|
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: 1020.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQLSGG 160
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNR 240
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 241 AAQLLTAPTHPYTKKLLNSEPSGDPVPLPVGQAPLLEVEKLRVAFPIRKGILKRVVDHNVVVNDVSFSLRPGETLGLVGE 320
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 321 SGSGKSTTGLALLRLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQ 400
Cdd:PRK15134 321 SGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 401 REAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYI 480
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2551249897 481 FISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLALS 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: 943.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVvYPSGDIRFHGESLLH 80
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAA-HPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQLSGG 160
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNR 240
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 241 AAQLLTAPTHPYTKKLLNSEPSGDPVPLPVGQAPLLEVEKLRVAFPIRKGILKRVVDHNVVVNDVSFSLRPGETLGLVGE 320
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 321 SGSGKSTTGLALLRLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQ 400
Cdd:COG4172 321 SGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 401 REAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYI 480
Cdd:COG4172 401 RRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2551249897 481 FISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 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: 604.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLHAN 82
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI--SGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQtlrdVRGNKIAMIFQEPMVSLNPLhNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSGGER 162
Cdd:COG1123 78 EA----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAA 242
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 243 QLLTAPTHPYTKKLLNSePSGDPVPLPVGQAPLLEVEKLRVAFPIRKG----ILKRVvdhnvvvndvSFSLRPGETLGLV 318
Cdd:COG1123 229 EILAAPQALAAVPRLGA-ARGRAAPAAAAAEPLLEVRNLSKRYPVRGKggvrAVDDV----------SLTLRRGETLGLV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 319 GESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpTLS 397
Cdd:COG1123 298 GESGSGKSTLARLLLGLLRpTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHG-LLS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 398 AEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRL 477
Cdd:COG1123 377 RAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGL 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 478 AYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:COG1123 457 TYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLA 506
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-527 |
2.77e-163 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 477.43 E-value: 2.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGD--IRFHGESLL 79
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmlLRRRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANEQT---LRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQ 156
Cdd:PRK10261 89 ELSEQSaaqMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 237 EQNRAAQLLTAPTHPYTKKLLNSEP-----SGDPVP--LP-------------------VGQAPLLEVEKLRVAFPIRKG 290
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPqlgamKGLDYPrrFPlislehpakqeppieqdtvVDGEPILQVRNLVTRFPLRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 291 ILKRVVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQLLPVRHRIQVVFQ 369
Cdd:PRK10261 329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 370 DPNSSLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVHG-LLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 450 DEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-265 |
2.11e-133 |
|
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: 389.80 E-value: 2.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLHANEQ 84
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQLSGGERQR 164
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQL 244
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 2551249897 245 LTAPTHPYTKKLLNSEPSGDP 265
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
271-527 |
8.86e-115 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 342.48 E-value: 8.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 271 GQAPLLEVEKLRVAFPIRKGILKRVVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLAL 349
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEpTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 350 HTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGG 429
Cdd:COG4608 83 TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHG-LASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 430 QRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250
....*....|....*...
gi 2551249897 510 CEHVFNAPQQAYTRQLLA 527
Cdd:COG4608 242 RDELYARPLHPYTQALLS 259
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-527 |
6.24e-107 |
|
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: 322.39 E-value: 6.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKGILK--RVVdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALLRLI----TSQGSIVFDGLA 348
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKavDGV---------SFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 349 LHTLNRRQLLPVRHR-IQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPtLSAEQREAQVKAVMAEVGLDSETRH--RYPAE 425
Cdd:COG0444 72 LLKLSEKELRKIRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGG-LSKAEARERAIELLERVGLPDPERRldRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250 260
....*....|....*....|..
gi 2551249897 506 EQGQCEHVFNAPQQAYTRQLLA 527
Cdd:COG0444 231 EEGPVEELFENPRHPYTRALLS 252
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-508 |
9.71e-103 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 307.90 E-value: 9.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKGILKrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLN 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVK-------ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 354 RRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQR 433
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 434 IAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 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 |
3.35e-100 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 301.35 E-value: 3.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLLHANEQ 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK--PT---SGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRdVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILtCLDRVGIRQAAKRLADYPHQLSGGERQR 164
Cdd:cd03257 76 LRK-IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQN 239
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-264 |
9.03e-96 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 293.94 E-value: 9.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLLH 80
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI--GGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQLSGG 160
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNR 240
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|....
gi 2551249897 241 AAQLLTAPTHPYTKKLLNSEPSGD 264
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLD 269
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-265 |
1.09e-95 |
|
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: 299.90 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQET-VRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyP-SGDIRFHGESL 78
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR------PtSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 79 LHANEQTLRDVRGnKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLadYPHQLS 158
Cdd:COG1123 330 TKLSRRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR--YPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
250 260
....*....|....*....|....*..
gi 2551249897 239 NRAAQLLTAPTHPYTKKLLNSEPSGDP 265
Cdd:COG1123 487 GPTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-529 |
6.50e-92 |
|
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: 280.92 E-value: 6.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKG---ILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALH 350
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrvpVLKDV----------SLEVAPGESFGLVGESGSGKSTLLRALAGLERpWSGEVTFDGRPVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 351 TLNRRQLlpvRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTlsaeQREAQVKAVMAEVGLDSETRHRYPAEFSGGQ 430
Cdd:COG1124 71 RRRRKAF---RRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP----DREERIAELLEQVGLPPSFLDRYPHQLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 431 RQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQC 510
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
250
....*....|....*....
gi 2551249897 511 EHVFNAPQQAYTRQLLALS 529
Cdd:COG1124 224 ADLLAGPKHPYTRELLAAS 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-265 |
1.93e-87 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 272.38 E-value: 1.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGF--------RQQETVRTVvNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDI 71
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgRTVGVVKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePT------SGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 72 RFHGESLLHANEQTLRDVRgNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIR-QAAKRl 150
Cdd:COG4608 76 LFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADR- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 151 adYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVM 230
Cdd:COG4608 154 --YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
|
250 260 270
....*....|....*....|....*....|....*
gi 2551249897 231 QNGQCVEQNRAAQLLTAPTHPYTKKLLNSEPSGDP 265
Cdd:COG4608 232 YLGKIVEIAPRDELYARPLHPYTQALLSAVPVPDP 266
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-264 |
1.85e-85 |
|
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: 273.87 E-value: 1.85e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETV--RTV-----VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGE 76
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLfrRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS------EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 77 SLLHANEQTLRDVRgNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHR-GMRREAARAEILTCLDRVGI-RQAAKRladYP 154
Cdd:COG4172 348 DLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHR---YP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250 260 270
....*....|....*....|....*....|
gi 2551249897 235 CVEQNRAAQLLTAPTHPYTKKLLNSEPSGD 264
Cdd:COG4172 504 VVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-259 |
4.48e-83 |
|
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: 258.19 E-value: 4.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyP-SGDIRFHGESLLHANe 83
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER------PwSGEVTFDGRPVTRRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 qtLRDVRGnKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILtclDRVGIRQAakrLAD-YPHQLSGGER 162
Cdd:COG1124 74 --RKAFRR-RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREERIAELL---EQVGLPPS---FLDrYPHQLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAA 242
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
250
....*....|....*..
gi 2551249897 243 QLLTAPTHPYTKKLLNS 259
Cdd:COG1124 225 DLLAGPKHPYTRELLAA 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
272-527 |
2.99e-81 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 256.43 E-value: 2.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 272 QAPLLEVEKLRVAFPIRKGILKrVVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDG 346
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKST----LARLLTmietpTGGELYYQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 LALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSETRHRYPAEF 426
Cdd:PRK11308 77 QDLLKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINT-SLSAAERREKALAMMAKVGLRPEHYDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVE 506
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250 260
....*....|....*....|.
gi 2551249897 507 QGQCEHVFNAPQQAYTRQLLA 527
Cdd:PRK11308 236 KGTKEQIFNNPRHPYTQALLS 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
274-527 |
2.61e-80 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 254.25 E-value: 2.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAFPIR--KGILKRVVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALH 350
Cdd:PRK15079 7 VLLEVADLKVHFDIKdgKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 351 TLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQ 430
Cdd:PRK15079 87 GMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 431 RQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQC 510
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTY 246
|
250
....*....|....*..
gi 2551249897 511 EHVFNAPQQAYTRQLLA 527
Cdd:PRK15079 247 DEVYHNPLHPYTKALMS 263
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-261 |
1.88e-79 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 251.97 E-value: 1.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYpSGDIRFHGESLLHANEQ 84
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVM-AEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQLSGGERQR 164
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQL 244
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*..
gi 2551249897 245 LTAPTHPYTKKLLNSEP 261
Cdd:PRK11022 242 FRAPRHPYTQALLRALP 258
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
274-526 |
1.97e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 249.37 E-value: 1.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAFPIRKGILKRVVDHNVVVNdvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLA 348
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQQFEAVKPV--SFTLEAGQTLAIIGENGSGKST----LAKMLAgiiepTSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 349 LHTLNRRQllpvR-HRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFS 427
Cdd:COG4167 77 LEYGDYKY----RcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNT-DLTAEEREERIFATLRLVGLLPEHANFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 428 GGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250
....*....|....*....
gi 2551249897 508 GQCEHVFNAPQQAYTRQLL 526
Cdd:COG4167 232 GKTAEVFANPQHEVTKRLI 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-265 |
6.20e-69 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 224.46 E-value: 6.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 15 FRQQETVRTVvNTLSLRVDAGQTLALVGESGSGKSVTAlsilRLL-----PSppvvypSGDIRFHGESLLHANEQTLRDV 89
Cdd:PRK11308 22 FKPERLVKAL-DGVSFTLERGKTLAVVGESGCGKSTLA----RLLtmietPT------GGELYYQGQDLLKADPEAQKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 90 RgNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIR-QAAKRladYPHQLSGGERQRVMIA 168
Cdd:PRK11308 91 R-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDR---YPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAP 248
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
250
....*....|....*..
gi 2551249897 249 THPYTKKLLNSEPSGDP 265
Cdd:PRK11308 247 RHPYTQALLSATPRLNP 263
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-277 |
1.66e-66 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 218.24 E-value: 1.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFR-QQETVRtVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVypSGD-IRFHGESLLHA 81
Cdd:COG4170 2 PLLDIRNLTIEIDtPQGRVK-AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHV--TADrFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVL--SLHRGM---RREAARAEILTCLDRVGIRQAAKRLADYPHQ 156
Cdd:COG4170 79 SPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpsWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2551249897 237 EQNRAAQLLTAPTHPYTKKLLNSEPS-GDPVP-------LPvGQAPLLE 277
Cdd:COG4170 239 ESGPTEQILKSPHHPYTKALLRSMPDfRQPLPhksrlntLP-GSIPPLQ 286
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
274-526 |
1.70e-64 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 213.05 E-value: 1.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAFPIRKGILkrvvdhnVVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLITSQG----SIVFDGLAL 349
Cdd:PRK09473 11 ALLDVKDLRVTFSTPDGDV-------TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGriggSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 350 HTLNRRQLLPVR-HRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQREAQVKavMAEVGLDSETRHR---YPAE 425
Cdd:PRK09473 84 LNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVR--MLDAVKMPEARKRmkmYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260
....*....|....*....|.
gi 2551249897 506 EQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLL 262
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-265 |
1.52e-62 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 208.02 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGFR---------QQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRF 73
Cdd:PRK15079 6 KVLLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-----DGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 74 HGESLLHANEQTLRDVRgNKIAMIFQEPMVSLNPLHNLEKQLYEVL-SLHRGMRREAARAEILTCLDRVGIR-QAAKRla 151
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLpNLINR-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 152 dYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQ 231
Cdd:PRK15079 158 -YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMY 236
|
250 260 270
....*....|....*....|....*....|....
gi 2551249897 232 NGQCVEQNRAAQLLTAPTHPYTKKLLNSEPSGDP 265
Cdd:PRK15079 237 LGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDP 270
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-259 |
2.25e-61 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 202.37 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFR-----QQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTAlsilRLLPSppVVYP-SGDIRFHGES 77
Cdd:COG4167 3 ALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLA----KMLAG--IIEPtSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 78 LLHANEQTlrdvRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIrqaakrLAD----Y 153
Cdd:COG4167 77 LEYGDYKY----RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGL------LPEhanfY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
250 260
....*....|....*....|....*.
gi 2551249897 234 QCVEQNRAAQLLTAPTHPYTKKLLNS 259
Cdd:COG4167 227 EVVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
306-527 |
7.34e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 195.68 E-value: 7.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKST----LIRCINllerpTSGSVLVDGVDLTALSERELRAARRKIGMIFQHFN--LLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG1135 99 VAENVALPLEIAG--VPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:COG1135 176 TRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLP 242
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
306-527 |
1.64e-57 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 192.33 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQI 384
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRvHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:TIGR02769 111 IGEPLR-HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVI 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 465 LTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAyTRQLLA 527
Cdd:TIGR02769 190 LELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPA-GRNLQS 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-257 |
3.53e-57 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 191.07 E-value: 3.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVgfrqqETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSppvvypsGDIRFHGESLLHANEQT 85
Cdd:PRK10418 5 IELRNIAL-----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-------GVRQTAGRVLLDGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLslhRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQLSGGERQRV 165
Cdd:PRK10418 73 PCALRGRKIATIMQNPRSAFNPLHTMHTHARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLL 245
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|..
gi 2551249897 246 TAPTHPYTKKLL 257
Cdd:PRK10418 230 NAPKHAVTRSLV 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
272-508 |
2.01e-56 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 188.65 E-value: 2.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 272 QAPLLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIV 343
Cdd:COG1127 2 SEPMIEVRNLTKSFgdrVVLDGV--------------SLDVPRGEILAIIGGSGSGKSV----LLKLIIgllrpDSGEIL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 344 FDGLALHTLNRRQLLPVRHRIQVVFQDP---NSslnprLSVLQIIEEGLRVHqPTLSAEQREAQVKAVMAEVGLdSETRH 420
Cdd:COG1127 64 VDGQDITGLSEKELYELRRRIGMLFQGGalfDS-----LTVFENVAFPLREH-TDLSEAEIRELVLEKLELVGL-PGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLR 500
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
....*...
gi 2551249897 501 QGEVVEQG 508
Cdd:COG1127 217 DGKIIAEG 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
306-506 |
3.53e-56 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 189.13 E-value: 3.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRLSVLQI 384
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRvHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PRK10419 112 IREPLR-HLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2551249897 465 LTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVE 506
Cdd:PRK10419 191 IRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
306-518 |
7.56e-56 |
|
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: 187.02 E-value: 7.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKST----LIRCINglerpTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQHFN--LLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03258 99 VFENVALPLEIAG--VPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:cd03258 176 TQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-240 |
1.47e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 183.32 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLL--PSppvvypSGDIRFHGESLLH 80
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLdrPT------SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQEP--MVSLNPLHNLEkqlyevLSLH-RGMRREAARAEILTCLDRVGIrqaAKRLADYPHQL 157
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFFnlLPELTALENVA------LPLLlAGVSRKERRERARELLERVGL---GDRLDHRPSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIvKKLADTVAVMQNGQCVE 237
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVS 224
|
...
gi 2551249897 238 QNR 240
Cdd:COG1136 225 DER 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
275-527 |
4.48e-53 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 180.76 E-value: 4.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKGILKRVVDHNVVVNdvSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLN 353
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVEAVKPL--SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 354 ---RRQllpvrhRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQ 430
Cdd:PRK15112 82 ysyRSQ------RIRMIFQDPSTSLNPRQRISQILDFPLRLNT-DLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 431 RQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQC 510
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250
....*....|....*..
gi 2551249897 511 EHVFNAPQQAYTRQLLA 527
Cdd:PRK15112 235 ADVLASPLHELTKRLIA 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-507 |
8.30e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 176.00 E-value: 8.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFPIRKG---ILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVF 344
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtALRGV----------SLSIEAGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 345 DGLALHTLNRRQLLPVR-HRIQVVFQDPNssLNPRLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYP 423
Cdd:COG1136 68 DGQDISSLSERELARLRrRHIGFVFQFFN--LLPELTALENVALPLLLAG--VSRKERRERARELLERVGL-GDRLDHRP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGE 503
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGR 221
|
....
gi 2551249897 504 VVEQ 507
Cdd:COG1136 222 IVSD 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-277 |
1.03e-51 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 179.23 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVypSGD-IRFHGESLLHAN 82
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRV--TADrMRFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVL--SLHRG---MRREAARAEILTCLDRVGIRQAAKRLADYPHQL 157
Cdd:PRK15093 80 PRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgWTYKGrwwQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2551249897 238 QNRAAQLLTAPTHPYTKKLLNSEPS-GDPVP-------LPvGQAPLLE 277
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPDfGSAMPhksrlntLP-GAIPLLE 286
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
276-518 |
1.03e-51 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 176.15 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 276 LEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLITSQ-----GSIVFDGL 347
Cdd:cd03261 1 IELRGLTKSFggrTVLKGV--------------DLDVRRGEILAIIGPSGSGKST----LLRLIVGLlrpdsGEVLIDGE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 348 ALHTLNRRQLLPVRHRIQVVFQDpnSSLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFS 427
Cdd:cd03261 63 DISGLSEAELYRLRRRMGMLFQS--GALFDSLTVFENVAFPLREHT-RLSEEEIREIVLEKLEAVGL-RGAEDLYPAELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 428 GGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQ 507
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
250
....*....|.
gi 2551249897 508 GQCEHVFNAPQ 518
Cdd:cd03261 219 GTPEELRASDD 229
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-526 |
7.05e-51 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 176.86 E-value: 7.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKGILKrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLITSQG-----SIVFDGLAL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaeKLEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 350 HTLN---RRQLlpVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQREAQVKaVMAEVGL-DSETR-HRYPA 424
Cdd:PRK11022 76 QRISekeRRNL--VGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAID-LLNQVGIpDPASRlDVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
250 260
....*....|....*....|..
gi 2551249897 505 VEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK11022 233 VETGKAHDIFRAPRHPYTQALL 254
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-254 |
1.08e-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: 173.63 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyP-SGDIRFHGESLL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR------PdSGEILVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANEQTLRDVRgNKIAMIFQEPMV--SLNPLHNLEKQLYEvlslHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQL 157
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQGGALfdSLTVFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---MPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALD-VSVqAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*...
gi 2551249897 237 EQNRAAQLLTApTHPYTK 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 ... |
6-234 |
1.14e-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: 172.67 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQT 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPT----SGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGNKIAMIFQEpmvslnplHNLEKQL--YEVLSL---HRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGG 160
Cdd:cd03255 76 LAAFRRRHIGFVFQS--------FNLLPDLtaLENVELpllLAGVPKKERRERAEELLERVGLGDRLNH---YPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVkKLADTVAVMQNGQ 234
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
306-518 |
1.64e-50 |
|
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: 172.90 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSslnprls 380
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKST----LLRLLNgllkpTSGEVLVDGKDITKKNLREL---RRKVGLVFQNPDD------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 vlQIIEE--------GLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:COG1122 87 --QLFAPtveedvafGPENLG--LPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-265 |
2.49e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.65 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHAN 82
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCInllerPT------SGSVLVDGVDLTALS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDVRGnKIAMIFQepmvslnplH-NL--EKQLYE-V-LSL-HRGMRREAARAEILTCLDRVGIRQAAKRladYPHQ 156
Cdd:COG1135 74 ERELRAARR-KIGMIFQ---------HfNLlsSRTVAEnVaLPLeIAGVPKAEIRKRVAELLELVGLSDKADA---YPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260
....*....|....*....|....*....
gi 2551249897 237 EQNRAAQLLTAPTHPYTKKLLNSEPSGDP 265
Cdd:COG1135 221 EQGPVLDVFANPQSELTRRFLPTVLNDEL 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-505 |
1.80e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 177.52 E-value: 1.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRqqeTVRtVVNTLSLRVDAGQTLALVGESGSGKSvTALSILrllpSPpvVYP--SGDIRFHGESLL 79
Cdd:COG1129 1 AEPLLEMRGISKSFG---GVK-ALDGVSLELRPGEVHALLGENGAGKS-TLMKIL----SG--VYQpdSGEILLDGEPVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANeqtLRDVRGNKIAMIFQEPMV--SLNPLHNL----EKQLYEVLSlHRGMRREAARAeiltcLDRVGIRQAAKRLADy 153
Cdd:COG1129 70 FRS---PRDAQAAGIAIIHQELNLvpNLSVAENIflgrEPRRGGLID-WRAMRRRAREL-----LARLGLDIDPDTPVG- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:COG1129 140 --DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 234 QCVEqnraaqllTAPTHPYTK----------KLLNSEPSGDPVPlpvgQAPLLEVEKLRVAfPIRKGIlkrvvdhnvvvn 303
Cdd:COG1129 217 RLVG--------TGPVAELTEdelvrlmvgrELEDLFPKRAAAP----GEVVLEVEGLSVG-GVVRDV------------ 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 304 dvSFSLRPGETLGLVGESGSGKSTTGLAL--LRLITSqGSIVFDGLALHTLNRRQllPVRHRI---------QVVFQDPN 372
Cdd:COG1129 272 --SFSVRAGEILGIAGLVGAGRTELARALfgADPADS-GEIRLDGKPVRIRSPRD--AIRAGIayvpedrkgEGLVLDLS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 373 SSLNPRLSVLQIIEEGLRVHQptlSAEQREAQvkAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:COG1129 347 IRENITLASLDRLSRGGLLDR---RRERALAE--EYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKhRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-265 |
1.59e-48 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 177.35 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGF--------RQQETVRTVVNtLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFH 74
Cdd:PRK10261 311 EPILQVRNLVTRFplrsgllnRVTREVHAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-----GGEIIFN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 75 GESLLHANEQTLRDVRGNkIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIR-QAAKRladY 153
Cdd:PRK10261 385 GQRIDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWR---Y 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
250 260 270
....*....|....*....|....*....|..
