTALD-VSVQ--AQILQLLRelqgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVDpISVIdiKRIIEHLR----DSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-201 |
1.94e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPVEylsGDIRFHGESLLHASDQTLRgvrgnkiAMIFQ 99
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILAglARPDA---GEVLWQGEPIRRQRDEYHQ-------DLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EPMVSLNPLHTLEKQLYEVLSLHRGMRREAargeILNCLDRVGIRqaakRLTDYP-HQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQRLHGPGDDEA----LWEALAQVGLA----GFEDVPvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|...
gi 16130118 179 IADEPTTALDVSVQAQILQLLRE 201
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
302-508 |
3.81e-12 |
|
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: 65.36 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ--------GSIIFDGQPLQNLNRRqllpirHRIQVVFQDPNS 373
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCST----LLKALANRtegnvsveGDIHYNGIPYKEFAEK------YPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPRLNVLQiieeglrvhqpTLSAAQREQQviavmhevgldpetrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03233 93 VHFPTLTVRE-----------TLDFALRCKG---------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFI----SHDLHvvrALCHQVIILRQGEVVEQG 508
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSDEIY---DLFDKVLVLYEGRQIYYG 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-247 |
7.17e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 1 MTQTLLAIENLSVGFRHQQtvrtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPvEYLSGDIRFHGESLLH 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDP-RATSGRIVFDGKDITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 81 AsdQTLRGVRgNKIAMIFQEPMVSLNplHTLEKQLyevlsLHRGMRreAARGEILNCLDRVgiRQAAKRLTDYPHQ---- 156
Cdd:PRK11614 72 W--QTAKIMR-EAVAIVPEGRRVFSR--MTVEENL-----AMGGFF--AERDQFQERIKWV--YELFPRLHERRIQragt 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
250
....*....|.
gi 16130118 237 EQNYAATLFAS 247
Cdd:PRK11614 217 LEDTGDALLAN 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
301-490 |
8.16e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLR---------------------------------------------- 334
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 335 ---------LINSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPnssLNPRLNVLQIIEEGLRvhQPTLSAAQREQQV 405
Cdd:PTZ00265 1263 eggsgedstVFKNSGKILLDGVDICDYNLKDL---RNLFSIVSQEP---MLFNMSIYENIKFGKE--DATREDVKRACKF 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 406 IAV---------MHEVGLDPetrhrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQ 476
Cdd:PTZ00265 1335 AAIdefieslpnKYDTNVGP-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD 1409
|
250
....*....|....
gi 16130118 477 LAYLFISHDLHVVR 490
Cdd:PTZ00265 1410 KTIITIAHRIASIK 1423
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
301-505 |
1.63e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.13 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTT-GLALLRLINSQGSIIFDGQPLQNLNRRQLLpiRHRIQVVfqdPNSSlnpRL 379
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLlGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAVAIV---PEGR---RV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 380 NVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
Cdd:PRK11614 92 FSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130118 460 VQAQILTLLKSLQQKHQLAYLfISHDLHVVRALCHQVIILRQGEVV 505
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFL-VEQNANQALKLADRGYVLENGHVV 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-236 |
4.54e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPpveyLSGDIRFHGESLlhaSDQTLRgvrgnKIAMIFQ 99
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKS-TLLNALagRIQGNN----FTGTILANNRKP---TKQILK-----RTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EPMvsLNPLHTLEKQLY--EVLSLHRGMRREAARGEILNCLDRVGIRQAAKRL--TDYPHQLSGGERQRVMIAMALLTRP 175
Cdd:PLN03211 148 DDI--LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 176 ELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
299-503 |
4.60e-11 |
|
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: 62.10 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 299 NVVVKNISFTLRAGETLGLVGESGSGKSTTGLALL-RLINSQGSIIFDGqplqnlnrrqllpirhRIQVVFQDP---NSS 374
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSVPG----------------SIAYVSQEPwiqNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LnpRLNVL---QIIEEglRVHQpTLSAAQREQQvIAVMH-----EVG-----LdpetrhrypaefSGGQRQRIAIARALI 441
Cdd:cd03250 82 I--RENILfgkPFDEE--RYEK-VIKACALEPD-LEILPdgdltEIGekginL------------SGGQKQRISLARAVY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 442 LKPSLIILDEPTSSLDKTVQAQILT--LLKSLQQK-------HQLAYLfiSHdlhvvralCHQVIILRQGE 503
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNktrilvtHQLQLL--PH--------ADQIVVLDNGR 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-247 |
4.85e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 16 RHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvEYLSGDIRFHGeslLHASDQTLRGVRgNKIA 95
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN-----ESAEGEIIIDG---LNIAKIGLHDLR-FKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 96 MIFQEPMV-------SLNPLHTL-EKQLYEVLSLHRGMRREAARGEILNcldrvgirqaaKRLTDYPHQLSGGERQRVMI 167
Cdd:TIGR00957 1364 IIPQDPVLfsgslrmNLDPFSQYsDEEVWWALELAHLKTFVSALPDKLD-----------HECAEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRElQGElNMGMLFITHNLSIVRKLAhRVAVMQNGRCVEQNYAATLFAS 247
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
301-518 |
1.16e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDP-------N 372
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKFGLMDL---RKVLGIIPQAPvlfsgtvR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSLNP--RLNVLQIIEEGLRVHqptLSAAQREqqviavmHEVGLDPETrhrypAE----FSGGQRQRIAIARALILKPSL 446
Cdd:PLN03130 1331 FNLDPfnEHNDADLWESLERAH---LKDVIRR-------NSLGLDAEV-----SEagenFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 447 IILDEPTSSLDKTVQAQIltlLKSLQQKHQ-LAYLFISHDLHVVRAlCHQVIILRQGEVVEqgpcarvFATPQ 518
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALI---QKTIREEFKsCTMLIIAHRLNTIID-CDRILVLDAGRVVE-------FDTPE 1457
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
1.41e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLP--SPPVeylSGDIRFHGEsllhasDQTLRGVR------GNK 93
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKT----TLLRLIAglLPPA---AGTIKLDGG------DIDDPDVAeachylGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 94 IAMifqepmvslNPLHTLEkqlyEVLSLHRGMRReAARGEILNCLDRVGIRqaakRLTDYPHQ-LSGGERQRVMIAMALL 172
Cdd:PRK13539 82 NAM---------KPALTVA----ENLEFWAAFLG-GEELDIAAALEAVGLA----PLAHLPFGyLSAGQKRRVALARLLV 143
|
170 180
....*....|....*....|....*....
gi 16130118 173 TRPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-234 |
1.42e-10 |
|
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: 63.69 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVgFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveylsgdiRFHGESLLHASDQ 84
Cdd:TIGR02633 257 ILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG----------KFEGNVFINGKPV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGVR---GNKIAMIFQE-------PMVSLNPLHTLEkqlyeVLSLHRGMRR---EAARGEILNCLDRVGIRQAAKRLT 151
Cdd:TIGR02633 326 DIRNPAqaiRAGIAMVPEDrkrhgivPILGVGKNITLS-----VLKSFCFKMRidaAAELQIIGSAIQRLKVKTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 dyPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:TIGR02633 401 --IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIG 477
|
...
gi 16130118 232 NGR 234
Cdd:TIGR02633 478 EGK 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
306-457 |
5.54e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 306 SFTLRAGETLGLVGESGSGKSTtglaLLRLINSQGsiiFDGQPlQNLNrrqllpIRHRIQVVFQDPNSSLNPRLNV---- 381
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTT----FLRYMAMHA---IDGIP-KNCQ------ILHVEQEVVGDDTTALQCVLNTdier 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 382 LQIIEEGLRVHQPTL----------------------SAAQR----------------EQQVIAVMHEVGLDPETRHRYP 423
Cdd:PLN03073 263 TQLLEEEAQLVAQQRelefetetgkgkgankdgvdkdAVSQRleeiykrlelidaytaEARAASILAGLSFTPEMQVKAT 342
|
170 180 190
....*....|....*....|....*....|....
gi 16130118 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-232 |
6.23e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHQQTVRT-VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP-------------------------- 60
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 61 -------------SPPVEYLSGD----IRFHGESLLHA---SDQTLRGVRgNKIAMIFQEPMVslnplhtLEKQLYEVLS 120
Cdd:PTZ00265 1246 eeqnvgmknvnefSLTKEGGSGEdstvFKNSGKILLDGvdiCDYNLKDLR-NLFSIVSQEPML-------FNMSIYENIK 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 121 LHRgmrREAARGEILNCLDRVGIRQAAKRLTD--------YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQ 192
Cdd:PTZ00265 1318 FGK---EDATREDVKRACKFAAIDEFIESLPNkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16130118 193 AQILQLLRELQGELNMGMLFITHNLSIVRKlAHRVAVMQN 232
Cdd:PTZ00265 1395 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-253 |
7.53e-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: 59.54 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQT 85
Cdd:cd03288 20 IKIHDLCV--RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM-----VDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LRgvrgNKIAMIFQEPMV-------SLNPLHTL-EKQLYEVLSLH--RGMRREAARGeilncLDRVgirqaakrLTDYPH 155
Cdd:cd03288 93 LR----SRLSIILQDPILfsgsirfNLDPECKCtDDRLWEALEIAqlKNMVKSLPGG-----LDAV--------VTEGGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaQILQLLrELQGELNMGMLFITHNLSIVRKlAHRVAVMQNGRC 235
Cdd:cd03288 156 NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGIL 232
|
250
....*....|....*...
gi 16130118 236 VEQNYAATLFASPTHPYT 253
Cdd:cd03288 233 VECDTPENLLAQEDGVFA 250
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
302-480 |
8.59e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.88 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLnprLNV 381
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL---LNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 382 lqIIEEGLRVHQPTlsAAQREQQVI---AVMHEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03290 94 --TVEENITFGSPF--NKQRYKAVTdacSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 16130118 455 SL-----DKTVQAQILTLLKSLQQ-----KHQLAYL 480
Cdd:cd03290 170 ALdihlsDHLMQEGILKFLQDDKRtlvlvTHKLQYL 205
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
303-471 |
1.48e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.64 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 303 KNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ-------GSIIFDGQPLqnlnrrqllPIRHRIQVVFQDPNSSL 375
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTT----LLDVLAGRktagvitGEILINGRPL---------DKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 376 NPRLNVlqiiEEGLRvhqptLSAAQReqqviavmhevGLDPEtrhrypaefsggQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:cd03232 91 SPNLTV----REALR-----FSALLR-----------GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSG 138
|
170
....*....|....*.
gi 16130118 456 LDKTVQAQILTLLKSL 471
Cdd:cd03232 139 LDSQAAYNIVRFLKKL 154
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-230 |
1.48e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 35 GETLALVGESGSGKSvTALSIL--RLLP------SPPveylSGD--IRFHGESLLHasdQTLRGVRGNKIAMIFQEPMVS 104
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALKILagKLKPnlgkfdDPP----DWDeiLDEFRGSELQ---NYFTKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPlHTLEKQLYEVLSlhrgmrREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:cd03236 98 LIP-KAVKGKVGELLK------KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130118 185 TALDVSVQAQILQLLRELQGELNmGMLFITHNLSIVRKLAHRVAVM 230
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-197 |
5.29e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppveylSGDIRFHGESLLHASDQT 85
Cdd:TIGR01271 1218 MDVQGLTA--KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LR---GVRGNKIAMIFQEPMVSLNPLHTLEKQlyevlslhrgmrreaargEILNCLDRVGIRQAAKR--------LTDYP 154
Cdd:TIGR01271 1290 WRkafGVIPQKVFIFSGTFRKNLDPYEQWSDE------------------EIWKVAEEVGLKSVIEQfpdkldfvLVDGG 1351
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130118 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQ 197
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIR 1393
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
301-503 |
7.60e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.79 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALL-RLINSQGSIifdgqplqnlnrrqllpiRHRIQVVFQDPNSSLNP-- 377
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKI------------------KHSGRISFSSQFSWIMPgt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 -RLNVLQIIEEGLRVHQPTLSAAQREQQVIA-------VMHEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLIIL 449
Cdd:cd03291 114 iKENIIFGVSYDEYRYKSVVKACQLEEDITKfpekdntVLGEGGIT----------LSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130118 450 DEPTSSLDKTVQAQIL--TLLKSLQQKHQLayLFISHDLHVVRAlcHQVIILRQGE 503
Cdd:cd03291 184 DSPFGYLDVFTEKEIFesCVCKLMANKTRI--LVTSKMEHLKKA--DKILILHEGS 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-236 |
9.93e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 4 TLLAIENLSVgfRH-QQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSIL-----RllpsppveYLSGDIRFHGES 77
Cdd:NF040905 256 VVFEVKNWTV--YHpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygR--------NISGTVFKDGKE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 78 LlhasdqTLRGVR---GNKIA----------MIFQEPM---VSLNPLHTLEKqlYEVLSLHRGMR-----REAARGEILN 136
Cdd:NF040905 326 V------DVSTVSdaiDAGLAyvtedrkgygLNLIDDIkrnITLANLGKVSR--RGVIDENEEIKvaeeyRKKMNIKTPS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 137 CLDRVGirqaakrltdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL--QGelnMGMLFIT 214
Cdd:NF040905 398 VFQKVG-------------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELaaEG---KGVIVIS 461
|
250 260
....*....|....*....|..
gi 16130118 215 HNLSIVRKLAHRVAVMQNGRCV 236
Cdd:NF040905 462 SELPELLGMCDRIYVMNEGRIT 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-262 |
1.50e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 7 AIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQTL 86
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI-----VELERGRILIDGCDISKFGLMDL 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RGVRGnkiaMIFQEPMV-------SLNPL--HTlEKQLYEvlSLHRGMRREAARGEILNcLDrvgirqaaKRLTDYPHQL 157
Cdd:PLN03130 1312 RKVLG----IIPQAPVLfsgtvrfNLDPFneHN-DADLWE--SLERAHLKDVIRRNSLG-LD--------AEVSEAGENF 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqgEL-NMGMLFITHNLSIVRKlAHRVAVMQNGRCV 236
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE---EFkSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
250 260
....*....|....*....|....*.
gi 16130118 237 EqnyaatlFASPthpytQKLLNSEPS 262
Cdd:PLN03130 1452 E-------FDTP-----ENLLSNEGS 1465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-236 |
1.53e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 125 MRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQG 204
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAA---AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110
....*....|....*....|....*....|..