gi 2551249897 234 QCVEQNRAAQLLTAPTHPYTKKLLNSEPSGDP 265
Cdd:PRK10261 541 QIVEIGPRRAVFENPQHPYTRKLMAAVPVADP 572
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-527 |
7.33e-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: 165.94 E-value: 7.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDG 346
Cdd:COG1126 1 MIEIENLHKSFgdlEVLKGI--------------SLDVEKGEVVVIIGPSGSGKST----LLRCINlleepDSGTITVDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 LALhTLNRRQLLPVRHRIQVVFQDPNssLNPRLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEF 426
Cdd:COG1126 63 EDL-TDSKKDINKLRRKVGMVFQQFN--LFPHLTVLENVTLAPIKVK-KMSKAEAEERAMELLERVGL-ADKADAYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD-RTVqAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDpELV-GEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
250 260
....*....|....*....|..
gi 2551249897 506 EQGQCEHVFNAPQQAYTRQLLA 527
Cdd:COG1126 216 EEGPPEEFFENPQHERTRAFLS 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
306-504 |
8.96e-48 |
|
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: 164.97 E-value: 8.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHR-IQVVFQDPNssLNPRL 379
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKST----LLNILGgldrpTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSFN--LLPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:cd03255 98 TALENVELPLLLAG--VPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRaLCHQVIVLRQGEV 504
Cdd:cd03255 175 TGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-516 |
3.19e-46 |
|
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: 162.14 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPiRKGILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLAL 349
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDV----------SLSLPPGEVTALLGPNGSGKST----LLRALAgllkpSSGEVLLDGRDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 350 HTLNRRQLlpvRHRIQVVFQDPNSSLNprLSVLQIIEEGLRVHQPTLSAEQRE--AQVKAVMAEVGLdSETRHRYPAEFS 427
Cdd:COG1120 66 ASLSRREL---ARRIAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSAEdrEAVEEALERTGL-EHLADRPVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 428 GGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQ 507
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
....*....
gi 2551249897 508 GQCEHVFNA 516
Cdd:COG1120 220 GPPEEVLTP 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
306-508 |
6.59e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 159.99 E-value: 6.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNrrqllPVRHRIQVVFQDPnsSLNPRLS 380
Cdd:cd03259 20 SLTVEPGEFLALLGPSGCGKTT----LLRLIAglerpDSGEILIDGRDVTGVP-----PERRNIGMVFQDY--ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03259 89 VAENIAFGLKLR--GVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03259 166 REELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-513 |
7.67e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.99 E-value: 7.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAFPIRKGILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLA 348
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDV----------SLEIERGEFVALIGPSGAGKST----LLRCLNglvepTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 349 LHTLNRRQLLPVRHRIQVVFQDPNssLNPRLSVLQIIEEGLRVHQPTL-------SAEQREaQVKAVMAEVGLdSETRHR 421
Cdd:COG3638 67 VTALRGRALRRLRRRIGMIFQQFN--LVPRLSVLTNVLAGRLGRTSTWrsllglfPPEDRE-RALEALERVGL-ADKAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQ 501
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 2551249897 502 GEVVEQGQCEHV 513
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
272-518 |
3.63e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.19 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 272 QAPLLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIV 343
Cdd:COG3842 2 AMPALELENVSKRYgdvTALDDV--------------SLSIEPGEFVALLGPSGCGKTT----LLRMIagfetPDSGRIL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 344 FDGlalHTLNRrqlLPVRHR-IQVVFQDPnsSLNPRLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRY 422
Cdd:COG3842 64 LDG---RDVTG---LPPEKRnVGMVFQDY--ALFPHLTVAENVAFGLRMRG--VPKAEIRARVAELLELVGLE-GLADRY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQG 502
Cdd:COG3842 133 PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
250
....*....|....*.
gi 2551249897 503 EVVEQGQCEHVFNAPQ 518
Cdd:COG3842 213 RIEQVGTPEEIYERPA 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
306-503 |
4.40e-45 |
|
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: 157.63 E-value: 4.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSSL-NPRl 379
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKST----LLRLLNgllgpTSGEVLVDGKDLTKLSLKEL---RRKVGLVFQNPDDQFfGPT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 svlqIIEE---GLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:cd03225 93 ----VEEEvafGLENLG--LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-248 |
4.50e-45 |
|
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: 158.51 E-value: 4.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLR 87
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPT----SGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQE--PMVSLNPLHNLEKQLyEVLslhrGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQRV 165
Cdd:cd03258 79 KAR-RRIGMIFQHfnLLSSRTVFENVALPL-EIA----GVPKAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLL 245
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 2551249897 246 TAP 248
Cdd:cd03258 230 ANP 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-258 |
5.22e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 158.23 E-value: 5.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlHANEQ 84
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLEEPD----SGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRGnKIAMIFQepmvSLN--P----LHNLEkqlyEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLS 158
Cdd:COG1126 71 DINKLRR-KVGMVFQ----QFNlfPhltvLENVT----LAPIKVKKMSKAEAEERAMELLERVGLADKADA---YPAQLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:COG1126 139 GGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEE 217
|
250 260
....*....|....*....|
gi 2551249897 239 NRAAQLLTAPTHPYTKKLLN 258
Cdd:COG1126 218 GPPEEFFENPQHERTRAFLS 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
306-509 |
8.65e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 157.14 E-value: 8.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKST----LLKLLYgeerpTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQDFR--LLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG2884 96 VYENVALPLRVT--GKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 461 QAQILTLLKSLqekHRL--AYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:COG2884 173 SWEIMELLEEI---NRRgtTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-245 |
6.02e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 6.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLLHANE 83
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKT-TTIRMLlgLLRPT------SGEVRVLGEDVARDPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRdvrgnKIAMIFQEPmvslnplhNLEKQL--YEVLSLH---RGMRREAARAEILTCLDRVGIRQAAKRLADyphQLS 158
Cdd:COG1131 70 EVRR-----RIGYVPQEP--------ALYPDLtvRENLRFFarlYGLPRKEARERIDELLELFGLTDAADRKVG---TLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:COG1131 134 GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
....*..
gi 2551249897 239 NRAAQLL 245
Cdd:COG1131 213 GTPDELK 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
273-529 |
6.39e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 156.24 E-value: 6.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFPIRKGIlkrvvdhnvvvNDVSFSLRPGETLGLVGESGSGKSTTgLALL--RLITSQGSIVFDG---- 346
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGC-----------RDVSFDLYPGEVLGIVGESGSGKTTL-LNALsaRLAPDAGEVHYRMrdgq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 -LALHTLN---RRQLLpvRHRIQVVFQDPNSSLNPRLSVlqiieeGLRVHQPTLSAEQR-----EAQVKAVMAEVGLDSE 417
Cdd:PRK11701 72 lRDLYALSeaeRRRLL--RTEWGFVHQHPRDGLRMQVSA------GGNIGERLMAVGARhygdiRATAGDWLERVEIDAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 418 TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVI 497
Cdd:PRK11701 144 RIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLL 223
|
250 260 270
....*....|....*....|....*....|..
gi 2551249897 498 VLRQGEVVEQGQCEHVFNAPQQAYTrQLLALS 529
Cdd:PRK11701 224 VMKQGRVVESGLTDQVLDDPQHPYT-QLLVSS 254
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
306-526 |
9.66e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.04 E-value: 9.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPN--SSLNpr 378
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKST----LIRCINllerpTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNllSSRT-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 lsVLQIIEEGLRVhqPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK11153 99 --VFDNVALPLEL--AGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK11153 174 ATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
306-508 |
1.11e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.84 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGLALHTLNRRqllpVRHRIQVVFQDPNssLNPRLS 380
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTT----IRMLLgllrpTSGEVRVLGEDVARDPAE----VRRRIGYVPQEPA--LYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG1131 90 VRENLRFFARLYG--LPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 461 QAQILTLLKSLQEKHRLayIFIS-HDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG1131 167 RRELWELLRELAAEGKT--VLLStHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
306-524 |
1.45e-43 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 155.49 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVR-HRIQVVFQdpNSSLNPRL 379
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKST----LLRCINrliepTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQ--SFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGL-DSEtrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:cd03294 118 TVLENVAFGLEVQG--VPRAEREERAAEALELVGLeGWE--HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQ 524
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
271-506 |
2.45e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.48 E-value: 2.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 271 GQAPLLEVEKLRVAFPIRKG---ILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSI 342
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvtALDDV----------SLTVAAGEFVALVGPSGCGKST----LLRLIAglekpTSGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 343 VFDGlalhtlnrRQLLPVRHRIQVVFQDPnsSLNPRLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRY 422
Cdd:COG1116 69 LVDG--------KPVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRG--VPKAERRERARELLELVGL-AGFEDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----RTVQAQILTLLkslqEKHRLAYIFISHDLH--VvrALCHQV 496
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQDELLRLW----QETGKTVLFVTHDVDeaV--FLADRV 209
|
250
....*....|..
gi 2551249897 497 IVL--RQGEVVE 506
Cdd:COG1116 210 VVLsaRPGRIVE 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-233 |
2.50e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.48 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQ--PLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRF 73
Cdd:COG1116 1 MSAaaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIaglekPT------SGEVLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 74 HGESLLHAneqtlrdvrGNKIAMIFQEPmvSLNP----LHNLEkqlyevLSL-HRGMRREAARAEILTCLDRVGIRQAAK 148
Cdd:COG1116 71 DGKPVTGP---------GPDRGVVFQEP--ALLPwltvLDNVA------LGLeLRGVPKAERRERARELLELVGLAGFED 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 149 RladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLS--IVkkLADT 226
Cdd:COG1116 134 A---YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaVF--LADR 208
|
....*..
gi 2551249897 227 VAVMQNG 233
Cdd:COG1116 209 VVVLSAR 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-248 |
3.35e-43 |
|
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: 153.26 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLlhaNEQT 85
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK--PT---SGEVLVDGKDI---TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEPmvslnplhnlEKQLYE--VLS------LHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQL 157
Cdd:COG1122 70 LRELR-RKVGLVFQNP----------DDQLFAptVEEdvafgpENLGLPREEIRERVEEALELVGLEHLADR---PPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|.
gi 2551249897 238 QNRAAQLLTAP 248
Cdd:COG1122 215 DGTPREVFSDY 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-249 |
3.67e-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: 154.05 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTAL-SILRLLPsppvvyP-SGDIRFHGESLlhaN 82
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLrALAGLLK------PsSGEVLLDGRDL---A 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDvRGNKIAMIFQEPMVSLnPLHnlekqLYEVLSL----HRGMRR---EAARAEILTCLDRVGIRQAAKRLADyph 155
Cdd:COG1120 67 SLSRRE-LARRIAYVPQEPPAPF-GLT-----VRELVALgrypHLGLFGrpsAEDREAVEEALERTGLEHLADRPVD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250
....*....|....
gi 2551249897 236 VEQNRAAQLLTAPT 249
Cdd:COG1120 217 VAQGPPEEVLTPEL 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
306-507 |
4.76e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 152.63 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalhtlnrRQLLPVRHRIQVVFQDPnsSLNPRLS 380
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKST----LLRIIAglerpTSGEVLVDG--------EPVTGPGPDRGYVFQQD--ALLPWLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03293 90 VLDNVALGLELQG--VPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVL--RQGEVVEQ 507
Cdd:cd03293 167 REQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
6.66e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 152.90 E-value: 6.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTAL-SILRLL-PSppvvypSGDIRFHGESLLHA 81
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKS-TLLrCLNGLVePT------SGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRDVRGnKIAMIFQEpmvslnplHNLEKQLYeVL-----------SLHRGMRREAARAEI---LTCLDRVGIRQAA 147
Cdd:COG3638 71 RGRALRRLRR-RIGMIFQQ--------FNLVPRLS-VLtnvlagrlgrtSTWRSLLGLFPPEDReraLEALERVGLADKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 148 KRLADyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTV 227
Cdd:COG3638 141 YQRAD---QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
....*....
gi 2551249897 228 AVMQNGQCV 236
Cdd:COG3638 218 IGLRDGRVV 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-259 |
1.42e-42 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 152.39 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGES- 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDV----SFDLYPGEVLGIVGESGSGKT-TLLNALsaRLAPD------AGEVHYRMRDg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 78 ----LLHANEQTLRDVRGNKIAMIFQEPMVSLNPL----HNLEKQLYEVLSLHRGMRREAAraeiLTCLDRVGIrqAAKR 149
Cdd:PRK11701 71 qlrdLYALSEAERRRLLRTEWGFVHQHPRDGLRMQvsagGNIGERLMAVGARHYGDIRATA----GDWLERVEI--DAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 150 LADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAV 229
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|
gi 2551249897 230 MQNGQCVEQNRAAQLLTAPTHPYTKKLLNS 259
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-254 |
1.98e-42 |
|
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: 151.50 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLLHANEQTLR 87
Cdd:cd03261 3 LRGLTKSFGG----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR--PD---SGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQEPMV--SLNPLHNLEKQLYEVLSLHRGMRREAARAeiltCLDRVGIRQAAKRladYPHQLSGGERQRV 165
Cdd:cd03261 74 RLR-RRMGMLFQSGALfdSLTVFENVAFPLREHTRLSEEEIREIVLE----KLEAVGLRGAEDL---YPAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLL 245
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
....*....
gi 2551249897 246 TApTHPYTK 254
Cdd:cd03261 226 AS-DDPLVR 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
306-526 |
4.95e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 153.76 E-value: 4.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTlNrrqlLPVRHR-IQVVFQDPnsSLNPRL 379
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTT----LLRIIAgletpDSGRIVLNGRDLFT-N----LPPRERrVGFVFQHY--ALFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQPtlSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:COG1118 91 TVAENIAFGLRVRPP--SKAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:COG1118 168 VRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-513 |
5.46e-42 |
|
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: 157.66 E-value: 5.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSVTaLSILRLLPS-PPVvypSGDIRFH---------- 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNI----SFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQyEPT---SGRIIYHvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 75 -------------GESL-------LHANEQTLRDVRgNKIAMIFQ-------EPMVSLNPLHNLEKQLYEvlslhrgmrr 127
Cdd:TIGR03269 73 erpskvgepcpvcGGTLepeevdfWNLSDKLRRRIR-KRIAIMLQrtfalygDDTVLDNVLEALEEIGYE---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 128 eaARAEILTCLDRVGIRQAAKRLADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELN 207
Cdd:TIGR03269 142 --GKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 208 MGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTA--PTHPYTKKLLNSEpsgdpvplpVGQaPLLEVEKLRVAF 285
Cdd:TIGR03269 220 ISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVfmEGVSEVEKECEVE---------VGE-PIIKVRNVSKRY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 286 -PIRKGILKrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVF-------DGLALHTLNRRQ 356
Cdd:TIGR03269 290 iSVDRGVVK-------AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVrvgdewvDMTKPGPDGRGR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 357 llpVRHRIQVVFQDpnSSLNPRLSVLQIIEEGLRVHQPtlsaeQREAQVKAV--MAEVGLDSETR----HRYPAEFSGGQ 430
Cdd:TIGR03269 363 ---AKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELP-----DELARMKAVitLKMVGFDEEKAeeilDKYPDELSEGE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 431 RQRIAIARALILKPSLIILDEPTSSLD----RTVQAQILTLLKSLQEkhrlAYIFISHDLHVVRALCHQVIVLRQGEVVE 506
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*..
gi 2551249897 507 QGQCEHV 513
Cdd:TIGR03269 509 IGDPEEI 515
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-249 |
9.61e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.85 E-value: 9.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTAL-SILRLLPspPVvypSGDIRFHGESLL 79
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKS-TLLkAILGLLP--PT---SGTVRLFGKPPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANeqtlrdvrgNKIAMIFQEPMVSLN-PLHnlekqLYEVLSL----HRGMRR---EAARAEILTCLDRVGIRQAAKRLA 151
Cdd:COG1121 72 RAR---------RRIGYVPQRAEVDWDfPIT-----VRDVVLMgrygRRGLFRrpsRADREAVDEALERVGLEDLADRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 152 DyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMq 231
Cdd:COG1121 138 G---ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL- 212
|
250
....*....|....*...
gi 2551249897 232 NGQCVEQNRAAQLLTAPT 249
Cdd:COG1121 213 NRGLVAHGPPEEVLTPEN 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
306-503 |
1.75e-41 |
|
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: 146.95 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlALHTLNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:cd03229 20 SLNIEAGEIVALLGPSGSGKST----LLRCIAgleepDSGSILIDG-EDLTDLEDELPPLRRRIGMVFQDFA--LFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLrvhqptlsaeqreaqvkavmaevgldsetrhrypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03229 93 VLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-505 |
2.00e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.57 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 29 SLRVDAGQTLALVGESGSGKSvTALSILrllpsppvvY----P-SGDIRFHGEsllhanEQTL---RDVRGNKIAMIFQE 100
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKS-TLMKIL---------YglyqPdSGEILIDGK------PVRIrspRDAIALGIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 PMV--SLNPLHNLekqlyeVLSLHRG----MRREAARAEILTCLDRVGIRQAAKRLAdypHQLSGGERQRVMIAMALLTR 174
Cdd:COG3845 89 FMLvpNLTVAENI------VLGLEPTkggrLDRKAARARIRELSERYGLDVDPDAKV---EDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 175 PELLIADEPTTALdvSVQ--AQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEqnraaqllTAPTHPY 252
Cdd:COG3845 160 ARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVG--------TVDTAET 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 253 TKKLLNSEPSGDPVPLPV------GQAPLLEVEKLRVAFPIRKGILKRvvdhnvvvndVSFSLRPGETLGLVGESGSGKS 326
Cdd:COG3845 229 SEEELAELMVGREVLLRVekapaePGEVVLEVENLSVRDDRGVPALKD----------VSLEVRAGEILGIAGVAGNGQS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 327 ttglALLRLIT-----SQGSIVFDGLALHTLNRRQLLpvRHRIQVVFQDPNSS-LNPRLSV-----LQIIEEGLRVHQPT 395
Cdd:COG3845 299 ----ELAEALAglrppASGSIRLDGEDITGLSPRERR--RLGVAYIPEDRLGRgLVPDMSVaenliLGRYRRPPFSRGGF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 396 LSAEQREAQVKAVMAE-----VGLDSETRHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKS 470
Cdd:COG3845 373 LDRKAIRAFAEELIEEfdvrtPGPDTPARS-----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
|
490 500 510
....*....|....*....|....*....|....*
gi 2551249897 471 LQEKhRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:COG3845 448 LRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
306-508 |
3.20e-41 |
|
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: 157.69 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnp 377
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKST----LLKLLLglyepTSGRILIDGIDLRQIDPASL---RRQIGVVLQDVflfSGT--- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 rlsvlqiIEEGLRVHQPTLSaeqrEAQVKAVMAEVGLDSETRHRyP-----------AEFSGGQRQRIAIARALILKPSL 446
Cdd:COG2274 565 -------IRENITLGDPDAT----DEEIIEAARLAGLHDFIEAL-PmgydtvvgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 447 IILDEPTSSLDRTVQAQILTLLKSLQEKHRLayIFISHDLHVVRaLCHQVIVLRQGEVVEQG 508
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-259 |
3.43e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.11 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLR 87
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPT----SGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQepmvslnplH-NL--EKQLYEVLSLH---RGMRREAARAEILTCLDRVGIrqAAKRLAdYPHQLSGGE 161
Cdd:PRK11153 79 KAR-RQIGMIFQ---------HfNLlsSRTVFDNVALPlelAGTPKAEIKARVTELLELVGL--SDKADR-YPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRA 241
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
250
....*....|....*...
gi 2551249897 242 AQLLTAPTHPYTKKLLNS 259
Cdd:PRK11153 226 SEVFSHPKHPLTREFIQS 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-242 |
3.86e-41 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 147.97 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPT----SGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQEPMV--SLNPLHN----LEKqlyevlslhRGMRREAARAEILtcLDRVGIrqaAKRLADYP 154
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSFQLlpTLTALENvmlpLEL---------AGRRDARARARAL--LERVGL---GHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQNGQ 234
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*...
gi 2551249897 235 CVEQNRAA 242
Cdd:COG4181 224 LVEDTAAT 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-259 |
4.62e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 148.78 E-value: 4.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFR------QQETVRTVVNtLSLRVDAGQTLALVGESGSGKSVTAlsilRLLPSppVVYPSGdirfhGESL 78
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfRRQTVEAVKP-LSFTLREGQTLAIIGENGSGKSTLA----KMLAG--MIEPTS-----GELL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 79 LHANEQTLRDV--RGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRqaAKRLADYPHQ 156
Cdd:PRK15112 72 IDDHPLHFGDYsyRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLL--PDHASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 2551249897 237 EQNRAAQLLTAPTHPYTKKLLNS 259
Cdd:PRK15112 230 ERGSTADVLASPLHELTKRLIAG 252
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
255-508 |
6.89e-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: 154.92 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 255 KLLNSEPSGDP---VPLPVGQAPLLEVEKLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTTGLA 331
Cdd:COG4988 313 ALLDAPEPAAPagtAPLPAAGPPSIELEDVSFSYPGGRPALD----------GLSLTIPPGERVALVGPSGAGKSTLLNL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 332 LLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPTLSaeqrEAQVKA 407
Cdd:COG4988 383 LLGFLPpYSGSILINGVDLSDLDPASW---RRQIAWVPQNPylfAGT----------IRENLRLGRPDAS----DEELEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 408 VMAEVGLDSETRhRYP-----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHR 476
Cdd:COG4988 446 ALEAAGLDEFVA-ALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT 524
|
250 260 270
....*....|....*....|....*....|..
gi 2551249897 477 LayIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG4988 525 V--ILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-508 |
7.93e-41 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 147.44 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLN 353
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALK----------NINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 354 RRQLLPVRHRIQVVFQDPNssLNPRLSVLQIIEEGLRVHQPTL--------SAEQREAqvKAVMAEVGLDsETRHRYPAE 425
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQHYN--LIERLTVLENVLHGRLGYKPTWrsllgrfsEEDKERA--LSALERVGLA-DKAYQRADQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
...
gi 2551249897 506 EQG 508
Cdd:TIGR02315 226 FDG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
1.33e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.86 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSVTalsiLRLL-----PSppvvypSGDIRFHG 75
Cdd:COG3842 1 MAMPALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMIagfetPD------SGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 76 ESLLH--ANEqtlRDvrgnkIAMIFQE----PMvsLNPLHN----LEkqlyevlslHRGMRREAARAEILTCLDRVGIRQ 145
Cdd:COG3842 67 RDVTGlpPEK---RN-----VGMVFQDyalfPH--LTVAENvafgLR---------MRGVPKAEIRARVAELLELVGLEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 146 AAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHN----LSivk 221
Cdd:COG3842 128 LADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA--- 201
|
250 260 270
....*....|....*....|....*....|.
gi 2551249897 222 kLADTVAVMQNGQCVEQNRAAQLLTAPTHPY 252
Cdd:COG3842 202 -LADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-274 |
2.18e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 147.14 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLS-----VGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTAlSILRLLPSPPvvypSGDIRFHGESL 78
Cdd:PRK10419 2 TLLNVSGLShhyahGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLA-RLLVGLESPS----QGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 79 LHANEQTLRDVRGNkIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQA-AKRLadyPHQL 157
Cdd:PRK10419 77 AKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKR---PPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 2551249897 238 QNRAAQLLTApTHPYTKKLLNSEPSGDPVPLPVGQAP 274
Cdd:PRK10419 233 TQPVGDKLTF-SSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
306-518 |
2.21e-40 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 145.94 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITS-----QGSIVFDGLALHTLNrrqllPVRHRIQVVFQdpNSSLNPRLS 380
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSV----LLETIAGfikpdSGKILLNGKDITNLP-----PEKRDISYVPQ--NYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03299 88 VYKNIAYGLKKR--KVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
306-527 |
2.71e-40 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 146.38 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-----TSQGSIVFDGLALHTlnrrQLLPVRHrIQVVFQDPNSSLNPRLS 380
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAP----CALRGRK-IATIMQNPRSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVhqptLSAEQREAQVKAVMAEVGLDSETR--HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK10418 98 MHTHARETCLA----LGKPADDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-504 |
3.14e-40 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 152.39 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFrqqETVRTVvNTLSLRVDAGQTLALVGESGSGKSvTALSILrllpspPVVYP----SGDIRFHGE 76
Cdd:PRK13549 1 MMEYLLEMKNITKTF---GGVKAL-DNVSLKVRAGEIVSLCGENGAGKS-TLMKVL------SGVYPhgtyEGEIIFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 77 sLLHAneQTLRDVRGNKIAMIFQEPMV--SLNPLHNLekQLYEVLSLHRGMRREAARAEILTCLDRVGIR-QAAKRLADY 153
Cdd:PRK13549 70 -ELQA--SNIRDTERAGIAIIHQELALvkELSVLENI--FLGNEITPGGIMDYDAMYLRAQKLLAQLKLDiNPATPVGNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 phqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:PRK13549 145 ----GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 234 QCVEQNRAAQLLTAP--THPYTKKLLNSEPSgdpVPLPVGQApLLEVEKLRVAFPIRKGIlKRvvdhnvvVNDVSFSLRP 311
Cdd:PRK13549 220 RHIGTRPAAGMTEDDiiTMMVGRELTALYPR---EPHTIGEV-ILEVRNLTAWDPVNPHI-KR-------VDDVSFSLRR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTTGLALL-----RlitSQGSIVFDGLALHTLNRRQllPVRHRIQVVFQD-------PNSSL--NP 377
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFgaypgR---WEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDrkrdgivPVMGVgkNI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLQIIEEGLRVHQptlSAEQREAQvkAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK13549 363 TLAALDRFTGGSRIDD---AAELKTIL--ESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2551249897 458 RTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
276-511 |
3.75e-40 |
|
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: 145.40 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 276 LEVEKLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALH 350
Cdd:cd03256 1 IEVENLSKTYPNGKKALK----------DVSLSINPGEFVALIGPSGAGKST----LLRCLNglvepTSGSVLIDGTDIN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 351 TLNRRQLLPVRHRIQVVFQDPNssLNPRLSVLQIIEEGLRVHQPTLS--------AEQREAqvKAVMAEVGLDSETRHRy 422
Cdd:cd03256 67 KLKGKALRQLRRQIGMIFQQFN--LIERLSVLENVLSGRLGRRSTWRslfglfpkEEKQRA--LAALERVGLLDKAYQR- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQG 502
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
....*....
gi 2551249897 503 EVVEQGQCE 511
Cdd:cd03256 222 RIVFDGPPA 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
273-527 |
3.96e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.10 E-value: 3.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVF 344
Cdd:COG4598 6 PPALEVRDLHKSFgdlEVLKGV--------------SLTARKGDVISIIGSSGSGKST----FLRCINlletpDSGEIRV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 345 DG----------LALHTLNRRQLLPVRHRIQVVFQDPNssLNPRLSVLQ-IIEEGLRVHQptLSAEQREAQVKAVMAEVG 413
Cdd:COG4598 68 GGeeirlkpdrdGELVPADRRQLQRIRTRLGMVFQSFN--LWSHMTVLEnVIEAPVHVLG--RPKAEAIERAEALLAKVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 414 LdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALC 493
Cdd:COG4598 144 L-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVS 221
|
250 260 270
....*....|....*....|....*....|....
gi 2551249897 494 HQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:COG4598 222 SHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLS 255
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
306-508 |
1.03e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.23 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRqllpVRHRIQVVFQDPNssLNPRLS 380
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTT----LLRMLAgllkpDSGSILIDGEDVRKEPRE----ARRQIGVLPDERG--LYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG4555 91 VRENIRYFAELYG--LFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4555 168 RRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
306-526 |
1.97e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 146.20 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQGSI-----VFDG---LALHTLNRRQLlpVRHRIQVVFQDPNSSLNP 377
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrfRWNGidlLKLSPRERRKI--IGREIAMIFQEPSSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLQIIEEGLRVHQPTLS----AEQREAQVKAVMAEVGLDSetrHR-----YPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:COG4170 105 SAKIGDQLIEAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKD---HKdimnsYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 449 LDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
273-529 |
2.51e-39 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 143.82 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFPIRKGIlkrvvdhnvvvNDVSFSLRPGETLGLVGESGSGKSTTGLALL-RLITSQGSIVFDG----- 346
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGC-----------RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYIMrsgae 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 ---LALHTLNRRQLLpvRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQPTLSAEQREAQVKAvMAEVGLDSETRHRYP 423
Cdd:TIGR02323 70 lelYQLSEAERRRLM--RTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDW-LEEVEIDPTRIDDLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:TIGR02323 147 RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR 226
|
250 260
....*....|....*....|....*.
gi 2551249897 504 VVEQGQCEHVFNAPQQAYTrQLLALS 529
Cdd:TIGR02323 227 VVESGLTDQVLDDPQHPYT-QLLVSS 251
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
306-454 |
2.75e-39 |
|
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: 140.09 E-value: 2.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNssLNPRLS 380
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKST----LLKLIAgllspTEGTILLDGQDLTDDERKSL---RKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 381 VLQIIEEGLRVhqPTLSAEQREAQVKAVMAEVGL--DSETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:pfam00005 76 VRENLRLGLLL--KGLSKREKDARAEEALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-230 |
2.85e-39 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 142.23 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaneqt 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIAGLERPT----SGEVLVDGEPV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 lrDVRGNKIAMIFQEPmvSLNP----LHNLEkqlyevLSL-HRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGG 160
Cdd:cd03293 69 --TGPGPDRGYVFQQD--ALLPwltvLDNVA------LGLeLQGVPKAEARERAEELLELVGLSGFENA---YPHQLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVM 230
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-521 |
4.13e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.54 E-value: 4.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVF 344
Cdd:COG1121 4 MPAIELENLTVSYggrPVLEDV--------------SLTIPPGEFVAIVGPNGAGKST----LLKAILgllppTSGTVRL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 345 DGLALHTlnrrqllpVRHRIQVVFQDPNSSLNPRLSVLQIIEEGLRVHQP---TLSAEQREAqVKAVMAEVGLdSETRHR 421
Cdd:COG1121 66 FGKPPRR--------ARRRIGYVPQRAEVDWDFPITVRDVVLMGRYGRRGlfrRPSRADREA-VDEALERVGL-EDLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQeKHRLAYIFISHDLHVVRALCHQVIVLRQ 501
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNR 214
|
250 260
....*....|....*....|..
gi 2551249897 502 GeVVEQGQCEHVFNAP--QQAY 521
Cdd:COG1121 215 G-LVAHGPPEEVLTPEnlSRAY 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
306-515 |
5.22e-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: 143.34 E-value: 5.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSIVFDGlaLHTLNRRQLLPVRHRIQVVFQDPNSSLnprls 380
Cdd:TIGR04520 22 SLSIEKGEFVAIIGHNGSGKSTlakllNGL----LLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVFQNPDNQF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEE----GLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:TIGR04520 91 VGATVEDdvafGLENLG--VPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
306-518 |
6.96e-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 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: 142.98 E-value: 6.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSslnprls 380
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTliqhlNGL----LKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEH------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 vlQIIEE--------GLRvhQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:TIGR04521 94 --QLFEEtvykdiafGPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
269-509 |
1.08e-38 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 141.03 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 269 PVGQAPLLEVEKLRVAFPIRKG---ILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQG 340
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGeltILKGI----------SLEVEAGESVAIVGASGSGKST----LLGLLagldrPTSG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 341 SIVFDGLALHTLNRRQLLPVR-HRIQVVFQdpNSSLNPRLSVLQiieeglRVHQPTLSAEQREAQVKA--VMAEVGLDSE 417
Cdd:COG4181 68 TVRLAGQDLFALDEDARARLRaRHVGFVFQ--SFQLLPTLTALE------NVMLPLELAGRRDARARAraLLERVGLGHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 418 TRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVI 497
Cdd:COG4181 140 LDH-YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVL 217
|
250
....*....|..
gi 2551249897 498 VLRQGEVVEQGQ 509
Cdd:COG4181 218 RLRAGRLVEDTA 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-237 |
1.12e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 140.95 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQ 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPT----SGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRGNKIAMIFQ--EPMVSLNPLHNLEKQLyevlsLHRGMRREAARAEILTCLDRVGIRqaaKRLADYPHQLSGGER 162
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKSVKEAKERAYEMLEKVGLE---HRINHRPSELSGGER 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLaDTVAVMQNGQCVE 237
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
306-503 |
1.46e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 138.67 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprlsv 381
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDpTSGEILIDGVDLRDLDLESL---RKNIAYVPQDPflfSGT------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 lqiIEEGLrvhqptlsaeqreaqvkavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQ 461
Cdd:cd03228 92 ---IRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2551249897 462 AQILTLLKSLQEKHRLayIFISHDLHVVRaLCHQVIVLRQGE 503
Cdd:cd03228 133 ALILEALRALAKGKTV--IVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-234 |
2.87e-38 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 139.52 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLlhaNEQT 85
Cdd:cd03225 2 LKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKS-TLLRLLngLLGPT------SGEVLVDGKDL---TKLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGnKIAMIFQEPmvslnplhnlEKQLY------EVLS--LHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQL 157
Cdd:cd03225 70 LKELRR-KVGLVFQNP----------DDQFFgptveeEVAFglENLGLPEEEIEERVEEALELVGLEGLRDR---SPFTL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03225 136 SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-244 |
2.90e-38 |
|
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: 140.01 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL-RLLPSPPVVYPSGDIRFHGESLLHANEQ 84
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKS-TLLRLLnRLNDLIPGAPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRgnKIAMIFQEPmvslNPLHnleKQLYEVLSL---HRGMRREAARAEI-LTCLDRVGIRQAAKRLADyPHQLSGG 160
Cdd:cd03260 76 VLELRR--RVGMVFQKP----NPFP---GSIYDNVAYglrLHGIKLKEELDERvEEALRKAALWDEVKDRLH-ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElnMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNR 240
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
....
gi 2551249897 241 AAQL 244
Cdd:cd03260 224 TEQI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-238 |
1.32e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 137.65 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLH 80
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIaglerPD------SGEILIDGRDVTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 aneqtlRDVRGNKIAMIFQEPmvSLNPLHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGG 160
Cdd:cd03259 67 ------VPPERRNIGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGqCVEQ 238
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG-RIVQ 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
306-504 |
3.23e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnsslnpRL- 379
Cdd:COG4619 20 SLTLEAGECVAITGPSGSGKST----LLRALadldpPTSGEIYLDGKPLSAMPPPEW---RRQVAYVPQEP------ALw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 --SVLQIIEEGLRVHQPTLSAEQreaqVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:COG4619 87 ggTVRDNLPFPFQLRERKFDRER----ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 458 RTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:COG4619 163 PENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-238 |
3.80e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 135.26 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 7 AIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTAL-SILRLLPSPpvvypSGDIRFHGESLLHANeqt 85
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLkTLAGLLKPS-----SGEILLDGKDLASLS--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 lrdvrgnkiamifqepmvslnplhnlekqlyevlslhrgmRREAAR--AEILTCLDRVGIRQAAKRLADyphQLSGGERQ 163
Cdd:cd03214 68 ----------------------------------------PKELARkiAYVPQALELLGLAHLADRPFN---ELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
306-517 |
5.07e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.21 E-value: 5.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGlalHTLNRrqlLPVRHR-IQVVFQDPnsSLNPRL 379
Cdd:COG3839 23 DLDIEDGEFLVLLGPSGCGKST----LLRMIagledPTSGEILIGG---RDVTD---LPPKDRnIAMVFQSY--ALYPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:COG3839 91 TVYENIAFPLKLRK--VPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:COG3839 168 LRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
306-526 |
5.32e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.42 E-value: 5.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGlALHTlnrrQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKST----LLNLIagflpPDSGRILWNG-QDLT----ALPPAERPVSMLFQENN--LFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRvhqPT--LSAEQReAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:COG3840 88 VAQNIGLGLR---PGlkLTAEQR-AQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-504 |
7.86e-37 |
|
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: 142.66 E-value: 7.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 23 TVVNTLSLRVDAGQTLALVGESGSGKSvTALSILrllpspPVVYP----SGDIRFHGESLlhaNEQTLRDVRGNKIAMIF 98
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKS-TLMKIL------SGVYPhgtwDGEIYWSGSPL---KASNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 99 QEPMVSLNpLHNLEKQLYEVLSLHRGMRREAA----RAEILTCLDRVGIRQAAKRLADYphqlSGGERQRVMIAMALLTR 174
Cdd:TIGR02633 85 QELTLVPE-LSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPVGDY----GGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 175 PELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVeQNRAAQLLTAP---THP 251
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMSEDdiiTMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 252 YTKKLLNSEPSGdpvPLPVGQApLLEVEKLRVAFPIRKGIlKRVVDHnvvvndvSFSLRPGETLGLVGESGSGKSTTGLA 331
Cdd:TIGR02633 238 VGREITSLYPHE---PHEIGDV-ILEARNLTCWDVINPHR-KRVDDV-------SFSLRRGEILGVAGLVGAGRTELVQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 332 LLRLITSQ--GSIVFDGLALHTLNRRQllPVRHRIQVVFQD-PNSSLNPRLSVLQIIEEGLRVHQPTLSAEQREAQVKAV 408
Cdd:TIGR02633 306 LFGAYPGKfeGNVFINGKPVDIRNPAQ--AIRAGIAMVPEDrKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQII 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 409 MAEVG-LDSETRHRY--PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHrLAYIFISHD 485
Cdd:TIGR02633 384 GSAIQrLKVKTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSE 462
|
490
....*....|....*....
gi 2551249897 486 LHVVRALCHQVIVLRQGEV 504
Cdd:TIGR02633 463 LAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
306-504 |
8.46e-37 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 135.35 E-value: 8.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALhTLNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKST----LLRCInlleePDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQFN--LFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLR-VHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:cd03262 93 VLENITLAPIkVKG--MSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 460 VQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:cd03262 170 LVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
306-518 |
1.42e-36 |
|
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: 135.44 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHtlnrrQLLPVRHRIQVVFQdpNSSLNPRLS 380
Cdd:cd03300 20 SLDIKEGEFFTLLGPSGCGKTT----LLRLIAgfetpTSGEILLDGKDIT-----NLPPHKRPVNTVFQ--NYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03300 89 VFENIAFGLRLKK--LPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-234 |
3.02e-36 |
|
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: 133.81 E-value: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHaNEQTLR 87
Cdd:cd03262 3 IKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEEPD----SGTIIIDGLKLTD-DKKNIN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQE----PmvSLNPLHNLEKQLYEVlslhRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSGGERQ 163
Cdd:cd03262 73 ELR-QKVGMVFQQfnlfP--HLTVLENITLAPIKV----KGMSKAEAEERALELLEKVGL---ADKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
306-508 |
4.12e-36 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 133.57 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLR-----PGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHR-IQVVFQdpNSS 374
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKST----LLRCIAglekpDGGTIVLNGTVLFDSRKKINLPPQQRkIGLVFQ--QYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 375 LNPRLSVLQIIEEGLRVHQPtlsAEQREaQVKAVMAEVGLDSETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03297 86 LFPHLNVRENLAFGLKRKRN---REDRI-SVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
306-499 |
4.86e-36 |
|
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: 133.43 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalhtlnrRQLLPVRHRIQVVFQDPNSSLNPRLS 380
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKST----LLKAILgllkpTSGSIRVFG--------KPLEKERKRIGYVPQRRSIDRDFPIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGL---RVHQPTLSAEQREAqVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03235 87 VRDVVLMGLyghKGLFRRLSKADKAK-VDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2551249897 458 RTVQAQILTLLKSLQEKHRLAyIFISHDLHVVRALCHQVIVL 499
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTI-LVVTHDLGLVLEYFDRVLLL 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
306-517 |
5.48e-36 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 137.15 E-value: 5.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLNRRQLLPV-RHRIQVVFQDPnsSLNPRL 379
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTT----LLRAIaglerPDSGRIRLGGEVLQDSARGIFLPPhRRRIGYVFQEA--RLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVhqptLSAEQREAQVKAVMAEVGLDsetrH---RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:COG4148 93 SVRGNLLYGRKR----APRAERRISFDEVVELLGIG----HlldRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-234 |
6.52e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 131.75 E-value: 6.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLLHANE 83
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKT-TLIKIIlgLLKPD------SGEIKVLGKDIKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRdvrgnKIAMIFQEPMvslnplhnlekqLYEVLSLHrgmrreaaraEILtcldrvgirqaakrladyphQLSGGERQ 163
Cdd:cd03230 70 EVKR-----RIGYLPEEPS------------LYENLTVR----------ENL--------------------KLSGGMKQ 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
306-508 |
1.00e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 140.69 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnp 377
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKST----LVNLLLrfydpTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTflfSGT--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 rlsvlqiIEEGLRVHQPTLSAEQ-REAqvkAVMAEV---------GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:COG1132 430 -------IRENIRYGRPDATDEEvEEA---AKAAQAhefiealpdGYDTVVGER-GVNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 448 ILDEPTSSLD----RTVQAQILTLLkslqeKHRLAyIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:COG1132 499 ILDEATSALDteteALIQEALERLM-----KGRTT-IVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
306-518 |
1.14e-35 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 132.95 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpVRHRIQVVFQdpNSSLNPRLS 380
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTT----LFNLISgflrpTSGSVLFDGEDITGLPPHEI--ARLGIGRTFQ--IPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPTL------SAEQREAQVKA--VMAEVGLDSEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03219 92 VLENVMVAAQARTGSGlllaraRREEREARERAeeLLERVGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:cd03219 171 AAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
273-521 |
1.45e-35 |
|
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: 133.24 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFpirkGILKrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGL 347
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLV-------AVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLITgfyrpTSGRILFDGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 348 ALHTLNRRQLlpVRHRIQVVFQdpNSSLNPRLSVLQIIEEGLRVHQ-----------PTLSAEQREAQVKA--VMAEVGL 414
Cdd:COG0411 67 DITGLPPHRI--ARLGIARTFQ--NPRLFPELTVLENVLVAAHARLgrgllaallrlPRARREEREARERAeeLLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 415 DSEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCH 494
Cdd:COG0411 143 ADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLAD 221
|
250 260
....*....|....*....|....*....
gi 2551249897 495 QVIVLRQGEVVEQGQCEHVFNAP--QQAY 521
Cdd:COG0411 222 RIVVLDFGRVIAEGTPAEVRADPrvIEAY 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-230 |
1.56e-35 |
|
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: 131.89 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTAL-SILRLLPsppvvyP-SGDIRFHGESLlhaneqt 85
Cdd:cd03235 2 VEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLK------PtSGSIRVFGKPL------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 lRDVRgNKIAMIFQEPMVSLN-PLhnlekQLYEVLSL----HRGMRR---EAARAEILTCLDRVGIRQAAKRLADyphQL 157
Cdd:cd03235 64 -EKER-KRIGYVPQRRSIDRDfPI-----SVRDVVLMglygHKGLFRrlsKADKAKVDEALERVGLSELADRQIG---EL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVM 230
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
306-526 |
1.69e-35 |
|
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: 132.81 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLalhtlNRRQLLPV--RHRIQVVFQdpNSSLNPRLSVL 382
Cdd:cd03295 21 NLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGE-----DIREQDPVelRRKIGYVIQ--QIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIeeGLrvhQPTL---SAEQREAQVKAVMAEVGLDSET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:cd03295 94 ENI--AL---VPKLlkwPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-236 |
1.72e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 132.69 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQT 85
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGnKIAMIFQEpmvslnplHNLEKQLY---EVL-------SLHRGMRR---EAARAEILTCLDRVGIRQAAKRLAD 152
Cdd:cd03256 73 LRQLRR-QIGMIFQQ--------FNLIERLSvleNVLsgrlgrrSTWRSLFGlfpKEEKQRALAALERVGLLDKAYQRAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQN 232
Cdd:cd03256 144 ---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
....