gi 16130118 205 ElNMGMLFITHNLSIVRKLAHRVAVMQNGRCV 236
Cdd:NF000106 193 D-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-262 |
1.56e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLLHASDQTLRGVrgn 92
Cdd:PLN03232 1240 VHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI-----VELEKGRIMIDDCDVAKFGLTDLRRV--- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 93 kIAMIFQEPMV-------SLNPL--HTlEKQLYEvlSLHRGMRREAARGEILNcLDrvgirqaaKRLTDYPHQLSGGERQ 163
Cdd:PLN03232 1312 -LSIIPQSPVLfsgtvrfNIDPFseHN-DADLWE--ALERAHIKDVIDRNPFG-LD--------AEVSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqgEL-NMGMLFITHNLSIVRKlAHRVAVMQNGRCVEQNYAA 242
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE---EFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQ 1454
|
250 260
....*....|....*....|
gi 16130118 243 TLFASPTHPYTQKLLNSEPS 262
Cdd:PLN03232 1455 ELLSRDTSAFFRMVHSTGPA 1474
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
312-500 |
1.75e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.53 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 312 GETLGLVGESGSGKSTTGLALLRLINSQGS--IIFDGQPLQNLNRRQLLPIRhriqvvfqdpnsslnprlnvlqiieegl 389
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 390 rvhqptlsaaqreqqviavmhevgldpetRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL---- 465
Cdd:smart00382 54 -----------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLllee 104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130118 466 -TLLKSLQQKHQLAYLFISH------DLHVVRALCHQVIILR 500
Cdd:smart00382 105 lRLLLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLL 146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
304-508 |
1.77e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 304 NISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPlqnlnrrQLLPIrhriqvvfqdpNSSLNPR 378
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKST----LSNLIAgvtmpNKGTVDIKGSA-------ALIAI-----------SSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIE-EGLRVHQPTLSAAQREQQVIAvMHEVGldpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK13545 100 LTGIENIElKGLMMGLTKEKIKEIIPEIIE-FADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 458 KTVQAQILTLLKSLQQKHQLAYlFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
306-515 |
1.92e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 306 SFTLRAGETLGLVGESGSGKSTTGLALL-RLINSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPNSSL------NPR 378
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAgELPLLSGERQSQFSHITRLSFEQL---QKLVSDEWQRNNTDMlspgedDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 379 LNVLQIIEEGlrVHQPTLSAAQREQQVIAVMhevgLDpeTRHRYpaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
Cdd:PRK10938 100 RTTAEIIQDE--VKDPARCEQLAQQFGITAL----LD--RRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 459 TVQAQILTLLKSLQQKhQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFA 515
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-457 |
2.36e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-----------RLLPSPPVEYLSGdirfhgESLLHASdQTLRGV- 89
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMagvdkefegeaRPAPGIKVGYLPQ------EPQLDPE-KTVRENv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 90 ------------RGNKIAMIFQEPMVSLNPLhtLEKQ--LYEVLslhrgmrrEAARGEILnclDRVgIRQAAKRL----T 151
Cdd:PRK11819 92 eegvaevkaaldRFNEIYAAYAEPDADFDAL--AAEQgeLQEII--------DAADAWDL---DSQ-LEIAMDALrcppW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVqAQILQLLRELQGELnmgmLFITHN-----------LS 218
Cdd:PRK11819 158 DAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSV-AWLEQFLHDYPGTV----VAVTHDryfldnvagwiLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 219 IVRklahrvavmqnGRCV--EQNYAATLF----------------------------ASP------------------TH 250
Cdd:PRK11819 233 LDR-----------GRGIpwEGNYSSWLEqkakrlaqeekqeaarqkalkrelewvrQSPkarqakskarlaryeellSE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 251 PYTQKLLNSE---PSGdpvplPEPASTLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKST 327
Cdd:PRK11819 302 EYQKRNETNEifiPPG-----PRLGDKVIEAENLSKSF-----------GDRLLIDDLSFSLPPGGIVGIIGPNGAGKST 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 328 tglaLLRLINSQ-----GSIIfdgqplqnlnrrqllpIRHRIQVVFQDPN-SSLNPRLNVLQIIEEGLRVhqptLSAAQR 401
Cdd:PRK11819 366 ----LFKMITGQeqpdsGTIK----------------IGETVKLAYVDQSrDALDPNKTVWEEISGGLDI----IKVGNR 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130118 402 E----------------QQVIavmheVGldpetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK11819 422 EipsrayvgrfnfkggdQQKK-----VG-----------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
301-502 |
2.83e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 301 VVKNISFTLRAGETLGLVGESGSGKSTTGLALL-RLINSQGSIifdgqplqnlnrrqllpiRHRIQVVFQDPNSSLNP-- 377
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKI------------------KHSGRISFSPQTSWIMPgt 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 -RLNVLQIIEEGLRVHQPTLSAAQREQqviavmhEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:TIGR01271 503 iKDNIIFGLSYDEYRYTSVIKACQLEE-------DIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 453 TSSLDKTVQAQIL--TLLKSLQQKHQLayLFISHDLHVVRAlcHQVIILRQG 502
Cdd:TIGR01271 576 FTHLDVVTEKEIFesCLCKLMSNKTRI--LVTSKLEHLKKA--DKILLLHEG 623
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
305-370 |
3.39e-08 |
|
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: 55.96 E-value: 3.39e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 305 ISFTLRAGETLGLVGESGSGKSTtglaLLRLIN-----SQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQD 370
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKST----LAKLLTglyrpESGEILLDGQPVTADNREAY---RQLFSAVFSD 414
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-227 |
3.86e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpVEYLSGDIRFHGESLL------ 79
Cdd:PRK15064 320 LEVENLTKGFDN----GPLFKNLNLLLEAGERLAIIGENGVGKT----TLLRTLVGE-LEPDSGTVKWSENANIgyyaqd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 80 HASDqtlrgvrgnkiamiFQEPMvslnplhtlekQLYEVLSLHR--GMRREAARGeilnCLDRV-----GIRQAAKrltd 152
Cdd:PRK15064 391 HAYD--------------FENDL-----------TLFDWMSQWRqeGDDEQAVRG----TLGRLlfsqdDIKKSVK---- 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAqiLQL-LRELQGELnmgmLFITHNLSIVRKLAHRV 227
Cdd:PRK15064 438 ---VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNMaLEKYEGTL----IFVSHDREFVSSLATRI 505
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
287-485 |
4.60e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 287 IRKGILkrivdhnVVVKNISFTLRAGETLGLVGESGSGKSTTgLALLR--LINSQGSIIFDGQ-PLQNLNRRQLLPIRHR 363
Cdd:PRK10636 9 IRRGVR-------VLLDNATATINPGQKVGLVGKNGCGKSTL-LALLKneISADGGSYTFPGNwQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 364 IQVVFQDPNS--SLNPRLNVLQIIEEG-----LRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAI 436
Cdd:PRK10636 81 LEYVIDGDREyrQLEAQLHDANERNDGhaiatIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16130118 437 ARALILKPSLIILDEPTSSLDKTVQAQILTLLKSlqqkHQLAYLFISHD 485
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS----YQGTLILISHD 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-504 |
7.61e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILR--------------------------LLPSPPVEY-LSGDIRF 73
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKS-TLLALLKneisadggsytfpgnwqlawvnqetpALPQPALEYvIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 74 HG--ESLLHASDQTlrgvRGNKIAmifqepmvslnplhTLEKQLYEVLSLhrGMRREAArgeilNCLDRVGIRQaaKRLT 151
Cdd:PRK10636 92 RQleAQLHDANERN----DGHAIA--------------TIHGKLDAIDAW--TIRSRAA-----SLLHGLGFSN--EQLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELnmgmLFITHNLS----IVRKLAH-- 225
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDfldpIVDKIIHie 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 226 --------------------RVAVMQNGRCVEQNYAATL------FASPTHPYTQ-----KLLNS----EPSG------- 263
Cdd:PRK10636 221 qqslfeytgnyssfevqratRLAQQQAMYESQQERVAHLqsyidrFRAKATKAKQaqsriKMLERmeliAPAHvdnpfhf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 264 ---DPVPLPEPastLLDVEQLQVAFpirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTTgLALL--RLINS 338
Cdd:PRK10636 301 sfrAPESLPNP---LLKMEKVSAGY-----------GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTL-IKLLagELAPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 339 QGSI-IFDGQPLQNLNRRQLLPIRhriqvvfqdpnsslnprlnvlqiIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPE 417
Cdd:PRK10636 366 SGEIgLAKGIKLGYFAQHQLEFLR-----------------------ADESPLQHLARLAPQELEQKLRDYLGGFGFQGD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 418 TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQkhqlAYLFISHDLHVVRALCHQVI 497
Cdd:PRK10636 423 KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLY 498
|
....*..