gi 2551249897 233 GQCV 236
Cdd:cd03256 221 GRIV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-252 |
2.38e-35 |
|
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: 133.15 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQETVR----TV-VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHG 75
Cdd:cd03294 12 KNPQKAFKLLAKGKSKEEILKktgqTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePT------SGKVLIDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 76 ESLLHANEQTLRDVRGNKIAMIFQE--PMVSLNPLHNLEKQLyEVlslhRGMRREAARAEILTCLDRVGIRQAAKRladY 153
Cdd:cd03294 86 QDIAAMSRKELRELRRKKISMVFQSfaLLPHRTVLENVAFGL-EV----QGVPRAEREERAAEALELVGLEGWEHK---Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:cd03294 158 PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
250
....*....|....*....
gi 2551249897 234 QCVEQNRAAQLLTAPTHPY 252
Cdd:cd03294 238 RLVQVGTPEEILTNPANDY 256
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-257 |
2.43e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 29 SLRVDAGQTLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESLLHaneqTLRDVRgnKIAMIFQEpmvsln 106
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS-TLLNLIAgfLPPD------SGRILWNGQDLTA----LPPAER--PVSMLFQE------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 107 plHNL------EKQLYevLSLHRGMR-REAARAEILTCLDRVGIRQAAKRLadyPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:COG3840 80 --NNLfphltvAQNIG--LGLRPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 180 ADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPTHPYTKKLL 257
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-234 |
2.69e-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: 131.26 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 35 GQTLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHANEQTLRDVRGNKIAMIFQEpmVSLNPLHNLEKQ 114
Cdd:cd03297 23 EEVTGIFGASGAGKS-TLLRCIAGLEKPDG----GTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 115 LYEVLSLHRGMRREAARAEILtclDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQ 194
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELL---DLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2551249897 195 ILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
306-513 |
4.63e-35 |
|
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: 131.15 E-value: 4.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI----------TSQGSIVFDGLALHTLNRRQLLpVRHRIQVVFQDPNssl 375
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKST----LLRLLnrlndlipgaPDEGEVLLDGKDIYDLDVDVLE-LRRRVGMVFQKPN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 nP-RLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:cd03260 92 -PfPGSIYDNVAYGLRLHG-IKLKEELDERVEEALRKAALWDEVkDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 454 SSLDRTVQAQILTLLKSLqeKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:cd03260 170 SALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
306-504 |
5.53e-35 |
|
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: 129.05 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGLALHTLNRRqllpVRHRIQVVFQDPnsSLNPRLS 380
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTL----IKIILgllkpDSGEIKVLGKDIKKEPEE----VKRRIGYLPEEP--SLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEeglrvhqptlsaeqreaqvkavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03230 90 VRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2551249897 461 QAQILTLLKSLQEKHRLAyIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:cd03230 131 RREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
306-515 |
6.60e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 132.48 E-value: 6.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSIVFDGLALhTLNRRQLLPVRHRIQVVFQDPNSSLNPRlS 380
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTliqhlNGL----LKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRvhQPTLSAEQREAQVKAVMAEVGLDSET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:PRK13637 101 IEKDIAFGPI--NLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
267-528 |
7.66e-35 |
|
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: 137.98 E-value: 7.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 267 PLPVGQAPLLEVEKLRVAFPirkgilkrvVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFD 345
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYP---------GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpQSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 346 GLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPTLSaeqrEAQVKAVMAEVGLDS------ 416
Cdd:COG4987 396 GVDLRDLDEDDL---RRRIAVVPQRPhlfDTT----------LRENLRLARPDAT----DEELWAALERVGLGDwlaalp 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 417 ---ETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL-TLLKSLQEKhrlAYIFISHDLHVVrA 491
Cdd:COG4987 459 dglDTWlGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGR---TVLLITHRLAGL-E 534
|
250 260 270
....*....|....*....|....*....|....*..
gi 2551249897 492 LCHQVIVLRQGEVVEQGQceHVFNAPQQAYTRQLLAL 528
Cdd:COG4987 535 RMDRILVLEDGRIVEQGT--HEELLAQNGRYRQLYQR 569
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-506 |
9.91e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 136.73 E-value: 9.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFrqqeTVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHgesllhaneqt 85
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKS-TLLKILagELEPD------SGEVSIP----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 lrdvRGNKIAMIFQEP------------MVSLNPLHNLEKQLYEVLSLHRGMRREAAR-AEILTCLDRVG-------IRQ 145
Cdd:COG0488 59 ----KGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERlAELQEEFEALGgweaearAEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 146 AAKRL---ADYPHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQaqilqLLRELQHELNMGLLFITHNL 217
Cdd:COG0488 135 ILSGLgfpEEDLDRpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 218 SIVKKLADTVAVMQNGQCVE--------------------------QNRAAQLLT------------------------- 246
Cdd:COG0488 210 YFLDRVATRILELDRGKLTLypgnysayleqraerleqeaaayakqQKKIAKEEEfirrfrakarkakqaqsrikalekl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 247 -----APTHPYTK-KLLNSEPSGDPVplpvgqaplLEVEKLRVAFPIRKgILKRVvdhnvvvndvSFSLRPGETLGLVGE 320
Cdd:COG0488 290 ereepPRRDKTVEiRFPPPERLGKKV---------LELEGLSKSYGDKT-LLDDL----------SLRIDRGDRIGLIGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 321 SGSGKSTtglaLLRLIT-----SQGSIVFdGlalhtlnrrqllpvrHRIQVVF--QDpNSSLNPRLSVLQIIEEGlrvhq 393
Cdd:COG0488 350 NGAGKST----LLKLLAgelepDSGTVKL-G---------------ETVKIGYfdQH-QEELDPDKTVLDELRDG----- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 394 ptlSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-RTVQAqiltLLKSLQ 472
Cdd:COG0488 404 ---APGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDiETLEA----LEEALD 476
|
570 580 590
....*....|....*....|....*....|....*...
gi 2551249897 473 EkhrlaY----IFISHDLHVVRALCHQVIVLRQGEVVE 506
Cdd:COG0488 477 D-----FpgtvLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-237 |
1.12e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHAN 82
Cdd:COG2884 4 FENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLygeerPT------SGQVLVNGQDLSRLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDVRgNKIAMIFQEpmvslnplHNL--EKQLYE--VLSLH-RGMRREAARAEILTCLDRVGIRQAAKRladYPHQL 157
Cdd:COG2884 71 RREIPYLR-RRIGVVFQD--------FRLlpDRTVYEnvALPLRvTGKSRKEIRRRVREVLDLVGLSDKAKA---LPHEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-234 |
2.59e-34 |
|
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: 127.30 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGEsLLHANEQT 85
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKS-TLLRCIAGLEEPD----SGSILIDGE-DLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEPmvSLNPLhnlekqlyevlslhrgmrreaaraeiLTCLDRVGIRqaakrladyphqLSGGERQRV 165
Cdd:cd03229 71 LPPLR-RRIGMVFQDF--ALFPH--------------------------LTVLENIALG------------LSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-260 |
4.34e-34 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 128.96 E-value: 4.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHANEQ 84
Cdd:cd03295 1 IEFENVTKRYGG---GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT------SGEIFIDGEDIREQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRdvrgNKIAMIFQEpmVSLNPLHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIrQAAKRLADYPHQLSGGERQR 164
Cdd:cd03295 72 ELR----RKIGYVIQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQL 244
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 2551249897 245 LTAPTHPYTKKLLNSE 260
Cdd:cd03295 224 LRSPANDFVAEFVGAD 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-252 |
5.01e-34 |
|
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: 136.50 E-value: 5.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLH 80
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRdvrgNKIAMIFQEPMV---SLnpLHNLekqlyevlslhRGMRREAARAEILTCLDRVGIRQAAKRLA---DYP 154
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFLfsgTI--RENI-----------TLGDPDATDEEIIEAARLAGLHDFIEALPmgyDTV 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 -----HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVkKLADTVAV 229
Cdd:COG2274 605 vgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIV 681
|
250 260
....*....|....*....|...
gi 2551249897 230 MQNGQCVEQNRAAQLLTAPTHPY 252
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYA 704
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-227 |
5.02e-34 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 127.73 E-value: 5.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHANEQTLR 87
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEK----FDSGQVYLNGQETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRGNKIAMIFQEpmVSLNPLHNLEKQLYEVLSLHRGMRREAaRAEILTCLDRVGIRqaaKRLADYPHQLSGGERQRVMI 167
Cdd:TIGR03608 72 KFRREKLGYLFQN--FALIENETVEENLDLGLKYKKLSKKEK-REKKKEALEKVGLN---LKLKQKIYELSGGEQQRVAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKlADTV 227
Cdd:TIGR03608 146 ARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRV 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-257 |
5.48e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLh 80
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKT----TLLRIIagletPD------SGRIVLNGRDLF- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 aneqTLRDVRGNKIAMIFQEPMvsLNPlH-----N----LEkqlyevlslHRGMRREAARAEILTCLDRVGIRQAAKRla 151
Cdd:COG1118 68 ----TNLPPRERRVGFVFQHYA--LFP-HmtvaeNiafgLR---------VRPPSKAEIRARVEELLELVQLEGLADR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 152 dYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQ 231
Cdd:COG1118 130 -YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
250 260
....*....|....*....|....*.
gi 2551249897 232 NGQCVEQNRAAQLLTAPTHPYTKKLL 257
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
309-526 |
9.56e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 128.33 E-value: 9.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 309 LRPGETLGLVGESGSGKSTtglaLLRLIT----------SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNssLNPR 378
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTT----LLRCINlleqpeagtiRVGDITIDTARSLSQQKGLIRQLRQHVGFVFQNFN--LFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVLQIIEEGLRVHQPTlSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK11264 100 RTVLENIIEGPVIVKGE-PKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIfISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-238 |
1.51e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 128.32 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTA--LSILrLLPSppvvypSGDIRFHGESLLhaNEQT 85
Cdd:TIGR04520 3 VENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAklLNGL-LLPT------SGKVTVDGLDTL--DEEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQepmvslNPlhnlEKQLyeVLSL----------HRGMRREAARAEILTCLDRVGIRQAAKRladYPH 155
Cdd:TIGR04520 72 LWEIR-KKVGMVFQ------NP----DNQF--VGATveddvafgleNLGVPREEMRKRVDEALKLVGMEDFRDR---EPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVkKLADTVAVMQNGQC 235
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKI 214
|
...
gi 2551249897 236 VEQ 238
Cdd:TIGR04520 215 VAE 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
306-508 |
1.60e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.24 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQdpnsslnprls 380
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKST----LLKTLAgllkpSSGEILLDGKDLASLSPKEL---ARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 vlqiieeglrvhqptlsaeqreaqvkaVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03214 81 ---------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-258 |
2.98e-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: 133.35 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHA 81
Cdd:COG4987 330 GGPSLELEDVSFRYPGAG--RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-----PQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRDVrgnkIAMIFQEPMV---SLnpLHNLekqlyevlslhRGMRREAARAEILTCLDRVGIRQAAKRLAD------ 152
Cdd:COG4987 403 DEDDLRRR----IAVVPQRPHLfdtTL--RENL-----------RLARPDATDEELWAALERVGLGDWLAALPDgldtwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 --YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVM 230
Cdd:COG4987 466 geGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVL 542
|
250 260
....*....|....*....|....*...
gi 2551249897 231 QNGQCVEQNRAAQLLTapTHPYTKKLLN 258
Cdd:COG4987 543 EDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-248 |
4.02e-33 |
|
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: 129.45 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 39 ALVGESGSGKSvtalSILRL---LPSPPvvypSGDIRFHGESLLHANEQTLRDVRGNKIAMIFQEPmvSLNP----LHNL 111
Cdd:COG4148 29 ALFGPSGSGKT----TLLRAiagLERPD----SGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA--RLFPhlsvRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 112 ekqLYevlslhrGMRREAARAEILTcLDRV----GIrqaAKRLADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
Cdd:COG4148 99 ---LY-------GRKRAPRAERRIS-FDEVvellGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 188 DVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAP 248
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-236 |
4.75e-33 |
|
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: 126.26 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHANE 83
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePS------SGSILLEGTDITKLRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRgNKIAMIFQEPMVsLNPLHNLEKQLYEVLSLHRGMRR------EAARAEILTCLDRVGIRQAAKRLADyphQL 157
Cdd:TIGR02315 72 KKLRKLR-RRIGMIFQHYNL-IERLTVLENVLHGRLGYKPTWRSllgrfsEEDKERALSALERVGLADKAYQRAD---QL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-238 |
7.18e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.67 E-value: 7.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlh 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-----AGTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 aNEQTLRDVRgNKIAMIFQEP-------MVSLNPLHNLEKQlyevlslhrGMRREAARAEILTCLDRVGIRQAAKRladY 153
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPdnqfvgaTVQDDVAFGLENI---------GVPREEMVERVDQALRQVGMEDFLNR---E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQNG 233
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
....*
gi 2551249897 234 QCVEQ 238
Cdd:PRK13635 217 EILEE 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-234 |
7.54e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.54 E-value: 7.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQT 85
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKS-TLLRALADLDPPT----SGEIYLDGKPLSAMPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRdvrgNKIAMIFQEP-MVSLNPLHNLEkqlyEVLSL-HRGMRREAARAEiltcLDRVGIrqaAKRLADYP-HQLSGGER 162
Cdd:COG4619 72 WR----RQVAYVPQEPaLWGGTVRDNLP----FPFQLrERKFDRERALEL----LERLGL---PPDILDKPvERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
306-518 |
8.33e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.51 E-value: 8.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRL-----ITSQGSIVFDGLAL---HTLNRRQLLPVRHRIQVVFQDPNssLNP 377
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSS----LLRVlnlleTPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQYN--LWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLQ-IIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:COG4161 96 HLTVMEnLIEAPCKVLG--LSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 457 DRTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHvFNAPQ 518
Cdd:COG4161 173 DPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASH-FTQPQ 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-185 |
8.34e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 122.37 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHANEQTLRdvrgNKIAMIFQEPmvS 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-----PTEGTILLDGQDLTDDERKSLR----KEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 105 LNPLHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIRQAAKRLADY-PHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPVGErPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 2551249897 184 TT 185
Cdd:pfam00005 149 TA 150
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
306-513 |
9.14e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 9.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLpvRHRIQVVFQDPNssLNPRLS 380
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKST----LMKILSgvyqpDSGEILLDGEPVRFRSPRDAQ--AAGIAIIHQELN--LVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQII------EEGLRVHQptlSAEQREAQvkAVMAEVGL--DSETRHRypaEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:COG1129 96 VAENIflgrepRRGGLIDW---RAMRRRAR--ELLARLGLdiDPDTPVG---DLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:COG1129 168 TASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
306-503 |
1.31e-32 |
|
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: 121.97 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQdpnsslnprlsvlqi 384
Cdd:cd00267 19 SLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEEL---RRRIGYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 ieeglrvhqptlsaeqreaqvkavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 2551249897 465 LTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:cd00267 120 LELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
306-527 |
1.50e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 125.23 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpVRHRiQVVFQdpNSSLNPRLS 380
Cdd:COG4559 21 SLTLRPGELTAIIGPNGAGKST----LLKLLTgeltpSSGEVRLNGRPLAAWSPWEL--ARRR-AVLPQ--HSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPtlSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALI-------LKPSLIILDEPT 453
Cdd:COG4559 92 VEEVVALGRAPHGS--SAAQDRQIVREALALVGLA-HLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 454 SSLDRTVQAQILTLLKSLQEKhRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGqcehvfnAPQQAYTRQLLA 527
Cdd:COG4559 169 SALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG-------TPEEVLTDELLE 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
306-527 |
1.79e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.08 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTL----------NRRQLLPVRHRIQVVFQD 370
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKST----FLRCINflekpSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 371 PNssLNPRLSVLQ-IIEEGLRVhqptLSAEQREAQVKAV--MAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:PRK10619 101 FN--LWSHMTVLEnVMEAPIQV----LGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 448 ILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
306-506 |
2.35e-32 |
|
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: 123.62 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHR-IQVVFQdpNSSLNPRL 379
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKST----LLHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIYQ--FHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQiieeglRVHQPTLSAEQ--REAQVKA--VMAEVGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:TIGR02211 99 TALE------NVAMPLLIGKKsvKEAKERAyeMLEKVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 456 LDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALcHQVIVLRQGEVVE 506
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
306-518 |
2.43e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-------TSQGSIV---FDgLALHTlNRRQLLPVRHRIQVVFQDPNssL 375
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSS----LLRVLnllemprSGTLNIAgnhFD-FSKTP-SDKAIRELRRNVGMVFQQYN--L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 NPRLSVLQ-IIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK11124 94 WPHLTVQQnLIEAPCRVLG--LSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHvFNAPQ 518
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-234 |
3.69e-32 |
|
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: 121.34 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHANEQT 85
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-----PTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRdvrgNKIAMIFQEPMV---SLnpLHNLekqlyevlslhrgmrreaaraeiltcldrvgirqaakrladyphqLSGGER 162
Cdd:cd03228 74 LR----KNIAYVPQDPFLfsgTI--RENI---------------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQ 234
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
306-526 |
4.47e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.28 E-value: 4.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTlNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKST----LLRCINkleeiTSGDLIVDGLKVND-PKVDERLIRQEAGMVFQQFY--LFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGlRVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK09493 94 ALENVMFG-PLRVRGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 461 QAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK09493 172 RHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
306-518 |
7.50e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.14 E-value: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLaLLRLITSQGSIVFDGLalhTLNRRQLLPVRHRIQVVFQDPNSSLnprls 380
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTiskliNGL-LLPDDNPNSKITVDGI---TLTAKTVWDIREKVGIVFQNPDNQF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEE----GLRVHQptLSAEQREAQVKAVMAEVGL----DSEtrhryPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK13640 98 VGATVGDdvafGLENRA--VPRPEMIKIVRDVLADVGMldyiDSE-----PANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
306-508 |
7.59e-32 |
|
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: 121.98 E-value: 7.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGlalhtlNRRQLLPVRHR-IQVVFQdpNSSLNPRL 379
Cdd:cd03301 20 NLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGG------RDVTDLPPKDRdIAMVFQ--NYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:cd03301 88 TVYDNIAFGLKLRK--VPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03301 165 LRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-255 |
1.11e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL---LHANEQTLRDVRGnKIAMIFQE 100
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPD----SGQLNIAGHQFdfsQKPSEKAIRLLRQ-KVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 ----PmvSLNPLHNLEKQLYEVLslhrGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPE 176
Cdd:COG4161 91 ynlwP--HLTVMENLIEAPCKVL----GLSKEQAREKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 177 LLIADEPTTALDVSVQAQILQLLRELQHelnMGL--LFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLltapTHPYTK 254
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQ---TGItqVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF----TQPQTE 234
|
.
gi 2551249897 255 K 255
Cdd:COG4161 235 A 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-258 |
1.15e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.55 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPV-VYPSGDIRFHGESLLHANEQTL 86
Cdd:PRK11264 6 VKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPEAgTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 87 RDVRgNKIAMIFQEpmVSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIrqAAKRLAdYPHQLSGGERQRVM 166
Cdd:PRK11264 81 RQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL--AGKETS-YPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLT 246
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
250
....*....|..
gi 2551249897 247 APTHPYTKKLLN 258
Cdd:PRK11264 234 DPQQPRTRQFLE 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
306-526 |
1.30e-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: 122.06 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalhtlNRRQLLPVRHR-IQVVFQdpNSSLNPRL 379
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTT----LLRLIAglerpDSGTILFGG------EDATDVPVQERnVGFVFQ--HYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVH--QPTLSAEQREAQVKAVMAEVGLDSETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03296 90 TVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 458 RTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
306-504 |
1.30e-31 |
|
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: 121.36 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDpnSSLNPRLSVLQI 384
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQptlsAEQREAQ--VKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:cd03292 99 VAFALEVTG----VPPREIRkrVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2551249897 463 QILTLLKSLQEkhRLAYIFIS-HDLHVVRALCHQVIVLRQGEV 504
Cdd:cd03292 174 EIMNLLKKINK--AGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-254 |
1.40e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 122.04 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL---LHANEQTLRDVRgNKIAMIFQE---- 100
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPR----SGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 PmvSLNPLHNLEKQLYEVLslhrGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK11124 95 P--HLTVQQNLIEAPCRVL----GLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 181 DEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAaqllTAPTHPYTK 254
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQPQTE 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
306-526 |
1.52e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.19 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpVRHRiQVVFQdpNSSLNPRLS 380
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKST----LLRALSgelspDSGEVRLNGRPLADWSPAEL--ARRR-AVLPQ--HSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALI------LKPSLIILDEPTS 454
Cdd:PRK13548 93 VEEVVAMGRAPH--GLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGqcehvfnAPQQAYTRQLL 526
Cdd:PRK13548 170 ALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG-------TPAEVLTPETL 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-245 |
2.46e-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: 127.57 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyP-SGDIRFHGESLLH 80
Cdd:COG4988 333 GPPSIELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP------PySGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRdvrgNKIAMIFQEPMVslnplhnLEKQLYEVLSLHRgmrREAARAEILTCLDRVGIRQAAKRLA---DYP--- 154
Cdd:COG4988 404 LDPASWR----RQIAWVPQNPYL-------FAGTIRENLRLGR---PDASDEELEAALEAAGLDEFVAALPdglDTPlge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 --HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVkKLADTVAVMQN 232
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT--VILITHRLALL-AQADRILVLDD 546
|
250
....*....|...
gi 2551249897 233 GQCVEQNRAAQLL 245
Cdd:COG4988 547 GRIVEQGTHEELL 559
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-234 |
2.51e-31 |
|
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: 118.50 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQTLR 87
Cdd:cd00267 2 IENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 dvrgNKIAMIFQepmvslnplhnlekqlyevlslhrgmrreaaraeiltcldrvgirqaakrladyphqLSGGERQRVMI 167
Cdd:cd00267 73 ----RRIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
306-502 |
3.60e-31 |
|
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: 120.62 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFD----GLALHTLNRRQLLPVR-HRIQVVFQdpnsSL 375
Cdd:COG4778 31 SFSVAAGECVALTGPSGAGKST----LLKCIygnylPDSGSILVRhdggWVDLAQASPREILALRrRTIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 N--PRLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:COG4778 103 RviPRVSALDVVAEPLLERG--VDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 454 SSLDRTVQAQILTLLKSLqeKHR-LAYIFISHDLHVVRALCHQVIVLRQG 502
Cdd:COG4778 181 ASLDAANRAVVVELIEEA--KARgTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
306-505 |
3.74e-31 |
|
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: 118.30 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLpvRHRIQVVFQdpnsslnprls 380
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKST----LMKILSglykpDSGEILVDGKEVSFASPRDAR--RAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 vlqiieeglrvhqptlsaeqreaqvkavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03216 83 ---------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 461 QAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:cd03216 118 VERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
306-519 |
3.91e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLalhTLNRRQLLPVRHRIQVVFQDPNSSLnprlsVLQI 384
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGM---VLSEETVWDVRRQVGMVFQNPDNQF-----VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEE----GLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK13635 99 VQDdvafGLENIG--VPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEVVEQGQCEHVFNAPQQ 519
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-526 |
4.30e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 122.99 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAFPIRKGILKrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLITSQGSIV--------FD 345
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVK-------AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTadrmrfddID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 346 GLALHTLNRRQLlpVRHRIQVVFQDPNSSLNPRLSV-LQIIEE----------GLRVHQptlsaeqREAQVKAVMAEVGL 414
Cdd:PRK15093 75 LLRLSPRERRKL--VGHNVSMIFQEPQSCLDPSERVgRQLMQNipgwtykgrwWQRFGW-------RKRRAIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 415 DS--ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRAL 492
Cdd:PRK15093 146 KDhkDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
250 260 270
....*....|....*....|....*....|....
gi 2551249897 493 CHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-257 |
4.41e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.58 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 23 TVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLL--HANEQTLRDVRGnkiaMIFQE 100
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEI-TSGDLIVDGLKVNdpKVDERLIRQEAG----MVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 pmVSLNP-LHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK09493 86 --FYLFPhLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 180 ADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPTHPYTKKLL 257
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
306-508 |
4.58e-31 |
|
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: 120.41 E-value: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLnrrQLLPVRHRIQVVFQDpnsslnprlS 380
Cdd:cd03253 21 SFTIPAGKKVAIVGPSGSGKST----ILRLLfrfydVSSGSILIDGQDIREV---TLDSLRRAIGVVPQD---------T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VL--QIIEEGLRVHQPTLSAEQREAQVKA----------------VMAEVGLdsetrhrypaEFSGGQRQRIAIARALIL 442
Cdd:cd03253 85 VLfnDTIGYNIRYGRPDATDEEVIEAAKAaqihdkimrfpdgydtIVGERGL----------KLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 443 KPSLIILDEPTSSLDRTVQAQILTLLKSLQeKHRLAyIFISHDLHVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTT-IVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-521 |
5.67e-31 |
|
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: 122.60 E-value: 5.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 317 LVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALhtlnrRQLLPVRHRIQVVFQdpNSSLNPRLSVLQIIEEGLRV 391
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLAgfeqpDSGSIMLDGEDV-----TNVPPHLRHINMVFQ--SYALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 392 HQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSL 471
Cdd:TIGR01187 70 RK--VPRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 472 QEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAY 521
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
306-508 |
6.65e-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: 6.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprlsv 381
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILLDGVDIRDLNLRWL---RSQIGLVSQEPvlfDGT------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 lqiIEEGLRVHQPTLSAEQREAQVKAVMAEV-------GLDSETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03249 93 ---IAENIRYGKPDATDEEVEEAAKKANIHDfimslpdGYDTLVGERG-SQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 455 SLDRTVQAQIltllkslQE------KHRLAyIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03249 169 ALDAESEKLV-------QEaldramKGRTT-IVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
306-517 |
1.06e-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: 122.53 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPV-RHRIQVVFQDpnSSLNPRL 379
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTT----LIRLIAgltrpDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQPtlsaEQREAQVKAVMAEVGLDSETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:TIGR02142 91 SVRGNLRYGMKRARP----SERRISFERVIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-245 |
2.52e-30 |
|
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: 118.42 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLLHAN 82
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKT-TLLRMLagLLKPD------SGSILIDGEDVRKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRdvrgnKIAMIFQEPMvslnplhnlekqLYEVLSLH---------RGMRREAARAEILTCLDRVGIRQAAKRLAdy 153
Cdd:COG4555 70 REARR-----QIGVLPDERG------------LYDRLTVReniryfaelYGLFDEELKKRIEELIELLGLEEFLDRRV-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 pHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:COG4555 131 -GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKG 208
|
250
....*....|..
gi 2551249897 234 QCVEQNRAAQLL 245
Cdd:COG4555 209 KVVAQGSLDELR 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
306-508 |
2.59e-30 |
|
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: 117.98 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPN-------SSLNP 377
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDL---RSRISIIPQDPVlfsgtirSNLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLS-----VLQIIEeglrvhqptlsaeqrEAQVKAVMAEV--GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:cd03244 101 FGEysdeeLWQALE---------------RVGLKEFVESLpgGLDTVVEEG-GENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 451 EPTSSLDRTVQAQILTLLKSlQEKHRlAYIFISHDLHVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03244 165 EATASVDPETDALIQKTIRE-AFKDC-TVLTIAHRLDTI-IDSDRILVLDKGRVVEFD 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-504 |
3.06e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 124.01 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVVNTLSlrvdAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANE 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLH----AGEVHALLGGNGAGKS-TLMKIIAGIVPPD----SGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVrgnKIAMIFQEPMVSLNpLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADyphqlsggeRQ 163
Cdd:PRK15439 81 AKAHQL---GIYLVPQEPLLFPN-LSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVAD---------RQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVeqnraaq 243
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIA------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 244 lLTAPTHPYTKKLLNS--EPSGDPVPLPVGQAPLLEVEKLRVAFPIRKGILKRVVDHNVVVNDVSFSLRPGETLGLVGES 321
Cdd:PRK15439 220 -LSGKTADLSTDDIIQaiTPAAREKSLSASQKLWLELPGNRRQQAAGAPVLTVEDLTGEGFRNISLEVRAGEILGLAGVV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 322 GSGKSTTGLAL--LRLITSqGSIVFDGL---ALHTLNRRQL----LPVRHRIQVVFQDPNSSLNPrlsvlqiieEGLRVH 392
Cdd:PRK15439 299 GAGRTELAETLygLRPARG-GRIMLNGKeinALSTAQRLARglvyLPEDRQSSGLYLDAPLAWNV---------CALTHN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 393 QPTLSaeQREAQVKAVM----AEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLL 468
Cdd:PRK15439 369 RRGFW--IKPARENAVLeryrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 2551249897 469 KSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:PRK15439 447 RSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
306-528 |
1.17e-29 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 116.44 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLalhtlNRRQLLPVRHRIQVVFQdpNSSLNPRLS 380
Cdd:TIGR00968 20 NLEVPTGSLVALLGPSGSGKST----LLRIIAgleqpDSGRIRLNGQ-----DATRVHARDRKIGFVFQ--HYALFKHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPTlsAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:TIGR00968 89 VRDNIAFGLEIRKHP--KAKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLAL 528
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGE 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
306-508 |
1.26e-29 |
|
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: 115.93 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGLALHtlnrRQLLPVRHRIQVVFQdpNSSLNPRLS 380
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDGFDVV----KEPAEARRRLGFVSD--STGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03266 95 ARENLEYFAGLY--GLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03266 172 TRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
306-505 |
1.28e-29 |
|
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: 115.43 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALHTLNRRQllpvrhRIQVVFQDPNSSLNpRLSVlqi 384
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERRK------SIGYVMQDVDYQLF-TDSV--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 iEEGLRVHQPTLSAEQreAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:cd03226 90 -REELLLGLKELDAGN--EQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2551249897 465 LTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:cd03226 166 GELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
306-526 |
1.35e-29 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 118.27 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLI------TSqGSIVFDGLALHTLNRRQLlpvRHRIQVVFQdpNSSLNPRL 379
Cdd:COG1125 22 SLTIPAGEFTVLVGPSGCGKTTT----LRMInrliepTS-GRILIDGEDIRDLDPVEL---RRRIGYVIQ--QIGLFPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEeglRVhqPTL---SAEQREAQVKAVMAEVGLDSET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:COG1125 92 TVAENIA---TV--PRLlgwDKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 456 LDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:COG1125 167 LDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-234 |
1.43e-29 |
|
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: 115.99 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTqPLLAIENLSVGFR---QQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRL-----LPSppvvypSGDIR 72
Cdd:COG4778 1 MT-TLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCiygnyLPD------SGSIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 73 FHGES----LLHANEQTLRDVRGNKIAMIFQ----EPMVS-----LNPLhnlekqlyevlsLHRGMRREAARAEILTCLD 139
Cdd:COG4778 70 VRHDGgwvdLAQASPREILALRRRTIGYVSQflrvIPRVSaldvvAEPL------------LERGVDREEARARARELLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 140 RVGIRQaakRLAD-YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLS 218
Cdd:COG4778 138 RLNLPE---RLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEE 213
|
250
....*....|....*.
gi 2551249897 219 IVKKLADTVAVMQNGQ 234
Cdd:COG4778 214 VREAVADRVVDVTPFS 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
306-526 |
1.69e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.14 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLLPVRHR-IQVVFQdpNSSLNPRLSVLQ 383
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQ--SFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 384 IIEEGLRVhqPTLSAEQREAQVKAVMAEVGLDSETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQ 463
Cdd:PRK10070 126 NTAFGMEL--AGINAEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 464 ILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
306-514 |
2.08e-29 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 115.79 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprlsv 381
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDISRKSL---RSMIGVVLQDTflfSGT------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 lqiIEEGLRVHQPTLSAEQREAQVKAVMA-------EVGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03254 93 ---IMENIRLGRPNATDEEVIEAAKEAGAhdfimklPNGYDTVLGEN-GGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 455 SLD----RTVQAQILTLLKSlqekhRLAYIfISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:cd03254 169 NIDteteKLIQEALEKLMKG-----RTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
306-504 |
2.11e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.14 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLI-----TSQGSIVFDGlalHTLNRRQLLPVRHRIQVVFQDPNSSLnprls 380
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTT----VRLIdglleAESGQIIIDG---DLLTEENVWDIRHKIGMVFQNPDNQF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEE----GLRvhQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK13650 95 VGATVEDdvafGLE--NKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEV 504
Cdd:PRK13650 172 DPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
306-485 |
2.23e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.89 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGlALLRLITSQGSIVFDGLALHTLNrrqllPVRHRIQVVFQDPnsSLNPRLS 380
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTllaaiAG-TLSPAFSASGEVLLNGRRLTALP-----AEQRRIGILFQDD--LLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRvhqPTLSAEQREAQVKAVMAEVGLDSeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG4136 93 VGENLAFALP---PTIGRAQRRARVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....*
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHD 485
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
306-501 |
2.38e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.88 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLnrrqllPVRHRIQVVFQDPNSSLNPRLS 380
Cdd:COG4133 22 SFTLAAGEALALTGPNGSGKTT----LLRILAgllppSAGEVLWNGEPIRDA------REDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLqiieEGLRVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG4133 92 VR----ENLRFWAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2551249897 461 QAQILTLLKSLQEKHRLAyIFISHDLhvVRALCHQVIVLRQ 501
Cdd:COG4133 167 VALLAELIAAHLARGGAV-LLTTHQP--LELAAARVLDLGD 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-248 |
2.65e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 115.61 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSV---GFrqqetvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLLH 80
Cdd:cd03219 1 LEVRGLTKrfgGL-------VALDDVSFSVRPGEIHGLIGPNGAGKT-TLFNLIsgFLRPT------SGSVLFDGEDITG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQtLRDVRGnkIAMIFQEPMV--SLNPLHNLE-----KQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADy 153
Cdd:cd03219 67 LPPH-EIARLG--IGRTFQIPRLfpELTVLENVMvaaqaRTGSGLLLARARREEREARERAEELLERVGLADLADRPAG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:cd03219 143 --ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
250
....*....|....*
gi 2551249897 234 QCVEQNRAAQLLTAP 248
Cdd:cd03219 220 RVIAEGTPDEVRNNP 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-253 |
3.65e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.64 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVrtvvNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH 80
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKAL----NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLrDVRgNKIAMIFQEPmvslNPLhnlEKQLYE--VLSLH-RGMRREAARAEIL-TCLDRVGIRQAAK-RLADYPH 155
Cdd:PRK14239 77 PRTDTV-DLR-KEIGMVFQQP----NPF---PMSIYEnvVYGLRlKGIKDKQVLDEAVeKSLKGASIWDEVKdRLHDSAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMglLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|....*...
gi 2551249897 236 VEQNRAAQLLTAPTHPYT 253
Cdd:PRK14239 226 IEYNDTKQMFMNPKHKET 243
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-245 |
4.92e-29 |
|
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: 114.63 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 9 ENLSVGFrqqETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHANE 83
Cdd:cd03253 4 ENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLfrfydVS------SGSILIDGQDIREVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRdvrgNKIAMIFQEpMVSLNP--LHNLEkqlYEVLSLHRGMRREAARA-----EILTCLD----RVGIRQAakrlad 152
Cdd:cd03253 71 DSLR----RAIGVVPQD-TVLFNDtiGYNIR---YGRPDATDEEVIEAAKAaqihdKIMRFPDgydtIVGERGL------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQN 232
Cdd:cd03253 137 ---KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKD 210
|
250
....*....|...
gi 2551249897 233 GQCVEQNRAAQLL 245
Cdd:cd03253 211 GRIVERGTHEELL 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
306-508 |
6.46e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 120.45 E-value: 6.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTgLALL-RLITSQ-GSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprls 380
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTL-INLLqRVFDPQsGRILIDGTDIRTVTRASL---RRNIAVVFQDAglfNRS------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 vlqiIEEGLRVHQPTLS-AEQREAQVKAVMAEV------GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK13657 425 ----IEDNIRVGRPDATdEEMRAAAERAQAHDFierkpdGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 454 SSLDRTVQAQILTLLKSLQeKHRLAYIfISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:PRK13657 500 SALDVETEAKVKAALDELM-KGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-254 |
6.85e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.13 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSIL-RLLPSPPVVYPSGDIRFHGESLLh 80
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDI----NLDIPENKVTALIGPSGCGKS-TLLRCLnRMNDLIPGARVEGEILLDGEDIY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRgNKIAMIFQEPmvslNPLhnlEKQLYE-V---LSLHrGMRREAARAEIL-TCLdrvgiRQAA-----K-R 149
Cdd:COG1117 82 DPDVDVVELR-RRVGMVFQKP----NPF---PKSIYDnVaygLRLH-GIKSKSELDEIVeESL-----RKAAlwdevKdR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 150 LADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVqAQILQLLRELQHELNMglLFITHNLSIVKKLADTVA 228
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKDYTI--VIVTHNMQQAARVSDYTA 224
|
250 260
....*....|....*....|....*.
gi 2551249897 229 VMQNGQCVEQNRAAQLLTAPTHPYTK 254
Cdd:COG1117 225 FFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-245 |
8.30e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.27 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLlhaNEQTLRDVRgNKIAMIFQ 99
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLR---FYDptSGRILIDGVDI---RDLTLESLR-RQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 100 EPMV-SLNPLHNLekqlyevlslhRGMRREAARAEILTCLDRVGIRQAAKRLAD-YPHQ-------LSGGERQRVMIAMA 170
Cdd:COG1132 422 DTFLfSGTIRENI-----------RYGRPDATDEEVEEAAKAAQAHEFIEALPDgYDTVvgergvnLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQLL 245
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-245 |
1.05e-28 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 113.79 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLlhaNEQTLRDVRgNKIAMIFQEPM 102
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPT------SGEILLDGVDI---RDLNLRWLR-SQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 VSLNPLhnLEKQLYEVLSLHRGMRREAARA----EILTCL-----DRVGIRQAakrladyphQLSGGERQRVMIAMALLT 173
Cdd:cd03249 88 LFDGTI--AENIRYGKPDATDEEVEEAAKKanihDFIMSLpdgydTLVGERGS---------QLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 174 RPELLIADEPTTALDVSVQAQILQLLRELQheLNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQLL 245
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
256-508 |
1.11e-28 |
|
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: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 256 LLNSEPSgdpVPLPVGQAP-----LLEVEKLRVAFPIR--KGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTT 328
Cdd:TIGR00958 457 YLDRKPN---IPLTGTLAPlnlegLIEFQDVSFSYPNRpdVPVLK----------GLTFTLHPGEVVALVGPSGSGKSTV 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 329 GLALLRLIT-SQGSIVFDGLALHTLNRRQLlpvrHR-IQVVFQDPnssLNPRLSVLQIIEEGLRvhqptlsaEQREAQVK 406
Cdd:TIGR00958 524 AALLQNLYQpTGGQVLLDGVPLVQYDHHYL----HRqVALVGQEP---VLFSGSVRENIAYGLT--------DTPDEEIM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 407 AVMAEVGLD---SETRHRYPAE-------FSGGQRQRIAIARALILKPSLIILDEPTSSLDrtvqAQILTLLKSLQEKHR 476
Cdd:TIGR00958 589 AAAKAANAHdfiMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRAS 664
|
250 260 270
....*....|....*....|....*....|..
gi 2551249897 477 LAYIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR00958 665 RTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-234 |
1.38e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.37 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPT----SGDVIFNGQPMSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQ--EPMVSLNPLHNLEKQLyevlsLHRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLS 158
Cdd:PRK11629 76 LSSAAKAELRNQKLGFIYQfhHLLPDFTALENVAMPL-----LIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAvMQNGQ 234
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-245 |
1.44e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 112.91 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvVYpSGDIRFHGESLLHAN-EQ 84
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PR-SGSIRFDGRDITGLPpHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRdvRGnkIAMIFQEPMV--SLNPLHNLEkqlyevLSLHRGMRREAAR--AEILTCLDRvgIRQAAKRLAdypHQLSGG 160
Cdd:cd03224 72 RAR--AG--IGYVPEGRRIfpELTVEENLL------LGAYARRRAKRKArlERVYELFPR--LKERRKQLA---GTLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNR 240
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
....*
gi 2551249897 241 AAQLL 245
Cdd:cd03224 216 AAELL 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-216 |
1.55e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 113.34 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHA 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILAGLDDGS----SGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRDVRGNKIAMIFQEPMV--SLNPLHNLEkqlyeVLSLHRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSG 159
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQSFMLipTLNALENVE-----LPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHN 216
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-244 |
2.23e-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: 112.46 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLhaneQTLR 87
Cdd:cd03265 3 VENLVKKYGDFEAVRGV----SFRVRRGEIFGLLGPNGAGKT-TTIKMLTTLLKPT----SGRATVAGHDVV----REPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQEPMV--SLNPLHNLEKQ--LYevlslhrGMRREAARAEILTCLDRVGIRQAAKRLADYphqLSGGERQ 163
Cdd:cd03265 70 EVR-RRIGIVFQDLSVddELTGWENLYIHarLY-------GVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQ 243
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
.
gi 2551249897 244 L 244
Cdd:cd03265 219 L 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-506 |
2.28e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 118.35 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFrqqeTVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlh 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPT----KGTITINNINY-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 aNEQTLRDVRGNKIAMIFQEPMV--SLNPLHNL------EKQLYEV-LSLHRGMRReaaRAEILtcLDRVGIRqaaKRLA 151
Cdd:PRK09700 70 -NKLDHKLAAQLGIGIIYQELSVidELTVLENLyigrhlTKKVCGVnIIDWREMRV---RAAMM--LLRVGLK---VDLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQ 231
Cdd:PRK09700 141 EKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 232 NG--------QCVEQNRAAQLLTApthpytKKLLNSEPSGDPVPLPVGQAPLLEVEKLrvafpIRKGILKrvvdhnvvVN 303
Cdd:PRK09700 220 DGssvcsgmvSDVSNDDIVRLMVG------RELQNRFNAMKENVSNLAHETVFEVRNV-----TSRDRKK--------VR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 304 DVSFSLRPGETLGLVGESGSGKSTTGLALLRL-ITSQGSIVFDGLALHTlnRRQLLPVRHRIQVVFQD-------PNSSL 375
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVdKRAGGEIRLNGKDISP--RSPLDAVKKGMAYITESrrdngffPNFSI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 NPRLSVLQIIEEGLRVHQPTLSAEQREAQV-KAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK09700 359 AQNMAISRSLKDGGYKGAMGLFHEVDEQRTaENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVE 506
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-264 |
2.52e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.04 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLhaNE 83
Cdd:PRK14271 20 PAMAAVNLTLGFAG----KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIF--NY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRgNKIAMIFQEPmvSLNPLHNLEKQLYEVLSlHRGMRREAARAEILTCLDRVGIRQAAK-RLADYPHQLSGGER 162
Cdd:PRK14271 94 RDVLEFR-RRVGMLFQRP--NPFPMSIMDNVLAGVRA-HKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAA 242
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
250 260
....*....|....*....|..