gi 16130118 498 ILRQGEV 504
Cdd:PRK10636 499 LVHDGKV 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-504 |
8.16e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 10 NLSVGFRHqqtvrtVVNDVSLQIEAGETLALVGESGSGKSV----TALSILRLLPSP----PVE-------------YLS 68
Cdd:PLN03073 184 SISVGGRD------LIVDASVTLAFGRHYGLVGRNGTGKTTflryMAMHAIDGIPKNcqilHVEqevvgddttalqcVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 69 GDIR----FHGESLLHASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILncldrVGIR 144
Cdd:PLN03073 258 TDIErtqlLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASIL-----AGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 145 QAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDV----------------------------SVQAQIL 196
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLhavlwletyllkwpktfivvshareflnTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 197 QL----------------------LRELQGELNMGMLFITHNLSIVRKL---AHRVAVMQNG-RCVEQ-NYAATLFASPT 249
Cdd:PLN03073 413 HLhgqklvtykgdydtfertreeqLKNQQKAFESNERSRSHMQAFIDKFrynAKRASLVQSRiKALDRlGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 250 HPYTQkllnsepsgdPVPLPEPASTLLDVEQLQVAFPirkgilkrivDHNVVVKNISFTLRAGETLGLVGESGSGKSTtg 329
Cdd:PLN03073 493 YKFEF----------PTPDDRPGPPIISFSDASFGYP----------GGPLLFKNLNFGIDLDSRIAMVGPNGIGKST-- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 330 laLLRLINSqgsiifDGQPLQNLNRRQllpIRHRIQVVFQDP----NSSLNPRLNVLQ----IIEEGLRVHQPTLsaaqr 401
Cdd:PLN03073 551 --ILKLISG------ELQPSSGTVFRS---AKVRMAVFSQHHvdglDLSSNPLLYMMRcfpgVPEQKLRAHLGSF----- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 402 eqqviAVMHEVGLDPETrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILTLLkslqqKHQLAYL 480
Cdd:PLN03073 615 -----GVTGNLALQPMY------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLV-----LFQGGVL 678
|
570 580
....*....|....*....|....
gi 16130118 481 FISHDLHVVRALCHQVIILRQGEV 504
Cdd:PLN03073 679 MVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-237 |
1.50e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 13 VGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVEYLSGDIRFHGESLlhaSDQTLRGVRgN 92
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-----VEVCGGEIRVNGREI---GAYGLRELR-R 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 93 KIAMIFQEPM-----VSLNPLHTLEKQLYEV---LSLhRGMR-REAARGEilncldrvGIRQaakRLTDYPHQLSGGERQ 163
Cdd:PTZ00243 1385 QFSMIPQDPVlfdgtVRQNVDPFLEASSAEVwaaLEL-VGLReRVASESE--------GIDS---RVLEGGSNYSVGQRQ 1452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 164 RVMIAMALLTRPELLI-ADEPTT----ALDVSVQAQILQLLRelqgelNMGMLFITHNLSIVRKLaHRVAVMQNGRCVE 237
Cdd:PTZ00243 1453 LMCMARALLKKGSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAE 1524
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
287-526 |
1.85e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 287 IRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQ---------GSIIFDGQPLQNLNRRql 357
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCST----LLKTIASNtdgfhigveGVITYDGITPEEIKKH-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 358 lpirHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPT-----LSAAQREQQVIAV-MHEVGLDPETRHRYPAEF----S 427
Cdd:TIGR00956 136 ----YRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrpdgVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 428 GGQRQRIAIARALILKPSLIILDEPTSSLD-----------KTvQAQIL--TLLKSLQQKHQLAY-LFishdlhvvralc 493
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDsatalefiralKT-SANILdtTPLVAIYQCSQDAYeLF------------ 278
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 16130118 494 HQVIILRQGEVVEQGPCARV--------FATPQQEYTRQLL 526
Cdd:TIGR00956 279 DKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDRQTTADFL 319
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
417-508 |
2.11e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHVVRALCHQV 496
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHEL 214
|
90
....*....|..
gi 16130118 497 IILRQGEVVEQG 508
Cdd:NF000106 215 TVIDRGRVIADG 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-219 |
2.83e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppveylsgdirfhGEsLLHASDQTLRGVRGNKIAMIFQEPMV 103
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKS----SLFRIL---------------GE-LWPVYGGRLTKPAKGKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 SLNplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:TIGR00954 527 TLG---TLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRelqgELNMGMLFITHNLSI 219
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSL 641
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-208 |
4.10e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 11 LSVGFR-----HQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVEYL---SGDIRFHGesllHAS 82
Cdd:TIGR00956 58 LTRGFRklkkfRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCS----TLLKTIASNTDGFHigvEGVITYDG----ITP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 83 DQTLRGVRGNKIamifqepMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRvgirqaAKRLTDY-------PH 155
Cdd:TIGR00956 130 EEIKKHYRGDVV-------YNAETDVHFPHLTVGETLDFAARCKTPQNRPDGVSREEY------AKHIADVymatyglSH 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 156 Q------------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNM 208
Cdd:TIGR00956 197 TrntkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDT 261
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
292-509 |
4.51e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.46 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 292 LKRIVDHNVvvKNISFTLRAGETLGLVGESGSGKSTtglallrLINSqgsIIFDGqpLQN-LNRRQLLPIRH-------- 362
Cdd:cd03271 3 LKGARENNL--KNIDVDIPLGVLTCVTGVSGSGKSS-------LIND---TLYPA--LARrLHLKKEQPGNHdriegleh 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 363 --RIQVVFQDP---NSSLNP---------------------RLN--VLQI--------------IEEGLRV--HQPTLSA 398
Cdd:cd03271 69 idKVIVIDQSPigrTPRSNPatytgvfdeirelfcevckgkRYNreTLEVrykgksiadvldmtVEEALEFfeNIPKIAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 399 aqreqqVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALiLKPS----LIILDEPTSSLDKTVQAQILTLLKSLQQK 474
Cdd:cd03271 149 ------KLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDK 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 16130118 475 HQLAyLFISHDLHVVRAlCHQVIIL------RQGEVVEQGP 509
Cdd:cd03271 222 GNTV-VVIEHNLDVIKC-ADWIIDLgpeggdGGGQVVASGT 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-234 |
6.13e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTaLSILRLLPSPPveylSGDIRFHGESLlhasDQTLRGVRgNKIAMIFQEP 101
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTGLLPPT----SGTVLVGGKDI----ETNLDAVR-QSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 102 MVsLNPLHTLEKQLYevLSLHRGMRREAARGEILNCLDRVGIRQaaKRlTDYPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:TIGR01257 1013 IL-FHHLTVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTGLHH--KR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130118 182 EPTTALDVSVQAQILQLLreLQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
427-503 |
6.61e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 427 SGGQRQ------RIAIARALILKPSLIILDEPTSSLDK-TVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIIL 499
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 16130118 500 RQGE 503
Cdd:cd03240 197 KDGR 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
148-229 |
7.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 148 KRLTDyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRV 227
Cdd:PRK13409 449 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
..