gi 2551249897 243 QLLTAPTHPYTKKLLnSEPSGD 264
Cdd:PRK14271 248 QLFSSPKHAETARYV-AGLSGD 268
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-252 |
2.68e-28 |
|
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: 115.59 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 27 TLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHANEQTLRDVRGNKIAMIFQEpmVSLN 106
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKT-TLIRLIAGLTRPDE----GEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 107 PLHNLEKQLYEVLSLHRGMRREAARAEILTCLdrvGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 187 LDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPTHPY 252
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-238 |
2.74e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 115.57 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGF-RQQetvrtVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGE--SLLHAn 82
Cdd:PRK10851 3 IEIANIKKSFgRTQ-----VLNDISLDIPSGQMVALLGPSGSGKT-TLLRIIAGLEH----QTSGHIRFHGTdvSRLHA- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 eqtlrdvRGNKIAMIFQEPMV--SLNPLHNLEKQLyEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGG 160
Cdd:PRK10851 72 -------RDRKVGFVFQHYALfrHMTVFDNIAFGL-TVLPRRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGqCVEQ 238
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
312-508 |
2.82e-28 |
|
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: 111.82 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTtglaLLRLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNssLNPRLSVLQIIEEGlRV 391
Cdd:cd03298 24 GEITAIVGPSGSGKST----LLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENN--LFAHLTVEQNVGLG-LS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 392 HQPTLSAEQREAqVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSL 471
Cdd:cd03298 97 PGLKLTAEDRQA-IEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 2551249897 472 QEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-237 |
3.08e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 112.43 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvrtvVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyP-SGDIRFHGESLLHANEQ 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK------PdSGKILLNGKDITNLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TlRDvrgnkIAMIFQEpmVSLNPLHNLEKQLYEVLSLHRGMRREAARaEILTCLDRVGIRQAAKRladYPHQLSGGERQR 164
Cdd:cd03299 70 K-RD-----ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGIDHLLNR---KPETLSGGEQQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
306-515 |
3.55e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtgLALLRL---ITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSSLnprlsVL 382
Cdd:PRK13648 29 SFNIPKGQWTSIVGHNGSGKST--IAKLMIgieKVKSGEIFYNNQAITDDNFEKL---RKHIGIVFQNPDNQF-----VG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEE----GLRVHqpTLSAEQREAQVKAVMAEVGL----DSEtrhryPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK13648 99 SIVKYdvafGLENH--AVPYDEMHRRVSEALKQVDMleraDYE-----PNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHRLAYIFISHDLhvVRAL-CHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDL--SEAMeADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
306-496 |
1.16e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 111.06 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLNRRQLLPVRHRiQVVFQDPNSSLNPRLS 380
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKST----LLHLLggldtPTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQiieeglRVHQPTL--SAEQREAQVKA--VMAEVGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK11629 104 ALE------NVAMPLLigKKKPAEINSRAleMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQV 496
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-238 |
1.18e-27 |
|
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: 110.79 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLH 80
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIagfetPT------SGEILLDGKDITN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 --ANEQtlrdvrgnKIAMIFQEpmVSLNPLHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLS 158
Cdd:cd03300 67 lpPHKR--------PVNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQcVEQ 238
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK-IQQ 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-238 |
1.94e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 110.51 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 23 TVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGEsllhanEQTLRDVRGNKIAMIFQ--- 99
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKT-TLLRLIAGLERPD----SGTILFGGE------DATDVPVQERNVGFVFQhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 100 ---EPMVSLNPLHNLEKQlyevlslHRGMRREAA--RAEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTR 174
Cdd:cd03296 85 lfrHMTVFDNVAFGLRVK-------PRSERPPEAeiRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 175 PELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQcVEQ 238
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQ 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
306-515 |
2.31e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.41 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSIVFDGLALHTLNR-RQLLPVRHRIQVVFQDPNSSLNPRl 379
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTliqniNAL----LKPTTGTVTVDDITITHKTKdKYIRPVRKRIGMVFQFPESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQPTLsaEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:PRK13646 102 TVEREIIFGPKNFKMNL--DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
306-508 |
3.22e-27 |
|
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: 109.63 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnp 377
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKST----LVNLIPrfydvDSGRILIDGHDVRDYTLASL---RRQIGLVSQDVflfNDT--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 rlsvlqiIEEGLRVHQPTLSAEQREAQVKAVMA-------EVGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
Cdd:cd03251 92 -------VAENIAYGRPGATREEVEEAARAANAhefimelPEGYDTVIGER-GVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 451 EPTSSLD----RTVQAQILTLLkslqeKHRLAYIfISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:cd03251 164 EATSALDteseRLVQAALERLM-----KNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
306-508 |
3.38e-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: 115.82 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITS-----QGSIVFDGLALHTLNRRQllpVRHRIQVVFQdpNSSLNPRlS 380
Cdd:TIGR03797 473 SLQIEPGEFVAIVGPSGSGKST----LLRLLLGfetpeSGSVFYDGQDLAGLDVQA---VRRQLGVVLQ--NGRLMSG-S 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVhqpTLSaeqrEAQVKAVMAevGLDSETR------HRYPAE----FSGGQRQRIAIARALILKPSLIILD 450
Cdd:TIGR03797 543 IFENIAGGAPL---TLD----EAWEAARMA--GLAEDIRampmgmHTVISEgggtLSGGQRQRLLIARALVRKPRILLFD 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 451 EPTSSLDRTVQAQILTLLKSLQekhrLAYIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03797 614 EATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-238 |
4.26e-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: 108.52 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQT 85
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 ---LRDVRGNKIAMIFQEPMVSLNPLhnlekqlyevlslhRGMRREAARAEILTCLDRVGIRQAAKRLADyphQLSGGER 162
Cdd:cd03269 72 igyLPEERGLYPKMKVIDQLVYLAQL--------------KGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
306-512 |
4.76e-27 |
|
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: 108.75 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGLALHTlNRRQllpVRHRIQVVFQDpnSSLNPRLS 380
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTT----LKMLTgelrpTSGTAYINGYSIRT-DRKA---ARQSLGYCPQF--DALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03263 92 VREHLRFYARLK--GLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 461 QAQILTLLKSLQEKHrlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEH 512
Cdd:cd03263 169 RRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-518 |
4.88e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.17 E-value: 4.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAFPIRKGILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALhTLN 353
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGI----------NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPI-KYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 354 RRQLLPVRHRIQVVFQDPNSSL-NPRlsVLQIIEEGlrvhqPT---LSAEQREAQVKAVMAEVGLDSETRhRYPAEFSGG 429
Cdd:PRK13639 70 KKSLLEVRKTVGIVFQNPDDQLfAPT--VEEDVAFG-----PLnlgLSKEEVEKRVKEALKAVGMEGFEN-KPPHHLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 430 QRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
....*....
gi 2551249897 510 CEHVFNAPQ 518
Cdd:PRK13639 221 PKEVFSDIE 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
308-514 |
5.65e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.32 E-value: 5.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 308 SLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALhTLNRRQLLPVRHRIQVVFQDPNSSLNPRlSVLQIIE 386
Cdd:PRK13636 28 NIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDPDNQLFSA-SVYQDVS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 387 EGlrVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILT 466
Cdd:PRK13636 106 FG--AVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 467 LLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13636 183 LLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-245 |
8.79e-27 |
|
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: 108.47 E-value: 8.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 12 SVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIRFHGESLlhaNEQTLRDV 89
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPR---FYdvDSGRILIDGHDV---RDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 90 RgNKIAMIFQEPMVSLNPLHnlEKQLYEvlslhrgmRREAARAEIltcldrvgiRQAAKrlADYPHQ------------- 156
Cdd:cd03251 75 R-RQIGLVSQDVFLFNDTVA--ENIAYG--------RPGATREEV---------EEAAR--AANAHEfimelpegydtvi 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVM 230
Cdd:cd03251 133 gergvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVL 209
|
250
....*....|....*
gi 2551249897 231 QNGQCVEQNRAAQLL 245
Cdd:cd03251 210 EDGKIVERGTHEELL 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-504 |
8.99e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 113.56 E-value: 8.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFrqqETVRTVVNTlSLRVDAGQTLALVGESGSGKSvTALSILrllpspPVVYP--SGDIRFHGESLL 79
Cdd:PRK10762 1 MQALLQLKGIDKAF---PGVKALSGA-ALNVYPGRVMALVGENGAGKS-TMMKVL------TGIYTrdAGSILYLGKEVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANEqtlRDVRGNKIAMIFQEpmvsLNPLHNLekQLYEVLSLHR------------GMRREAARaeiltCLDRVGIRQAA 147
Cdd:PRK10762 70 FNGP---KSSQEAGIGIIHQE----LNLIPQL--TIAENIFLGRefvnrfgridwkKMYAEADK-----LLARLNLRFSS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 148 KRLADyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTV 227
Cdd:PRK10762 136 DKLVG---ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 228 AVMQNGQCVEQNRAAQLltapthpyTKKLLnsepsgdpVPLPVGQAplLEVEKLRVAFPIRKGILKRVVDHNVVVNDVSF 307
Cdd:PRK10762 212 TVFRDGQFIAEREVADL--------TEDSL--------IEMMVGRK--LEDQYPRLDKAPGEVRLKVDNLSGPGVNDVSF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 308 SLRPGETLGLVGESGSGKSttglALLRLI-----TSQGSIVFDGLALHTLNRRQLLpvRHRIQVVFQD------------ 370
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRT----ELMKVLygalpRTSGYVTLDGHEVVTRSPQDGL--ANGIVYISEDrkrdglvlgmsv 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 371 -PNSSLNprlSVLQIIEEGLRVhqptlsaeQREAQVKAVMAEVGL---DSETRHRYPAEFSGGQRQRIAIARALILKPSL 446
Cdd:PRK10762 348 kENMSLT---ALRYFSRAGGSL--------KHADEQQAVSDFIRLfniKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 447 IILDEPTSSLDRTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
306-514 |
9.21e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 9.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGL---ALLrlITSQGSIVFDGLalHTLNRRQLLPVRHRIQVVFQDPNSSLnprlsVL 382
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKhmnALL--IPSEGKVYVDGL--DTSDEENLWDIRNKAGMVFQNPDNQI-----VA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEEGLRVHQPTLSAEQRE--AQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEirERVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDL-HVVRAlcHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIF 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
306-516 |
1.59e-26 |
|
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: 108.25 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT------SQGSI-VFDglalHTLNRRQLLPVRHRIQVVFQDPNSSLNPR 378
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKST----LLSLITgdlpptYGNDVrLFG----ERRGGEDVWELRKRIGLVSPALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVLQIIEEGL-----RVHQPTlsAEQREaQVKAVMAEVGLDSETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:COG1119 95 ETVLDVVLSGFfdsigLYREPT--DEQRE-RARELLELLGLAHLADRPF-GTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 454 SSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNA 516
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
306-508 |
1.82e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalHTLNRrqlLPVRHR-IQVVFQdpNSSLNPRL 379
Cdd:PRK09452 34 DLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIMLDG---QDITH---VPAENRhVNTVFQ--SYALFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVhQPTLSAEQREaQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:PRK09452 102 TVFENVAFGLRM-QKTPAAEITP-RVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK09452 179 LRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
306-515 |
2.74e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.15 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSSLnPRLSVLQI 384
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITISKENLKEI---RKKIGIIFQNPDNQF-IGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PRK13632 105 IAFGLENKK--VPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 465 LTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-201 |
3.09e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.02 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLP--SPPVvypSGDIRFHGESLLHA 81
Cdd:COG4133 1 MMLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKT----TLLRILAglLPPS---AGEVLWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRDvrgnkIAMIFQEPMV--SLNPLHNLEkqlyevlsLHRGMR-REAARAEILTCLDRVGIRQAAKRLAdypHQLS 158
Cdd:COG4133 70 REDYRRR-----LAYLGHADGLkpELTVRENLR--------FWAALYgLRADREAIDEALEAVGLAGLADLPV---RQLS 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-238 |
3.39e-26 |
|
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: 106.18 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSVTalsiLRLL-----PSppvvypSGDIRFHGESL--LHANEqtlRDvrgnkI 94
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleePT------SGRIYIGGRDVtdLPPKD---RD-----I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 95 AMIFQEpmVSLNPLHNLEKQLYEVLSLHRGMRREAAR-----AEILtcldrvgirQAAKRLADYPHQLSGGERQRVMIAM 169
Cdd:cd03301 75 AMVFQN--YALYPHMTVYDNIAFGLKLRKVPKDEIDErvrevAELL---------QIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQcVEQ 238
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-249 |
3.71e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.12 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLL 79
Cdd:COG4559 1 MLEAENLSVRLGG----RTLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANEQTLRDVRgnkiAMIFQEpmVSLN-PLHnlekqLYEVLSLHR---GMRREAARAEILTCLDRVGIRQAAKRlaDYPh 155
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFT-----VEEVVALGRaphGSSAAQDRQIVREALALVGLAHLAGR--SYQ- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALL-------TRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVA 228
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRIL 211
|
250 260
....*....|....*....|.
gi 2551249897 229 VMQNGQCVEQNRAAQLLTAPT 249
Cdd:COG4559 212 LLHQGRLVAQGTPEEVLTDEL 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
306-508 |
4.13e-26 |
|
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: 105.91 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALhtlnRRQLLPVRHRIQVVFQDPnsSLNPRLSVLQI 384
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkPTSGRATVAGHDV----VREPREVRRRIGIVFQDL--SVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHqpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:cd03265 94 LYIHARLY--GVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2551249897 465 LTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
308-518 |
4.66e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.80 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 308 SLRPGETLGLVGESGSGKSTtgL-----ALLRLITSQGSIVFDGLALHTLNRrQLLPVRHRIQVVFQDPNSSLNPRlSVL 382
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKST--LlqhlnGLLQPTSGTVTIGERVITAGKKNK-KLKPLRKKVGIVFQFPEHQLFEE-TVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEEGlrvhqPT---LSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:PRK13634 105 KDICFG-----PMnfgVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 460 VQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-238 |
5.66e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 105.38 E-value: 5.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHaNEQTLRdvrgnKIAMIFQEP 101
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKT-TTMKIILGLIKPD----SGEITFDGKSYQK-NIEALR-----RIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 mvSLNPLHNLEKQLYeVLSLHRGMRREaaraEILTCLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:cd03268 82 --GFYPNLTARENLR-LLARLLGIRKK----RIDEVLDVVGLKDSAKKKVK---GFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 182 EPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
306-509 |
5.78e-26 |
|
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: 106.01 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalhtlnRRQLLPVRHRIqVVFQdpNSSLNPRLS 380
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKST----LLNLISglaqpTSGGVILEG-------KQITEPGPDRM-VVFQ--NYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
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 2551249897 3 QPLLAIENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaN 82
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKS-TISKILTGLLKPQ----SGEIKIDGITI---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDVRgNKIAMIFQEP-------MVSLNPLHNLEkqlyevlslHRGMRREAARAEILTCLDRVGIRQAAKRladYPH 155
Cdd:PRK13632 75 KENLKEIR-KKIGIIFQNPdnqfigaTVEDDIAFGLE---------NKKVPPKKMKDIIDDLAKKVGMEDYLDK---EPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVkKLADTVAVMQNGQC 235
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL 220
|
250
....*....|.
gi 2551249897 236 VEQNRAAQLLT 246
Cdd:PRK13632 221 IAQGKPKEILN 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
306-528 |
6.77e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 106.03 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRL-ITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDpNSSLNprlsvlQI 384
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE-NVLFN------RS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYP-------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHDFI-SELPEGYDtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 458 RTVQAQILTLLKSLQeKHRLAyIFISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVFNApqQAYTRQLLAL 528
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTV-IIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE--NGLYAYLYQL 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
306-510 |
1.17e-25 |
|
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: 104.56 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLalhtlNRRQLLPVRHRIQVVFQDPNssLNPRLS 380
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKST----LLNLIAgfiepASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENN--LFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRvhqPTL--SAEQREaQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:TIGR01277 87 VRQNIGLGLH---PGLklNAEQQE-KVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQC 510
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
276-508 |
1.33e-25 |
|
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: 104.82 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 276 LEVEKLRVA---FPIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHT 351
Cdd:cd03224 1 LEVENLNAGygkSQILFGV--------------SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 352 LNRRQLlpVRHRIQVVFQDPNssLNPRLSVlqiiEEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQR 431
Cdd:cd03224 67 LPPHER--ARAGIGYVPEGRR--IFPELTV----EENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 432 QRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKhRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-248 |
1.52e-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: 105.06 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLLHAN- 82
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGV----SLEVEEGEIVALLGRNGAGKTTLLKAISGLLP--PR---SGSIRFDGEDITGLPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRdvRGnkIAMIFQEPMV--SLNPLHNLEkqlyevLSLHRGMRREAARAEILTCLDRVgirqaaKRLADYPHQ---- 156
Cdd:COG0410 73 HRIAR--LG--IGYVPEGRRIfpSLTVEENLL------LGAYARRDRAEVRADLERVYELF------PRLKERRRQragt 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
250
....*....|..
gi 2551249897 237 EQNRAAQLLTAP 248
Cdd:COG0410 216 LEGTAAELLADP 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-255 |
1.64e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVYP----SGDIRFHGESLLHA 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGV----NLEIPDNTITALMGPSGSGKS----TLLRVFNRLIELYPearvSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRdvrgNKIAMIFQEPmvslNPLHNLekQLYEVLSLHRGMRREA-ARAEILT----CLDRVGIRQAAKRLADYPH- 155
Cdd:PRK14247 76 DVIELR----RRVQMVFQIP----NPIPNL--SIFENVALGLKLNRLVkSKKELQErvrwALEKAQLWDEVKDRLDAPAg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElnMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250 260
....*....|....*....|
gi 2551249897 236 VEQNRAAQLLTAPTHPYTKK 255
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTEK 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-249 |
2.28e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESL 78
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALsgelsPD------SGEVRLNGRPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 79 LHANEQTLRDVRgnkiAMIFQEPMVSLnPLhnlekQLYEVLSLHR---GMRREAARAEILTCLDRVGIRQAAKRlaDYPh 155
Cdd:PRK13548 67 ADWSPAELARRR----AVLPQHSSLSF-PF-----TVEEVVAMGRaphGLSRAEDDALVAAALAQVDLAHLAGR--DYP- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMAL--LTRPE----LLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAV 229
Cdd:PRK13548 134 QLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
250 260
....*....|....*....|
gi 2551249897 230 MQNGQCVEQNRAAQLLTAPT 249
Cdd:PRK13548 214 LHQGRLVADGTPAEVLTPET 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
306-508 |
3.48e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 103.04 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGeTLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALhtlnRRQLLPVRHRIQVVFQDPNSSlnPRLS 380
Cdd:cd03264 20 SLTLGPG-MYGLLGPNGAGKTT----LMRILAtltppSSGTIRIDGQDV----LKQPQKLRRRIGYLPQEFGVY--PNFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VlqiiEEGLRvHQPTL---SAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03264 89 V----REFLD-YIAWLkgiPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 458 RTVQAQILTLLKSLQEKHrlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03264 163 PEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-236 |
3.90e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 101.35 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANeqt 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGV----SLSVRRGEVHALLGENGAGKS-TLMKILSGLYKPD----SGEILVDGKEVSFAS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGNKIAMIfqepmvslnplhnlekqlyevlslhrgmrreaaraeiltcldrvgirqaakrladypHQLSGGERQRV 165
Cdd:cd03216 69 PRDARRAGIAMV---------------------------------------------------------YQLSVGERQMV 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-527 |
4.12e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 104.79 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 317 LVGESGSGKSTTGLALLRL------ITSQGSIVFDGLALhtLNRRQLLPVRHRIQVVFQDPNSSlnpRLSVLQIIEEGLR 390
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF---PMSIMDNVLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 391 VHQPTLSAEQReAQVKAVMAEVGLDSETRHRY---PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTL 467
Cdd:PRK14271 127 AHKLVPRKEFR-GVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 468 LKSLQEkhRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLLA 527
Cdd:PRK14271 206 IRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-257 |
4.86e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.15 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 7 AIE--NLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHANEQ 84
Cdd:PRK14267 4 AIEtvNLRVYYGSNHVIKGV----DLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRdVRgNKIAMIFQEPmvslNPLHNLekQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAA------KRLADYPHQLS 158
Cdd:PRK14267 80 PIE-VR-REVGMVFQYP----NPFPHL--TIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
250
....*....|....*....
gi 2551249897 239 NRAAQLLTAPTHPYTKKLL 257
Cdd:PRK14267 230 GPTRKVFENPEHELTEKYV 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
306-524 |
5.17e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.84 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT------SQGSIVFDGLALHTLNrrqLLPVRHRIQVVFQDPNSSlnPRL 379
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMD---VIELRRRVQMVFQIPNPI--PNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPA---EFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK14247 98 SIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 457 DRTVQAQILTLLksLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQ 524
Cdd:PRK14247 178 DPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
306-514 |
5.85e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.40 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITS-QGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSSLnprlsVLQI 384
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGELLTAENVWNL---RRKIGMVFQNPDNQF-----VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTlSAEQREAQVK----AVMAEVGLDSETRHryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK13642 99 VEDDVAFGMEN-QGIPREEMIKrvdeALLAVNMLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
8-276 |
5.98e-25 |
|
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: 106.23 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSppVVYPSGdirFHGESLLHANEQTLR 87
Cdd:TIGR03258 8 IDHLRVAYGA----NTVLDDLSLEIEAGELLALIGKSGCGKT----TLLRAIAG--FVKAAG---LTGRIAIADRDLTHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRGNKIAMIFQEpmVSLNPLHNLEKQLYEVLSLHRGMRREAARaEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMI 167
Cdd:TIGR03258 75 PPHKRGLALLFQN--YALFPHLKVEDNVAFGLRAQKMPKADIAE-RVADALKLVGLGDAAAH---LPAQLSGGMQQRIAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHEL-NMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLT 246
Cdd:TIGR03258 149 ARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYD 228
|
250 260 270
....*....|....*....|....*....|
gi 2551249897 247 APTHPYTKKLLNSEPSGDPVPLPVGQAPLL 276
Cdd:TIGR03258 229 APADGFAAEFLGAANILPAIALGITEAPGL 258
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-246 |
6.77e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.37 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQETvrTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGE 76
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLtrawdPQ------QGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 77 SLLHANEQTLRdvrgNKIAMIFQEPmvslnplHNLEKQLYEVLSLhrgMRREAARAEILTCLDRVGIR---QAAKRL--- 150
Cdd:PRK11160 403 PIADYSEAALR----QAISVVSQRV-------HLFSATLRDNLLL---AAPNASDEALIEVLQQVGLEkllEDDKGLnaw 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 151 -ADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQHELNMGLLFITHNLSIVKKLaDTVAV 229
Cdd:PRK11160 469 lGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA--EHAQNKTVLMITHRLTGLEQF-DRICV 545
|
250
....*....|....*..
gi 2551249897 230 MQNGQCVEQNRAAQLLT 246
Cdd:PRK11160 546 MDNGQIIEQGTHQELLA 562
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-258 |
7.36e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.51 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSILRLL--PSPPVVYPSGD----IRFH 74
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGV----SLQANAGDVISIIGSSGSGKS-TFLRCINFLekPSEGSIVVNGQtinlVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 75 GESLLHANEQTLRDVRgNKIAMIFQEPMV--SLNPLHNLEKQLYEVLslhrGMRREAARAEILTCLDRVGIRQAAKrlAD 152
Cdd:PRK10619 76 DGQLKVADKNQLRLLR-TRLTMVFQHFNLwsHMTVLENVMEAPIQVL----GLSKQEARERAVKYLAKVGIDERAQ--GK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQN 232
Cdd:PRK10619 149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
250 260
....*....|....*....|....*.
gi 2551249897 233 GQCVEQNRAAQLLTAPTHPYTKKLLN 258
Cdd:PRK10619 228 GKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-528 |
8.49e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.69 E-value: 8.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFrqqETVRTVVNtLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHA 81
Cdd:PRK11288 1 SSPYLSFDGIGKTF---PGVKALDD-ISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPD----AGSILIDGQEMRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NeqtLRDVRGNKIAMIFQEpmvslnpLHNL-EKQLYEVLSL----HRG--MRREAARAEILTCLDRVGIR-QAAKRLADy 153
Cdd:PRK11288 72 S---TTAALAAGVAIIYQE-------LHLVpEMTVAENLYLgqlpHKGgiVNRRLLNYEAREQLEHLGVDiDPDTPLKY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 phqLSGGERQRVMIAMALLtRPELLIA-DEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQN 232
Cdd:PRK11288 141 ---LSIGQRQMVEIAKALA-RNARVIAfDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 233 GQCVEqnraaqlltapTHP----YTKKLLNSEPSGDPV-------PLPVGqAPLLEVEKL---RVAFPIrkgilkrvvdh 298
Cdd:PRK11288 216 GRYVA-----------TFDdmaqVDRDQLVQAMVGREIgdiygyrPRPLG-EVRLRLDGLkgpGLREPI----------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 299 nvvvndvSFSLRPGETLGLVGESGSGKSttglALLRLI-----TSQGSIVFDGLALHTLNRRQllPVRHRIQVVFQDPNS 373
Cdd:PRK11288 273 -------SFSVRAGEIVGLFGLVGAGRS----ELMKLLygatrRTAGQVYLDGKPIDIRSPRD--AIRAGIMLCPEDRKA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 374 -SLNPRLSVLQIIEEGLRVHQPTLS--------AEQREAQVKAvmaevgLDSETRHRYPA--EFSGGQRQRIAIARALIL 442
Cdd:PRK11288 340 eGIIPVHSVADNINISARRHHLRAGclinnrweAENADRFIRS------LNIKTPSREQLimNLSGGNQQKAILGRWLSE 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 443 KPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVeqGQCEHvfnapQQAYT 522
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR-----EQATE 485
|
....*.
gi 2551249897 523 RQLLAL 528
Cdd:PRK11288 486 RQALSL 491
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
306-497 |
9.41e-25 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 102.47 E-value: 9.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVF----DGLALHTLNRRQLLPVR-HRIQVVFQdpnsSL 375
Cdd:TIGR02324 28 SLTVNAGECVALSGPSGAGKST----LLKSLyanylPDSGRILVrhegAWVDLAQASPREVLEVRrKTIGYVSQ----FL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 N--PRLSVLQIIEEGLRVhqptLSAEQREAQVKA--VMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:TIGR02324 100 RviPRVSALEVVAEPLLE----RGVPREAARARAreLLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 452 PTSSLDRTVQAQILTLLKSLqeKHR-LAYIFISHDLHVVRALCHQVI 497
Cdd:TIGR02324 176 PTASLDAANRQVVVELIAEA--KARgAALIGIFHDEEVRELVADRVM 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-527 |
1.02e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.01 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQdpnsslNPRLsVLQII 385
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESW---RKHLSWVGQ------NPQL-PHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 EEGLRVHQPTLSAEQ-----REAQVKAVMAEV--GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK11174 440 RDNVLLGNPDASDEQlqqalENAWVSEFLPLLpqGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 459 TVQAQILTLLKslQEKHRLAYIFISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVfnAPQQAYTRQLLA 527
Cdd:PRK11174 519 HSEQLVMQALN--AASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAEL--SQAGGLFATLLA 582
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-238 |
1.03e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.16 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSVTalsiLRLL-----PSppvvypSGDIRFHGesllh 80
Cdd:COG3839 4 LELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagledPT------SGEILIGG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 aneqtlRDV-------RGnkIAMIFQEP-----M-VSLN---PLHNlekqlyevlslhRGMRREAARAEILTCLDRVGIR 144
Cdd:COG3839 65 ------RDVtdlppkdRN--IAMVFQSYalyphMtVYENiafPLKL------------RKVPKAEIDRRVREAAELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 145 QAAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHN----LSiv 220
Cdd:COG3839 125 DLLDR---KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT-- 199
|
250
....*....|....*...
gi 2551249897 221 kkLADTVAVMQNGQcVEQ 238
Cdd:COG3839 200 --LADRIAVMNDGR-IQQ 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-234 |
1.09e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 103.66 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVvNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLlhaNEQTLR 87
Cdd:PRK13650 7 VKNLTFKYKEDQEKYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL-----EAESGQIIIDGDLL---TEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQEP-------MVSLNPLHNLEKQlyevlslhrGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGG 160
Cdd:PRK13650 78 DIR-HKIGMVFQNPdnqfvgaTVEDDVAFGLENK---------GIPHEEMKERVNEALELVGMQDFKER---EPARLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVkKLADTVAVMQNGQ 234
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
254-520 |
1.69e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.14 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 254 KKLLNSEPS-GDPVPLPVGQAPLlEVEKLRVAFPIRKG-ILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtgla 331
Cdd:COG4618 309 NELLAAVPAePERMPLPRPKGRL-SVENLTVVPPGSKRpILRGV----------SFSLEPGEVLGVIGPSGSGKST---- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 332 LLRLIT-----SQGSIVFDGLALHTLNRRQL------LPvrhriQVV-------------FQDPNSSlnprlsvlQIIEe 387
Cdd:COG4618 374 LARLLVgvwppTAGSVRLDGADLSQWDREELgrhigyLP-----QDVelfdgtiaeniarFGDADPE--------KVVA- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 388 glrvhqptlsaeqreAqvkAVMAEV---------GLD---SETRHRypaeFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:COG4618 440 ---------------A---AKLAGVhemilrlpdGYDtriGEGGAR----LSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 456 LDRTVQAQILTLLKSLQEKHRLAyIFISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVFNAPQQA 520
Cdd:COG4618 498 LDDEGEAALAAAIRALKARGATV-VVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-255 |
1.74e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVYPS-----GDIRFHGESLLHANEQTLRdvrgNKIAM 96
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKS----TLLKVLNRLIEIYDSkikvdGKVLYFGKDIFQIDAIKLR----KEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 97 IFQEPmvslNPLHNLE--KQLYEVLSLHRGMRREAARAEILTCLDRVGI-RQAAKRLADYPHQLSGGERQRVMIAMALLT 173
Cdd:PRK14246 95 VFQQP----NPFPHLSiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 174 RPELLIADEPTTALDVSVQAQILQLLRELQHElnMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPTHPYT 253
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
..
gi 2551249897 254 KK 255
Cdd:PRK14246 249 EK 250
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
306-504 |
1.88e-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: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNsslnprL- 379
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKST----LARLILgllrpTSGRVRLDGADISQWDPNEL---GDHVGYLPQDDE------Lf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 --SVLQIIeeglrvhqptlsaeqreaqvkavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03246 89 sgSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 458 RTVQAQILTLLKSLQeKHRLAYIFISHDLHVVrALCHQVIVLRQGEV 504
Cdd:cd03246 129 VEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
306-521 |
1.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLalHTLNRRQLLPVRHRIQVVFQDPNSSLnprlsVLQI 384
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGI--DTGDFSKLQGIRKLVGIVFQNPETQF-----VGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTLSAEQREAQ--VKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRkrVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 463 QILTLLKSLQEKHRlAYIFISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVFNAPQQAY 521
Cdd:PRK13644 174 AVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-238 |
2.10e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.03 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 27 TLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHAneqtlrDVRGNKIAMIFQEPmvslN 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS-TLLNLIAGFETPQ----SGRVLINGVDVTAA------PPADRPVSMLFQEN----N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 107 PLHNLEKQLYEVLSLHRGMR-REAARAEILTCLDRVGIRQAAKRLadyPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKlTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 186 ALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
306-508 |
2.26e-24 |
|
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: 100.75 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLalhtlNRRQLLPVRHRIQVVFQDPnsSLNPRLSVlqi 384
Cdd:cd03268 20 SLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpDSGEITFDGK-----SYQKNIEALRRIGALIEAP--GFYPNLTA--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 iEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:cd03268 90 -RENLRLLA--RLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 465 LTLLKSLQEKHRLayIFI-SHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03268 166 RELILSLRDQGIT--VLIsSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-236 |
2.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.86 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 17 QQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSPPVVYPSGdirfhgesLLHANEQTLRDVRgNKIA 95
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDG--------LDTSDEENLWDIR-NKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 96 MIFQEPM-----------VSLNPlHNLekqlyevlslhrGMRREAARAEILTCLDRVGIrQAAKRLAdyPHQLSGGERQR 164
Cdd:PRK13633 89 MVFQNPDnqivativeedVAFGP-ENL------------GIPPEEIRERVDESLKKVGM-YEYRRHA--PHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQNGQCV 236
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
306-507 |
2.52e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.25 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTlnrrqllPVRHRiQVVFQDpnSSLNPRLS 380
Cdd:COG4525 27 SLTIESGEFVVALGASGCGKTT----LLNLIAgflapSSGEITLDGVPVTG-------PGADR-GVVFQK--DALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:COG4525 93 VLDNVAFGLRLRG--VPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVL--RQGEVVEQ 507
Cdd:COG4525 170 REQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
306-508 |
2.97e-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: 106.75 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQLlpvRHRIQVVFQDpnsslnprlSVL-- 382
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQhGQVLVDGVDLAIADPAWL---RRQMGVVLQE---------NVLfs 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEEGLRVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAE-------FSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:TIGR01846 545 RSIRDNIALCNPGAPFEHVIHAAKLAGAHDFI-SELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 456 LDRTVQAQILTLLKSLQEKHRLayIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR01846 624 LDYESEALIMRNMREICRGRTV--IIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
261-499 |
3.14e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.22 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 261 PSGDPVPLPVGQAPLLEVEKLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQ 339
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYPGRRPALR----------PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 340 GSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnsslnprLSVLQIIEEGLRVHQPtlsaEQREAQVKAVMAEVGLDSETR 419
Cdd:TIGR02857 377 GSIAVNGVPLADADADSW---RDQIAWVPQHP-------FLFAGTIAENIRLARP----DASDAEIREALERAGLDEFVA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 420 HR----------YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLayIFISHDLHVV 489
Cdd:TIGR02857 443 ALpqgldtpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV--LLVTHRLALA 520
|
250
....*....|
gi 2551249897 490 rALCHQVIVL 499
Cdd:TIGR02857 521 -ALADRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
264-508 |
3.43e-24 |
|
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: 106.44 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 264 DPVPLPVGQApllEVEKLRVAF------PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALLRLI- 336
Cdd:COG5265 347 DAPPLVVGGG---EVRFENVSFgydperPILKGV--------------SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 337 TSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSlnprlsvlqiIEEGLRVHQPTLSAEQREAQVKA------ 407
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTvlfNDT----------IAYNIAYGRPDASEEEVEAAARAaqihdf 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 408 ----------VMAEVGLdsetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-RTVQAqILTLLKSLQEKHr 476
Cdd:COG5265 477 ieslpdgydtRVGERGL----------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDsRTERA-IQAALREVARGR- 544
|
250 260 270
....*....|....*....|....*....|...
gi 2551249897 477 lAYIFISHDLH-VVRAlcHQVIVLRQGEVVEQG 508
Cdd:COG5265 545 -TTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-247 |
3.65e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 106.34 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSppVVYP-SGDIRFHGESLLHAneqTL 86
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPR--FYEPdSGQILLDGHDLADY---TL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 87 RDVRgNKIAMIFQEPMVSLNPLHNlekqlyevlSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQ--------LS 158
Cdd:TIGR02203 402 ASLR-RQVALVSQDVVLFNDTIAN---------NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvlLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQ 238
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVER 548
|
....*....
gi 2551249897 239 NRAAQLLTA 247
Cdd:TIGR02203 549 GTHNELLAR 557
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
306-504 |
3.72e-24 |
|
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: 100.62 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnsSLNPRlSVLQI 384
Cdd:cd03248 34 SFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYL---HSKVSLVGQEP--VLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLrvhqPTLSAEQ-REAQVKA------VMAEVGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03248 108 IAYGL----QSCSFECvKEAAQKAhahsfiSELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 458 RTVQAQILTLLKSLQEKHRlaYIFISHDLHVV-RAlcHQVIVLRQGEV 504
Cdd:cd03248 183 AESEQQVQQALYDWPERRT--VLVIAHRLSTVeRA--DQILVLDGGRI 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
273-517 |
4.20e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVF 344
Cdd:PRK09536 1 MPMIDVSDLSVEFgdtTVLDGV--------------DLSVREGSLVGLVGPNGAGKTT----LLRAIngtltPTAGTVLV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 345 DGLALHTLNRRQllpVRHRIQVVFQDpnSSLNPRLSVLQIIEEGLRVHQPTLSA--EQREAQVKAVMAEVGLDSETrHRY 422
Cdd:PRK09536 63 AGDDVEALSARA---ASRRVASVPQD--TSLSFEFDVRQVVEMGRTPHRSRFDTwtETDRAAVERAMERTGVAQFA-DRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFIsHDLHVVRALCHQVIVLRQG 502
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADG 215
|
250
....*....|....*
gi 2551249897 503 EVVEQGQCEHVFNAP 517
Cdd:PRK09536 216 RVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-258 |
4.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 7 AIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVVYPSGDIRFHGESLlhaNEQTL 86
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL--PDDNPNSKITVDGITL---TAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 87 RDVRgNKIAMIFQEP-------MVSLNPLHNLEkqlyevlslHRGMRREAARAEILTCLDRVGirqaakrLADY----PH 155
Cdd:PRK13640 80 WDIR-EKVGIVFQNPdnqfvgaTVGDDVAFGLE---------NRAVPRPEMIKIVRDVLADVG-------MLDYidsePA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSiVKKLADTVAVMQNGQC 235
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKL 221
|
250 260 270
....*....|....*....|....*....|.
gi 2551249897 236 VEQNRAAQLLTAPTH--------PYTKKLLN 258
Cdd:PRK13640 222 LAQGSPVEIFSKVEMlkeigldiPFVYKLKN 252
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
309-507 |
4.29e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.62 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 309 LRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHR-IQVVFQdpNSSLNPRLSVL 382
Cdd:PRK10584 33 VKRGETIALIGESGSGKST----LLAILAglddgSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQ--SFMLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QiieeglRVHQPTL----SAEQREAQVKAVMAEVGLDSETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK10584 107 E------NVELPALlrgeSSRQSRNGAKALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVrALCHQVIVLRQGEVVEQ 507
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-508 |
4.93e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.43 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlALHTLNRrqllPVRHRIQVVFQDPNssLNPRLS 380
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKST----LLNLIAgfltpASGSLTLNG-QDHTTTP----PSRRPVSMLFQENN--LFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIeeGLRVHqP--TLSAEQREaQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK10771 88 VAQNI--GLGLN-PglKLNAAQRE-KLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
256-508 |
5.87e-24 |
|
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: 105.55 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 256 LLNSEPS----GDPVPLPVGQAPLLEVEKLRVAFPIRKGILkrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTTGLA 331
Cdd:TIGR02204 314 LLQAEPDikapAHPKTLPVPLRGEIEFEQVNFAYPARPDQP--------ALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 332 LLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSSLNprlSVLqiieEGLRVHQPTLSAEQ-REAQVKAVM 409
Cdd:TIGR02204 386 LLRFYDpQSGRILLDGVDLRQLDPAEL---RARMALVPQDPVLFAA---SVM----ENIRYGRPDATDEEvEAAARAAHA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 410 AEV------GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQeKHRLAYIfIS 483
Cdd:TIGR02204 456 HEFisalpeGYDTYLGER-GVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLM-KGRTTLI-IA 532
|
250 260
....*....|....*....|....*
gi 2551249897 484 HDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR02204 533 HRLATVLK-ADRIVVMDQGRIVAQG 556
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
306-518 |
5.88e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSIVFDG--LALHTLNRrQLLPVRHRIQVVFQDPNSSLNPR 378
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPSSGTITIAGyhITPETGNK-NLKKLRKKVSLVFQFPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 lSVLQIIEEGLRvhqpTLSAEQREAQVKAV--MAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK13641 102 -TVLKDVEFGPK----NFGFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 457 DRTVQAQILTLLKSLQ-EKHRLayIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQkAGHTV--ILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
306-520 |
6.38e-24 |
|
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: 105.72 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALhtlnrRQLLP--VRHRIQVVFQDPnsslnpR 378
Cdd:TIGR03375 485 SLTIRPGEKVAIIGRIGSGKST----LLKLLLglyqpTEGSVLLDGVDI-----RQIDPadLRRNIGYVPQDP------R 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 L---SVLQIIEEGlrvhqptlSAEQREAQVKAVMAEVGLDSETRhRYPAEF-----------SGGQRQRIAIARALILKP 444
Cdd:TIGR03375 550 LfygTLRDNIALG--------APYADDEEILRAAELAGVTEFVR-RHPDGLdmqigergrslSGGQRQAVALARALLRDP 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 445 SLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLayIFISHDLHVVRaLCHQVIVLRQGEVVEQGQCEHVFNAPQQA 520
Cdd:TIGR03375 621 PILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-524 |
7.01e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 315 LGLVGESGSGKSTTGLALLRLITSQGS-IVFDGLALH---TLNRRQLLPVRHRIQVVFQDPNSSlnPRLSVLQIIEEGLR 390
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYfgkDIFQIDAIKLRKEVGMVFQQPNPF--PHLSIYDNIAYPLK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 391 VHQptlSAEQREaqVKAVMAE----VGLDSETRHRY--PA-EFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQ 463
Cdd:PRK14246 117 SHG---IKEKRE--IKKIVEEclrkVGLWKEVYDRLnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 464 ILTLLKSLqeKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQ 524
Cdd:PRK14246 192 IEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
28-234 |
9.71e-24 |
|
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: 99.24 E-value: 9.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHANEQTLRDVRgNKIAMIFQEPM 102
Cdd:TIGR02673 21 VSLHIRKGEFLFLTGPSGAGKT----TLLKLLygaltPS------RGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 VSLNplhnleKQLYE--VLSLH-RGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:TIGR02673 90 LLPD------RTVYEnvALPLEvRGKKEREIQRRVGAALRQVGL---EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 180 ADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-245 |
1.40e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.27 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLRdvrgNKIAMIFQEP 101
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPQ----SGRILIDGTDIRTVTRASLR----RNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 MVslnplhnLEKQLYEVLSLHRG------MRREAARAEILTCLDR--------VGIRQaakrladypHQLSGGERQRVMI 167
Cdd:PRK13657 419 GL-------FNRSIEDNIRVGRPdatdeeMRAAAERAQAHDFIERkpdgydtvVGERG---------RQLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQLL 245
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELV 557
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
276-508 |
1.47e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 276 LEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALL----RLITSqGSIVFDG-- 346
Cdd:COG0396 1 LEIKNLHVSVegkEILKGV--------------NLTIKPGEVHAIMGPNGSGKSTLAKVLMghpkYEVTS-GSILLDGed 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 -LALHTLNRrqllpVRHRIQVVFQDPnsslnPR---LSVLQIIEEGL-RVHQPTLSAEQREAQVKAVMAEVGLDSETRHR 421
Cdd:COG0396 66 iLELSPDER-----ARAGIFLAFQYP-----VEipgVSVSNFLRTALnARRGEELSAREFLKLLKEKMKELGLDEDFLDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 422 YPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLD----RTVQAQIltllKSLQEKHRlAYIFISHD---LHVVRAlc 493
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidalRIVAEGV----NKLRSPDR-GILIITHYqriLDYIKP-- 208
|
250
....*....|....*
gi 2551249897 494 HQVIVLRQGEVVEQG 508
Cdd:COG0396 209 DFVHVLVDGRIVKSG 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-234 |
1.60e-23 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 98.73 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqeTVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLlhane 83
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLtgELRPT------SGTAYINGYSI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRGNKIAMIFQEPMV--SLNPLHNLEkqLYevlSLHRGMRREAARAEILTCLDRVGIRQAAKRLAdypHQLSGGE 161
Cdd:cd03263 67 RTDRKAARQSLGYCPQFDALfdELTVREHLR--FY---ARLKGLPKSEIKEEVELLLRVLGLTDKANKRA---RTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMglLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
306-523 |
1.77e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.72 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLalhtlnrrqllPVRHR-IQ-----VVFQdpNSS 374
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDGE-----------DVTHRsIQqrdicMVFQ--SYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 375 LNPRLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLDSeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLG--VPKEERKQRVKEALELVDLAG-FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGqcehvfnAPQQAYTR 523
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIG-------SPQELYRQ 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-257 |
2.03e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.42 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLRDVRGNKIAMIFQE--PM 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKS-TMVRLLNRLIEPT----RGQVLIDGVDIAKISDAELREVRRKKIAMVFQSfaLM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 VSLNPLHNLEKQLyEVLSLHRGMRREAAraeiLTCLDRVGIRQAAKrlaDYPHQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:PRK10070 119 PHMTVLDNTAFGM-ELAGINAEERREKA----LDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 183 PTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPTHPYTKKLL 257
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
264-526 |
2.89e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 264 DPVPLPVGQA-----PLLEVEKLRVAFPIRKGIlkrvvdhnvvvNDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT- 337
Cdd:PRK11607 3 DAIPRPQAKTrkaltPLLEIRNLTKSFDGQHAV-----------DDVSLTIYKGEIFALLGASGCGKST----LLRMLAg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 338 ----SQGSIVFDGLALhtlnrRQLLPVRHRIQVVFQdpNSSLNPRLSVLQIIEEGLRvhQPTLSAEQREAQVKAVMAEVG 413
Cdd:PRK11607 68 feqpTAGQIMLDGVDL-----SHVPPYQRPINMMFQ--SYALFPHMTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 414 LdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALC 493
Cdd:PRK11607 139 M-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMA 217
|
250 260 270
....*....|....*....|....*....|...