gi 16130118 228 AV 229
Cdd:PRK13409 525 MV 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-236 |
7.92e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLpSPPVEYLSGDIRFHGESLLhasdQTLRGVRGNkiaMIFQEPMVS 104
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTT----FKML-TGDTTVTSGDATVAGKSIL----TNISDVHQN---MGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARL-RGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 185 TALDVSVQAQ----ILQLLRElqgelNMGMLFITHNLSIVRKLAHRVAVMQNG--RCV 236
Cdd:TIGR01257 2099 TGMDPQARRMlwntIVSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGafQCL 2151
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
8-234 |
8.12e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVgfrhqQTVRTVVNDVSLQIEAGETLaLVGESGSGKSvtalSILRLLpsppvEY-LSGDIRFHGESLLHASDQTL 86
Cdd:cd03240 1 IDKLSI-----RNIRSFHERSEIEFFSPLTL-IVGQNGAGKT----TIIEAL-----KYaLTGELPPNSKGGAHDPKLIR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RGVRGNKIAMIFQEPmvslnplhtlEKQLYEVlslhrgmRREAArgEILNCldrVGIRQ--AAKRLTDYPHQLSGGERQ- 163
Cdd:cd03240 66 EGEVRAQVKLAFENA----------NGKKYTI-------TRSLA--ILENV---IFCHQgeSNWPLLDMRGRCSGGEKVl 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 164 -----RVMIAMALLTRPELLIADEPTTALDV-SVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGR 234
Cdd:cd03240 124 asliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-206 |
8.44e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVEYLSGDIRF-HGESLLHASD 83
Cdd:PRK10636 312 LLKMEKVSAGYGD----RIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLL-AGELAPVSGEIGLaKGIKLGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 84 QTLRGVRGNKIAMifqEPMVSLNPlHTLEKQLYEVLSlhrgmrreaargeilncldrvGIRQAAKRLTDYPHQLSGGERQ 163
Cdd:PRK10636 383 HQLEFLRADESPL---QHLARLAP-QELEQKLRDYLG---------------------GFGFQGDKVTEETRRFSGGEKA 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGEL 206
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-197 |
8.52e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.62 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 6 LAIENLSVgfRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppveYLSGDIRFHGESLLHASDQT 85
Cdd:cd03289 3 MTVKDLTA--KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 86 LR---GVRGNKIaMIFQEPM-VSLNPLHTLEKQlyevlslhrgmrreaargEILNCLDRVGIRQAAKR--------LTDY 153
Cdd:cd03289 75 WRkafGVIPQKV-FIFSGTFrKNLDPYGKWSDE------------------EIWKVAEEVGLKSVIEQfpgqldfvLVDG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130118 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQ 197
Cdd:cd03289 136 GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIR 178
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
297-471 |
8.95e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 297 DHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINsqGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSsln 376
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHL--- 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 PRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMHEVGLDpetrhRY-------PAE-FSGGQRQRIAIARALILKPSLI 447
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPkSVSKSEKMEYVEEVIKLLEME-----SYadavvgvPGEgLNVEQRKRLTIGVELVAKPKLL 923
|
170 180
....*....|....*....|....*
gi 16130118 448 I-LDEPTSSLDKTVQAQILTLLKSL 471
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-217 |
1.07e-06 |
|
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: 49.64 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILrllpsPPVEYLSGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEPMVs 104
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL-----GEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPlhTLE----------KQLYEVLSLHRGMRREAargEILNCLDRVGIRQAAKrltdyphQLSGGERQRVMIAMALLTR 174
Cdd:cd03290 91 LNA--TVEenitfgspfnKQRYKAVTDACSLQPDI---DLLPFGDQTEIGERGI-------NLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130118 175 PELLIADEPTTALDVSV-----QAQILQLLRELQGELnmgmLFITHNL 217
Cdd:cd03290 159 TNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKL 202
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-237 |
1.07e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 5 LLAIENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSilrLLPSPPVEYLSGDIRFHGESLLHASDQ 84
Cdd:PRK09580 1 MLSIKDLHVSVED----KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFKGKDLLELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 85 TLRGvrgNKIAMIFQEPMvslnPLHTLEKQLYEVLSLHrgMRREAARGEILNCLDRVGIRQAAKRLTDYPHQL------- 157
Cdd:PRK09580 74 DRAG---EGIFMAFQYPV----EIPGVSNQFFLQTALN--AVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 158 --SGGERQRVMI-AMALLtRPELLIADEPTTALDVSVQAQILQLLRELQGElNMGMLFITHNLSIVRKLA-HRVAVMQNG 233
Cdd:PRK09580 145 gfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQG 222
|
....
gi 16130118 234 RCVE 237
Cdd:PRK09580 223 RIVK 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
302-502 |
1.29e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTglalLRLINSQGSIIFDGQPLQNLNrrqllpIRHRIQVVFQdpNSSLNPRLNV 381
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTVTSGDATVAGKS------ILTNISDVHQ--NMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 382 LQII---EEGLRVHQPTLSAAQREQQVIA--VMHEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:TIGR01257 2023 IDDLltgREHLYLYARLRGVPAEEIEKVAnwSIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16130118 457 DKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIILRQG 502
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
310-488 |
1.61e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 310 RAGETLGLVGESGSGKSTTgLALL--RLINSQGS---------II--FDGQPLQN----LNRRQLLPIrHRIQVVFQDPN 372
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTA-LKILagKLKPNLGKfddppdwdeILdeFRGSELQNyftkLLEGDVKVI-VKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 373 SSlnpRLNVLQIIEeglRVHQptlsaaqREQQVIaVMHEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03236 102 AV---KGKVGELLK---KKDE-------RGKLDE-LVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 16130118 453 TSSLDKTVQAQILTLLKSLqQKHQLAYLFISHDLHV 488
Cdd:cd03236 167 SSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAV 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
302-508 |
1.70e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTgLALLR--LINSQGSIIFDGQPLQ-NLNR-RQLLPIRHRIQVVFQdpnsslnp 377
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTT-LSILTglLPPTSGTVLVGGKDIEtNLDAvRQSLGMCPQHNILFH-------- 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 378 RLNVLQIIEEGLRVHQPTLSAAQREQQviAVMHEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGRSWEEAQLEME--AMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16130118 458 KTVQAQILTLLksLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQG 508
Cdd:TIGR01257 1094 PYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
298-490 |
1.76e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVvvKNISFTLRAGETLGLVGESGSGKSTtglallrlinsqgsIIFDGQPLQNLNR-RQLLPIRHRIQVVFQDPNSSLN 376
Cdd:cd03238 9 HNL--QNLDVSIPLNVLVVVTGVSGSGKST--------------LVNEGLYASGKARlISFLPKFSRNKLIFIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 prlnvlqiieeglrvhqptlsaaqreqqviavmhEVGLDPETRHRYPAEFSGGQRQRIAIARALI--LKPSLIILDEPTS 454
Cdd:cd03238 73 ----------------------------------DVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPST 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 16130118 455 SLDKTVQAQILTLLKSL-QQKHQLAYlfISHDLHVVR 490
Cdd:cd03238 119 GLHQQDINQLLEVIKGLiDLGNTVIL--IEHNLDVLS 153
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-229 |
2.07e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 26 NDVSLQIEAG-----ETLALVGESGSGKSvTALSIL--RLLPSppveylSGDIrfhgesllhasdqtlrGVRGNKIAMIF 98
Cdd:cd03237 11 GEFTLEVEGGsisesEVIGILGPNGIGKT-TFIKMLagVLKPD------EGDI----------------EIELDTVSYKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 99 QEpmVSLNPLHTLEKQLYEVLslhRGMRREAA-RGEILNCLDRVGIRQaaKRLTDyphqLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03237 68 QY--IKADYEGTVRDLLSSIT---KDFYTHPYfKTEIAKPLQIEQILD--REVPE----LSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130118 178 LIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAV 229
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-225 |
2.30e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 155 HQLSGGERQRVMIAMAL----LTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMgMLFITHNLSIVRKLAH 225
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELAELADK 149
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
401-514 |
2.94e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 401 REQQVIAVMHEVGLDP-----ETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILT--LLKSLQQ 473
Cdd:PLN03232 712 RAIDVTALQHDLDLLPgrdltEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKG 790
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16130118 474 KHQlayLFISHDLHVVrALCHQVIILRQGEVVEQGPCARVF 514
Cdd:PLN03232 791 KTR---VLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAELS 827
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-231 |
2.94e-06 |
|
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: 47.57 E-value: 2.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
308-518 |
2.96e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 48.56 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 308 TLRAGETLGLVGESGSGKSTTGLALLRLIN-SQGSIIFDG----------QPLQNLNRRQLLpiRHRIQVVFQDP---NS 373
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIELdtvsykpqyiKADYEGTVRDLL--SSITKDFYTHPyfkTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 374 SLNPrlnvLQIieEGLRvhqptlsaaqrEQQViavmhevgldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03237 99 IAKP----LQI--EQIL-----------DREV------------------PELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 454 SSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILrQGEVVEQGpcarVFATPQ 518
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNG----VANPPQ 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-224 |
3.49e-06 |
|
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: 46.98 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 35 GETLALVGESGSGKSVTALSILRLL--PSPPVEYLSGDIRFhgesllhasdqtlrgvrgnkiamifqepmvslnplhtle 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELgpPGGGVIYIDGEDIL--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 113 kqlyevlslhrgmrreaargeilnclDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQ 192
Cdd:smart00382 43 --------------------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180 190
....*....|....*....|....*....|....*..
gi 16130118 193 AQILQLLRELQG-----ELNMGMLFITHNLSIVRKLA 224
Cdd:smart00382 97 ALLLLLEELRLLlllksEKNLTVILTTNDEKDLGPAL 133
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
148-229 |
3.74e-06 |
|
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: 49.78 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 148 KRLTDyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRV 227
Cdd:COG1245 451 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
..
gi 16130118 228 AV 229
Cdd:COG1245 527 MV 528
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
427-508 |
5.34e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL-TLLK-SLQQKHQlayLFISHDLHVVRALcHQVIILRQGEV 504
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKdELRGKTR---VLVTNQLHFLSQV-DRIILVHEGMI 817
|
....
gi 16130118 505 VEQG 508
Cdd:PLN03130 818 KEEG 821
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-221 |
6.02e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.24 E-value: 6.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTR---PELLIADEPTTALDVsvqAQILQLLRELQGELNMG--MLFITHNLSIVR 221
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRLVDKGntVVVIEHNLDVIK 896
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-509 |
7.93e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALltRPELL----IADEPTTALDVSVQAQILQLLRELQGELNMgMLFITHNLSIVrKLAHRV----- 227
Cdd:PRK00635 477 LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNT-VLLVEHDEQMI-SLADRIidigp 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 228 -------AVMQNGRCVEqnyaatlFASPTHPYTQKLLNSEPSGD-PVPLPEPASTLLdveqlqvafpirkgiLKRIVDHN 299
Cdd:PRK00635 553 gagifggEVLFNGSPRE-------FLAKSDSLTAKYLRQELTIPiPEKRTNSLGTLT---------------LSKATKHN 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VvvKNISFTLRAGETLGLVGESGSGKST------------------------TGLALLRLIN--------SQGSI----- 342
Cdd:PRK00635 611 L--KDLTISLPLGRLTVVTGVSGSGKSSlindtlvpaveefieqgfcsnlsiQWGAISRLVHitrdlpgrSQRSIpltyi 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 343 --------IFDGQP---LQNLNRRQL---LPIRHRIQ------VVFQDPNSSLNPRL--------NVLQIIEEGLRVHQP 394
Cdd:PRK00635 689 kafddlreLFAEQPrskRLGLTKSHFsfnTPLGACAEcqglgsITTTDNRTSIPCPSclgkrflpQVLEVRYKGKNIADI 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 395 -TLSAAQREQ---------QVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALIL---KPSLIILDEPTSSL-DKTV 460
Cdd:PRK00635 769 lEMTAYEAEKffldepsihEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhTHDI 848
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16130118 461 QAQILTLLKSLQQKHQLayLFISHDLHVVRALCHqviilrqgeVVEQGP 509
Cdd:PRK00635 849 KALIYVLQSLTHQGHTV--VIIEHNMHVVKVADY---------VLELGP 886
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-202 |
1.01e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLlpspPVEYLSGDIRFhgesllhasdqtlrgVRGNKIAMIFQ 99
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKT-TLLNVLaeRV----TTGVITGGDRL---------------VNGRPLDSSFQ 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 EPM--VSLNPLHTLEKQLYEVLSLHRGMRR--EAARGEILNCLDRV----GIRQAAKRLTDYPHQ-LSGGERQRVMIAMA 170
Cdd:TIGR00956 836 RSIgyVQQQDLHLPTSTVRESLRFSAYLRQpkSVSKSEKMEYVEEVikllEMESYADAVVGVPGEgLNVEQRKRLTIGVE 915
|
170 180 190
....*....|....*....|....*....|...
gi 16130118 171 LLTRPELLI-ADEPTTALDVSVQAQILQLLREL 202
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-249 |
1.25e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVEYLSGDIRfhgESLLHASdqtlrgvrgnKIAMIF 98
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS--HAETSSVVIR---GSVAYVP----------QVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 99 QePMVSLNPL--HTLEKQLY----EVLSLHRGMRREAARGeilncLDRVGIRQAakrltdyphQLSGGERQRVMIAMALL 172
Cdd:PLN03232 692 N-ATVRENILfgSDFESERYwraiDVTALQHDLDLLPGRD-----LTEIGERGV---------NISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 173 TRPELLIADEPTTALDVSVQAQILQ--LLRELQGELNmgmLFITHNLSIVrKLAHRVAVMQNGRCVEQNYAATLFASPT 249
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTR---VLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
302-487 |
1.31e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLGLVGESGSGKSTTGLALLRL-INSQGSIIFDGQPLQNLNRRQLlpiRHRIQVVFQDPNssLNPRLn 380
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKPVTAEQPEDY---RKLFSAVFTDFH--LFDQL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 381 vlqIIEEGlrvHQPTLSAAQREQQVIAVMHEVGLDpetRHRYP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
Cdd:PRK10522 413 ---LGPEG---KPANPALVEKWLERLKMAHKLELE---DGRISnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180
....*....|....*....|....*...
gi 16130118 460 VQAQILTLLKSLQQKHQLAYLFISHDLH 487
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDH 511
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-237 |
1.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGESLLHASDQTLRGvrgnkiamifqepmvs 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKS-TLSNIIGGSLSPT----VGKVDRNGEVSVIAISAGLSG---------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 lnPLHTLEKQLYEVLSLhrGMRREAARG---EILNcLDRVG--IRQAAKRLtdyphqlSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK13546 99 --QLTGIENIEFKMLCM--GFKRKEIKAmtpKIIE-FSELGefIYQPVKKY-------SSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130118 180 ADEPTTALDVSVQAQILQLLRELQgELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVE 237
Cdd:PRK13546 167 IDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-221 |
1.34e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILrllpsppveYLSGDIRFhgESLLHASDQTlrgvrgnkiamifqePMVS 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---------YASGKARL--ISFLPKFSRN---------------KLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTLEKQLYEVLSLHRGMRreaargeilncldrvgirqaakrltdyphQLSGGERQRVMIA--MALLTRPELLIADE 182
Cdd:cd03238 65 IDQLQFLIDVGLGYLTLGQKLS-----------------------------TLSGGELQRVKLAseLFSEPPGTLFILDE 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16130118 183 PTTALDvsvQAQILQLLRELQGELNMG--MLFITHNLSIVR 221
Cdd:cd03238 116 PSTGLH---QQDINQLLEVIKGLIDLGntVILIEHNLDVLS 153
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
298-508 |
1.73e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 298 HNVvvKNISFTLRAGETLGLVGESGSGKSTtgLAL--------LRLINSQGSiiFDGQPLQNLNRRQLLPIRHRIQVVFQ 369
Cdd:cd03270 9 HNL--KNVDVDIPRNKLVVITGVSGSGKSS--LAFdtiyaegqRRYVESLSA--YARQFLGQMDKPDVDSIEGLSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 370 DPNS-SLNPRLNVLQIIE--EGLRVhqptLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARAL--ILKP 444
Cdd:cd03270 83 DQKTtSRNPRSTVGTVTEiyDYLRL----LFARVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 445 SLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVII-----LRQGEVVEQG 508
Cdd:cd03270 159 VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-281 |
2.32e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 42.39 E-value: 2.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 16130118 236 VEQNYAATLFASPTHPYTQKLLNSEPSGDPV--PLPEPASTLLDVEQL 281
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPkrPLYTIPGNVPSLLEL 48
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
157-221 |
2.48e-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: 46.07 E-value: 2.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130118 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVSVQAQILQLLRElQGElnmGMLFITHNLSIVR 221
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVD-KGN---TVVVIEHNLDVIK 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-189 |
2.72e-05 |
|
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: 46.85 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 8 IENLSVGFRHqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFhGESLLHAS-DQTL 86
Cdd:TIGR03719 325 AENLTKAFGD----KLLIDDLSFKLPPGGIVGVIGPNGAGKS-TLFRMITGQEQPD----SGTIEI-GETVKLAYvDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 87 RGVRGNKiaMIFQEpmVSlNPLHTLEKQLYEVLSlhrgmrreaaRGEIlnclDRVGIRQAA--KRLTdyphQLSGGERQR 164
Cdd:TIGR03719 395 DALDPNK--TVWEE--IS-GGLDIIKLGKREIPS----------RAYV----GRFNFKGSDqqKKVG----QLSGGERNR 451
|
170 180
....*....|....*....|....*
gi 16130118 165 VMIAMALLTRPELLIADEPTTALDV 189
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
425-499 |
2.99e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIIL 499
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-521 |
4.08e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 275 LLDVEQLQVAfpirkgilkriVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLIN---SQGSIIFDGQPLQN 351
Cdd:PRK09580 1 MLSIKDLHVS-----------VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyevTGGTVEFKGKDLLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 352 LNRRQllPIRHRIQVVFQDP------------NSSLNP-----------RLNVLQIIEEGLRVHQPTLSAAQREQQViav 408
Cdd:PRK09580 70 LSPED--RAGEGIFMAFQYPveipgvsnqfflQTALNAvrsyrgqepldRFDFQDLMEEKIALLKMPEDLLTRSVNV--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 409 mhevgldpetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHV 488
Cdd:PRK09580 145 ----------------GFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRI 207
|
250 260 270
....*....|....*....|....*....|....
gi 16130118 489 VRALCHQ-VIILRQGEVVEQGPCARVFATPQQEY 521
Cdd:PRK09580 208 LDYIKPDyVHVLYQGRIVKSGDFTLVKQLEEQGY 241
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-501 |
4.41e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 4.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130118 427 SGGQRQRIAIARALIL---KP-SLIILDEPTSSLDKTVQAQILTLLKSLQQkHQLAYLFISHDLHVVRALCHQVIILRQ 501
Cdd:cd03227 79 SGGEKELSALALILALaslKPrPLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
300-484 |
5.63e-05 |
|
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: 45.90 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLInsqGSI--IFDGqplqnlnrRQLLPIRHRIQVVFQDP---NSS 374
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSS----LFRIL---GELwpVYGG--------RLTKPAKGKLFYVPQRPymtLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 375 LNPRL----NVLQIIEEGLRvhqptlsaaqrEQQVIAVMHEVGLDP--------ETRHRYPAEFSGGQRQRIAIARALIL 442
Cdd:TIGR00954 531 LRDQIiypdSSEDMKRRGLS-----------DKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16130118 443 KPSLIILDEPTSSLDKTVQAQILTLLKslqqKHQLAYLFISH 484
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-327 |
6.12e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLT---RPELLIADEPTTALDVSVQAQILQLLREL--QGElnmGMLFITHNLSIVRKLAHRVAVMQ 231
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLthQGH---TVVIIEHNMHVVKVADYVLELGP 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 232 NGrcveQNYAATLFAS-----------PTHPYTQKLLNSEPSGDPVPLPEPASTLLdveqlqvafpiRKGILKRIVDHNv 300
Cdd:PRK00635 887 EG----GNLGGYLLAScspeelihlhtPTAKALRPYLSSPQELPYLPDPSPKPPVP-----------ADITIKNAYQHN- 950
|
170 180
....*....|....*....|....*..
gi 16130118 301 vVKNISFTLRAGETLGLVGESGSGKST 327
Cdd:PRK00635 951 -LKHIDLSLPRNALTAVTGPSASGKHS 976
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-237 |
8.63e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.71 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpVEYLSGDIRFHGeSLLHASDQTLRGVRGNKIAMIFQEPmvs 104
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKS----SLLSALLAE-MDKVEGHVHMKG-SVAYVPQQAWIQNDSLRENILFGKA--- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 105 LNPLHTleKQLYEVLSLHRGMrreaargEILNCLDRVGIRQAAKrltdyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:TIGR00957 725 LNEKYY--QQVLEACALLPDL-------EILPSGDRTEIGEKGV-------NLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16130118 185 TALDVSVQAQILQLLRELQGEL-NMGMLFITHNLSIVRKLaHRVAVMQNGRCVE 237
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
302-523 |
1.10e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 302 VKNISFTLRAGETLgLVGESGSGKSTTGLALLRLINSQGSIIFD---------------------GQPLQNLNRRQLLP- 359
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKFDeedfylgddpdlpeieieltfGSLLSRLLRLLLKEe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 360 IRHRIQVVFQDPNSSLNPRLNVLQ-----IIEEGLRVHQPTLSAAQREQQVIAVMHEVGLdpETRHRYPAEFSG-GQRQR 433
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNellseYLKELLDGLDLELELSLDELEDLLKSLSLRI--EDGKELPLDRLGsGFQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 434 IAIARALIL-------KPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHqlAYLFIS-HDLHVVRALC-HQVIILRQGEv 504
Cdd:COG3593 171 ILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKP--NQVIITtHSPHLLSEVPlENIRRLRRDS- 247
|
250
....*....|....*....
gi 16130118 505 vEQGPCARVFATPQQEYTR 523
Cdd:COG3593 248 -GGTTSTKLIDLDDEDLRK 265
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
300-517 |
1.11e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 300 VVVKNISFTLRAGETLGLVGESGSGKSTtglaLLRLINSQgsiiFDGQPLQNLNRRQllpirhrIQVVFQDP---NSSLn 376
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKST----LLQSLLSQ----FEISEGRVWAERS-------IAYVPQQAwimNATV- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 377 pRLNVLQIIEEglrvHQPTLSAAQREQQVIAVMHEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PTZ00243 738 -RGNILFFDEE----DAARLADAVRVSQLEADLAQLGGGLETEiGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 456 LDKTVQAQIL--TLLKSLQQKHQ-LAylfiSHDLHVVrALCHQVIILRQGEVVEQGPCARVFATP 517
Cdd:PTZ00243 813 LDAHVGERVVeeCFLGALAGKTRvLA----THQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-235 |
1.28e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSIL-RLLPSppveylSGDIRFHGEslLHASDQTLRGVRGNkiamifq 99
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPS------EGKIKHSGR--ISFSPQTSWIMPGT------- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 100 epmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVgirqaakrLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:TIGR01271 503 ---IKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTV--------LGEGGITLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130118 180 ADEPTTALDVSVQAQILQ-LLRELQgeLNMGMLFITHNLSIVRKlAHRVAVMQNGRC 235
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFEsCLCKLM--SNKTRILVTSKLEHLKK-ADKILLLHEGVC 625
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
157-221 |
1.86e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 1.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 157 LSGGERQRVMIAMALLTRP---ELLIADEPTTAL---DVSvqaqilQLLRELQGELNMG--MLFITHNLSIVR 221
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIR------KLLEVLHRLVDKGntVVVIEHNLDVIK 897
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
427-508 |
2.84e-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: 43.85 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 427 SGGQRQRIAIARALILK---PSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAyLFISHDLHVVRALCHqVIIL---- 499
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVIEHNLDVIKTADY-IIDLgpeg 908
|
90
....*....|.
gi 16130118 500 --RQGEVVEQG 508
Cdd:TIGR00630 909 gdGGGTVVASG 919
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
425-499 |
6.33e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 6.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHqlAYLFISHDLHVVRALCHQVIIL 499
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
156-189 |
6.70e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 6.70e-04
10 20 30
....*....|....*....|....*....|....
gi 16130118 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
157-233 |
7.61e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQ--LLRELQGELNMGMLFITHNLSIVRK--LAHRVAVMQN 232
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTRVLVTNQLHFLSQVDRiiLVHEGMIKEE 820
|
.
gi 16130118 233 G 233
Cdd:PLN03130 821 G 821
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
427-465 |
8.87e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 8.87e-04
10 20 30
....*....|....*....|....*....|....*....
gi 16130118 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
305-509 |
9.61e-04 |
|
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: 42.24 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 305 ISFTLRAGETLGLVGESGSGKSTTGLALLRLINS-QGSIIFDGQPlqnlnrrQLLPIRHRIQvvfqdpNSSLnpRLNVLQ 383
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKvEGHVHMKGSV-------AYVPQQAWIQ------NDSL--RENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 384 iieeGLRVHQPtlsaaqREQQVI---AVMHEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:TIGR00957 722 ----GKALNEK------YYQQVLeacALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 457 DKTVQAQILT-------LLKSLQQ---KHQLAYLfishdlhvvrALCHQVIILRQGEVVEQGP 509
Cdd:TIGR00957 792 DAHVGKHIFEhvigpegVLKNKTRilvTHGISYL----------PQVDVIIVMSGGKISEMGS 844
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-221 |
1.24e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130118 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVSVQAQILQLLRELqgelnmG--MLFITHNLSIVR 221
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIRKLLEVLHRLVDK------GntVVVIEHNLDVIK 893
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
425-499 |
1.88e-03 |
|
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: 40.92 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQlAYLFISHDLHVVRALCHQVIIL 499
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-188 |
5.19e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.68 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPveylSGDIRFHGEsllHASdqtlRGVRGNKIAMIFQEPMV 103
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKT-TLLRVLAGLLHVE----SGQIQIDGK---TAT----RGDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 104 SLNpLHTLEkQLYEVLSLHrGMRREAARGeilNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK13543 94 KAD-LSTLE-NLHFLCGLH-GRRAKQMPG---SALAIVGLAGYEDTLV---RQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 16130118 184 TTALD 188
Cdd:PRK13543 165 YANLD 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
164-215 |
5.20e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 5.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 16130118 164 RVMIAMALLTRPELLIADEPTTALDVSVqaqilqlLRELQGELNM---GMLFITH 215
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINT-------IRWLEDVLNErnsTMIIISH 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
157-234 |
5.82e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQ--LLRELQGELNmgmLFITHNLSIVrKLAHRVAVMQNGR 234
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTR---VLATHQVHVV-PRADYVVALGDGR 858
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-262 |
6.14e-03 |
|
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: 36.19 E-value: 6.14e-03
10 20
....*....|....*....|....*..
gi 16130118 236 VEQNYAATLFASPTHPYTQKLLNSEPS 262
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPT 29
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
317-482 |
7.10e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.48 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 317 LVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRiqvvfqdpnsslnprlnvLQIIEEGLRVHQPTL 396
Cdd:pfam13191 29 LTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTR------------------EGLLRQLLDELESSL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 397 SAAQREQQVIAVMHEVGLDPETRHRYPAEFsggqrQRIAIARALILKPSLIILDEptssLDKtVQAQILTLLKSLQQKHQ 476
Cdd:pfam13191 91 LEAWRAALLEALAPVPELPGDLAERLLDLL-----LRLLDLLARGERPLVLVLDD----LQW-ADEASLQLLAALLRLLE 160
|
....*.
gi 16130118 477 LAYLFI 482
Cdd:pfam13191 161 SLPLLV 166
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
411-493 |
8.37e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130118 411 EVGLdPETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQ--AQILTLLKSlqqkhqlAYLFISHDL 486
Cdd:PRK15064 141 GVGI-PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDiNTIRwlEDVLNERNS-------TMIIISHDR 212
|
....*..
gi 16130118 487 HVVRALC 493
Cdd:PRK15064 213 HFLNSVC 219
|
|
| |