gi 2551249897 494 HQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK11607 218 GRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-247 |
3.16e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLLHANEQT 85
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT--PQ---SGTVFLGDKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LrdvrGNKIAMIFQEPMVslnPLHNLEKQLYEV-----LSLHrGMRREAARAEILTCLDRVGIRQAAKRLADyphQLSGG 160
Cdd:PRK11231 74 L----ARRLALLPQHHLT---PEGITVRELVAYgrspwLSLW-GRLSAEDNARVNQAMEQTRINHLADRRLT---DLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElnmGLLFIT--HNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ---GKTVVTvlHDLNQASRYCDHLVVLANGHVMAQ 219
|
....*....
gi 2551249897 239 NRAAQLLTA 247
Cdd:PRK11231 220 GTPEEVMTP 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-236 |
3.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.74 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTV-VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHANEQt 85
Cdd:PRK13637 5 IENLTHIYMEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPT------SGKIIIDGVDITDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEPmvslnplhnlEKQLYEVL--------SLHRGMRREAARAEILTCLDRVGIRQaaKRLAD-YPHQ 156
Cdd:PRK13637 78 LSDIR-KKVGLVFQYP----------EYQLFEETiekdiafgPINLGLSEEEIENRVKRAMNIVGLDY--EDYKDkSPFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
306-505 |
3.85e-23 |
|
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: 102.60 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-------TSQGSIVFDGLALHTLNRRQllPVRHRIQVVFQDpnSSLNPR 378
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKST----LMKILsgvyphgTWDGEIYWSGSPLKASNIRD--TERAGIVIIHQE--LTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVLQ-------IIEEGLRVHQPTLSAeqreaQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:TIGR02633 93 LSVAEniflgneITLPGGRMAYNAMYL-----RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 452 PTSSLDRTVQAQILTLLKSLQeKHRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-234 |
4.34e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLpsppvvYP-SGDIRFHGESLlhaNEQTLRDV------RGnki 94
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL------APdSGEVLWDGEPL---DPEDRRRIgylpeeRG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 95 amifqepmvsLNPLHNLEKQLYEVLSLHrGMRREAARAEILTCLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTR 174
Cdd:COG4152 82 ----------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKVE---ELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 175 PELLIADEPTTALD-VSVQAqILQLLRELQHElnmG--LLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:COG4152 148 PELLILDEPFSGLDpVNVEL-LKDVIRELAAK---GttVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-245 |
4.46e-23 |
|
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: 97.68 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHANEQTL 86
Cdd:cd03254 5 FENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQ------KGQILIDGIDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 87 RdvrgNKIAMIFQEPMVslnplhnLEKQLYEVLSLHrgmRREAARAEILTCLDRVGIRQAAKRLAD-YPHQ-------LS 158
Cdd:cd03254 76 R----SMIGVVLQDTFL-------FSGTIMENIRLG---RPNATDEEVIEAAKEAGAHDFIMKLPNgYDTVlgenggnLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQ 238
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
....*..
gi 2551249897 239 NRAAQLL 245
Cdd:cd03254 219 GTHDELL 225
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-289 |
4.82e-23 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 100.15 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQEtvrtvVNTLSLRVDAGQTLALVGESGSGKSVTaLSILRLLPSPPvvypSGDIRFHGESL-LHANE 83
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVL-LELIAGIWPPD----SGKIYLDGKDItNLPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QtlrdvRGnkIAMIFQEPMvsLNPlhnlEKQLYEVLSLhrGMR-REAARAEILTCLDRV----GIRQAAKRladYPHQLS 158
Cdd:NF040840 71 K-----RG--IAYVYQNYM--LFP----HKTVFENIAF--GLKlRKVPKEEIERKVKEImellGISHLLHR---KPRTLS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:NF040840 133 GGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQV 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 239 NRAAQLLTAPTHPYTKKLLNSEPSGDPVPLPVGQAPLLEVEKLRVAFPIRK 289
Cdd:NF040840 213 GDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTILDTGNIKIELPEEK 263
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
306-508 |
5.00e-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: 103.10 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGlallRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDpnsslnprLS 380
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIPREEIPREVL---ANSVAMVDQD--------IF 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQ-IIEEGLRVHQPTLSAEQ--REAQVKAVMAEV-----GLDSETrhrypAE----FSGGQRQRIAIARALILKPSLII 448
Cdd:TIGR03796 564 LFEgTVRDNLTLWDPTIPDADlvRACKDAAIHDVItsrpgGYDAEL-----AEgganLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 449 LDEPTSSLDRTVQAQILTLLKslqeKHRLAYIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR03796 639 LDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRG 693
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
306-523 |
5.04e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.19 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLR-------LITSQ---GSIVFDGlalHTLNRRQLLPVRHRIQV--VFQDPNs 373
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPGArveGEILLDG---EDIYDPDVDVVELRRRVgmVFQKPN- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 374 slnP-RLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDSETRHR---YPAEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:COG1117 103 ---PfPKSIYDNVAYGLRLHG-IKSKSELDEIVEESLRKAALWDEVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 450 DEPTSSLDRTVQAQILTLLKSLqeKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTR 523
Cdd:COG1117 179 DEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-234 |
5.31e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSppVVYPSGdirfhGESLlhANEQT 85
Cdd:PRK11247 13 LLLNAVSKRYGE----RTVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAG--LETPSA-----GELL--AGTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEpmVSLNPLhnleKQLYEVLSLH-RGMRREAARAeiltCLDRVGIrqaAKRLADYPHQLSGGERQR 164
Cdd:PRK11247 76 LAEAR-EDTRLMFQD--ARLLPW----KKVIDNVGLGlKGQWRDAALQ----ALAAVGL---ADRANEWPAALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-249 |
5.82e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANE 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDT----TVLDGVDLSVREGSLVGLVGPNGAGKT-TLLRAINGTLTPT----AGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLrdvrGNKIAMIFQEPMVSLNplhNLEKQLYEV-LSLHRG---MRREAARAEILTCLDRVGIRQAAKRLADyphQLSG 159
Cdd:PRK09536 73 RAA----SRRVASVPQDTSLSFE---FDVRQVVEMgRTPHRSrfdTWTETDRAAVERAMERTGVAQFADRPVT---SLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFItHNLSIVKKLADTVAVMQNGQCVEQN 239
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
250
....*....|
gi 2551249897 240 RAAQLLTAPT 249
Cdd:PRK09536 222 PPADVLTADT 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
307-514 |
6.25e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.54 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 307 FSLRPgeTLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHtLNRRQLLPVRHRIQVVFQDPNSSLnprlsVLQII 385
Cdd:PRK13638 24 FSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQkGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQI-----FYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 EEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 465 LTLLKSLQEKHRLAYIfISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13638 176 IAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-252 |
7.35e-23 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 99.49 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 40 LVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaneqTLRDVRGNKIAMIFQEpmVSLNPLHNLEKQLYEVL 119
Cdd:TIGR01187 1 LLGPSGCGKT-TLLRLLAGFEQPD----SGSIMLDGEDV------TNVPPHLRHINMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 120 SLhRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLL 199
Cdd:TIGR01187 68 KM-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 200 RELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPTHPY 252
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-249 |
7.91e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.55 E-value: 7.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 32 VDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhGESLLHA--NEQTLRDVRgNKIAMIFQEPmvslnplh 109
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKS-TLLQHLNGLLQPT----SGTVTI-GERVITAgkKNKKLKPLR-KKVGIVFQFP-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 110 nlEKQLYE--VLS------LHRGMRREAARAEILTCLDRVGIRQAAkrLADYPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:PRK13634 95 --EHQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGLPEEL--LARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 182 EPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPT 249
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-238 |
9.69e-23 |
|
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: 96.41 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQTLR 87
Cdd:cd03244 5 FKNVSLRYRPNL--PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 dvrgNKIAMIFQEPMV-------SLNPLHnlekqlyevlslhrgmrrEAARAEILTCLDRVGIRQAAK--------RLAD 152
Cdd:cd03244 78 ----SRISIIPQDPVLfsgtirsNLDPFG------------------EYSDEELWQALERVGLKEFVEslpggldtVVEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqHELNMGLLFITHNLSIVKKlADTVAVMQN 232
Cdd:cd03244 136 GGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDK 212
|
....*.
gi 2551249897 233 GQCVEQ 238
Cdd:cd03244 213 GRVVEF 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
306-508 |
1.22e-22 |
|
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: 96.12 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRL-ITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnsslnpRL---SV 381
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDV------TLfygTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 LQIIEEGLrvhqptLSAEQREAQVKAVMAEV---------GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03245 95 RDNITLGA------PLADDERILRAAELAGVtdfvnkhpnGLDLQIGER-GRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRLayIFISHDLHVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-248 |
1.44e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 23 TVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRL---LPSPPvvypSGDIRFHGESLLHANEQTlRDvrgnkIAMIFQ 99
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLvagLEKPT----EGQIFIDGEDVTHRSIQQ-RD-----ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 100 E----PMVSLNplHNLEKQLyEVLSLHRGMRREAARaEILTCLDRVGIrqaAKRLADyphQLSGGERQRVMIAMALLTRP 175
Cdd:PRK11432 86 SyalfPHMSLG--ENVGYGL-KMLGVPKEERKQRVK-EALELVDLAGF---EDRYVD---QISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 176 ELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAP 248
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
306-517 |
1.92e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.62 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQllpvrHRIQVVFQdpNSSLNPRLS 380
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTT----LLRIIAglehqTSGHIRFHGTDVSRLHARD-----RKVGFVFQ--HYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRV--HQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:PRK10851 91 VFDNIAFGLTVlpRRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 459 TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-247 |
2.02e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 96.31 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVgFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPS--PPVVypSGDIRFHGESLLH 80
Cdd:COG1119 1 DPLLELRNVTV-RRGG---KTILDDISWTVKPGEHWAILGPNGAGKS----TLLSLITGdlPPTY--GNDVRLFGERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANeqtLRDVRgNKIAMIFQEPMVSLNPLHNLEK----QLYEVLSLHRG-MRREAARAEILtcLDRVGIRQAAKRLadyPH 155
Cdd:COG1119 71 ED---VWELR-KRIGLVSPALQLRFPRDETVLDvvlsGFFDSIGLYREpTDEQRERAREL--LELLGLAHLADRP---FG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|..
gi 2551249897 236 VEQNRAAQLLTA 247
Cdd:COG1119 222 VAAGPKEEVLTS 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-526 |
2.29e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.45 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 317 LVGESGSGKSTTGLALLRLIT------SQGSIVFDGLALHTLNRRQLlPVRHRIQVVFQDPNSSlnPRLSVLQIIEEGLR 390
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSPDVDPI-EVRREVGMVFQYPNPF--PHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 391 VHQPTLSAEQREAQVKAVMAEVGLDSETRHR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTL 467
Cdd:PRK14267 112 LNGLVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 468 LKSLQEKHRLayIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTRQLL 526
Cdd:PRK14267 192 LFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-234 |
2.33e-22 |
|
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: 95.02 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHANEQTLR 87
Cdd:cd03226 2 IENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKT----TLAKIL--------AGLIKESSGSILLNGKPIKA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRGNKIAMIFQEPmvslnplhnlEKQLYE--VLS-LHRGMRREAARAEILTC-LDRVGIRQAAKRladYPHQLSGGERQ 163
Cdd:cd03226 67 KERRKSIGYVMQDV----------DYQLFTdsVREeLLLGLKELDAGNEQAETvLKDLDLYALKER---HPLSLSGGQKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhelNMG--LLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA---AQGkaVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
276-508 |
2.70e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 95.86 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 276 LEVEKLRVAFPIR----------KGILKRVVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVF 344
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 345 DGLALHTlNRRQLLpvrHRIQVVFQDpNSSLNPRLSVLqiieEGLRVHQPTLSAEQREAQVK----AVMAEVG--LDSET 418
Cdd:cd03267 81 AGLVPWK-RRKKFL---RRIGVVFGQ-KTQLWWDLPVI----DSFYLLAAIYDLPPARFKKRldelSELLDLEelLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 419 RhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIV 498
Cdd:cd03267 152 R-----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLV 226
|
250
....*....|
gi 2551249897 499 LRQGEVVEQG 508
Cdd:cd03267 227 IDKGRLLYDG 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-508 |
3.43e-22 |
|
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: 95.43 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRV---AFPIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLA 348
Cdd:COG0410 1 MPMLEVENLHAgygGIHVLHGV--------------SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 349 LHTLNRRQLlpVRHRI-QV-----VFqdpnsslnPRLSVlqiiEEGLRVhqpTLSAEQREAQVKAVMAEVgLD-----SE 417
Cdd:COG0410 67 ITGLPPHRI--ARLGIgYVpegrrIF--------PSLTV----EENLLL---GAYARRDRAEVRADLERV-YElfprlKE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 418 TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKhRLAYIFISHDLHVVRALCHQVI 497
Cdd:COG0410 129 RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAY 207
|
250
....*....|.
gi 2551249897 498 VLRQGEVVEQG 508
Cdd:COG0410 208 VLERGRIVLEG 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-505 |
4.39e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 99.48 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 29 SLRVDAGQTLALVGESGSGKSvTALSILRllpsppVVYP----SGDIRFHGEsllhanEQTLRDVRGNK---IAMIFQE- 100
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKS-TLMKVLS------GVYPhgsyEGEILFDGE------VCRFKDIRDSEalgIVIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 ---PMVSLNP---LHNlEKQLYEVLSLHRGMRReaarAEILtcLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTR 174
Cdd:NF040905 88 aliPYLSIAEnifLGN-ERAKRGVIDWNETNRR----AREL--LAKVGLDESPDTLVT---DIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 175 PELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQnraaqlLTAPTHPYT- 253
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET------LDCRADEVTe 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 254 ---------KKLLNSEPSGDPvplPVGQaPLLEVEKLRVAFPI---RKgILKRvvdhnvvvndVSFSLRPGETLGLVGES 321
Cdd:NF040905 231 driirgmvgRDLEDRYPERTP---KIGE-VVFEVKNWTVYHPLhpeRK-VVDD----------VSLNVRRGEIVGIAGLM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 322 GSGKstTGLALL-------RLITsqGSIVFDGLALHTLNRRQllPVRHRIQVVFQD-------------PNSSLN--PRL 379
Cdd:NF040905 296 GAGR--TELAMSvfgrsygRNIS--GTVFKDGKEVDVSTVSD--AIDAGLAYVTEDrkgyglnliddikRNITLAnlGKV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEglrvHQPTLSAEQ--REAQVKA--VMAEVGldsetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:NF040905 370 SRRGVIDE----NEEIKVAEEyrKKMNIKTpsVFQKVG-----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRG 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 456 LDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:NF040905 435 IDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-519 |
5.62e-22 |
|
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: 94.53 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 307 FSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGlalhtlnrRQLLPVRHRIQVVFQDPNSSLNPRLSVLQII 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIpPAKGTVKVAG--------ASPGKGWRHIGYVPQRHEFAWDFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 EEGLRVHQPTLSAEQRE--AQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQ 463
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVAdfAAVRDALRRVGL-TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 464 ILTLLKSL-QEKHrlAYIFISHDLHVVRALCHQViVLRQGEVVEQGqcehvfnAPQQ 519
Cdd:TIGR03771 152 LTELFIELaGAGT--AILMTTHDLAQAMATCDRV-VLLNGRVIADG-------TPQQ 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
306-514 |
5.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTgLALLR--LITSQGSIVFDGLALHTLNR-RQLLPVRHRIQVVFQDPNSSLNPRlSVL 382
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTI-MQLLNglHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFPESQLFEE-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEEGlrvhqPT---LSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:PRK13649 105 KDVAFG-----PQnfgVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 460 VQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13649 180 GRKELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-238 |
8.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLlhaNEQTLR 87
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE-----KVKSGEIFYNNQAI---TDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRgNKIAMIFQEP-------MVSLNPLHNLEKQLYEvlslHRGMRREAARA-EILTCLDRvgirqaakrlADY-PHQLS 158
Cdd:PRK13648 80 KLR-KHIGIVFQNPdnqfvgsIVKYDVAFGLENHAVP----YDEMHRRVSEAlKQVDMLER----------ADYePNALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQ 238
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKE 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
306-505 |
8.85e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.79 E-value: 8.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDP----NSSLN 376
Cdd:PRK10908 22 TFHMRPGEMAFLTGHSGAGKST----LLKLICgierpSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHhllmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 377 PRLSVLQIIEEGlrvhqptlSAEQREAQVKAVMAEVGLDSETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK10908 98 DNVAIPLIIAGA--------SGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 457 DRTVQAQILTLlksLQEKHRLA--YIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:PRK10908 169 DDALSEGILRL---FEEFNRVGvtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-509 |
9.08e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.74 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSLnp 377
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKST----LLQLLTrawdpQQGEILLNGQPIADYSEAAL---RQAISVVSQRVhlfSATL-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 rlsvlqiiEEGLRVHQPTLSaeqrEAQVKAVMAEVGLDS--ETRHRYPA-------EFSGGQRQRIAIARALILKPSLII 448
Cdd:PRK11160 431 --------RDNLLLAAPNAS----DEALIEVLQQVGLEKllEDDKGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 449 LDEPTSSLDRTVQAQILTLL-KSLQEKhrlAYIFISHDLhvvRALCH--QVIVLRQGEVVEQGQ 509
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLaEHAQNK---TVLMITHRL---TGLEQfdRICVMDNGQIIEQGT 556
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
306-526 |
9.21e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQL------LPVRHriqvvfqdpnssLNPR 378
Cdd:PRK11231 22 SLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLarrlalLPQHH------------LTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 -LSVLQIIEEGlrvHQPTLS-----AEQREAQVKAVMAEVGLDSETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PRK11231 90 gITVRELVAYG---RSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRL-TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGqcehvfnAPQQAYTRQLL 526
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-516 |
9.21e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFPIRKGILKRVVDHNVVVNDV-----------SFSLRPGETLGLVGESGSGKSTtglaLLRLIT---- 337
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKELLLRRRRTrreefwalkdvSFEVERGESVGIIGRNGAGKST----LLKLIAgile 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 338 -SQGSIVFDGlalhtlnrrqllpvrhRIQVVFqDPNSSLNPRLSVLQIIEEGLRVHQptLSAEQREAQVKAVM--AEVG- 413
Cdd:COG1134 78 pTSGRVEVNG----------------RVSALL-ELGAGFHPELTGRENIYLNGRLLG--LSRKEIDEKFDEIVefAELGd 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 414 -LDSETRHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRAL 492
Cdd:COG1134 139 fIDQPVKT-----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|....
gi 2551249897 493 CHQVIVLRQGEVVEQGQCEHVFNA 516
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
307-514 |
9.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 307 FSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSI-VFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRlSVLQI 384
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE-TVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRvhQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PRK13643 106 VAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 465 LTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13643 184 MQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
306-524 |
1.05e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.72 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRL------ITSQGSIVFDGLALHTlNRRQLLPVRHRIQVVFQDPNssLNPrL 379
Cdd:PRK14258 27 SMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneleseVRVEGRVEFFNQNIYE-RRVNLNRLRRQVSMVHPKPN--LFP-M 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRV--HQPTLsaeQREAQVKAVMAEVGLDSETR---HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK14258 103 SVYDNVAYGVKIvgWRPKL---EIDDIVESALKDADLWDEIKhkiHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 455 SLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVL-----RQGEVVEQGQCEHVFNAPQQAYTRQ 524
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-230 |
1.08e-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: 98.51 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFrqqETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFHGESLLHANEQT 85
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKS----TLLNLLLGFVDPT-EGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDvrgnKIAMIFQEPMVslnplhnLEKQLYEVLSLHRgmrREAARAEILTCLDRVGIRQAAK--------RLADYPHQL 157
Cdd:TIGR02857 394 WRD----QIAWVPQHPFL-------FAGTIAENIRLAR---PDASDAEIREALERAGLDEFVAalpqgldtPIGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSiVKKLADTVAVM 230
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-241 |
1.33e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTqPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPT----SGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMIFQE--PMVSLNPLHNLEkqlyeVLSLHRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLS 158
Cdd:PRK10535 75 LDADALAQLRREHFGFIFQRyhLLSHLTAAQNVE-----VPAVYAGLERKQRLLRAQELLQRLGL---EDRVEYQPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQ 238
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
...
gi 2551249897 239 NRA 241
Cdd:PRK10535 225 PPA 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
274-522 |
1.67e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAFPIRKGIlkrvvdhnvvvNDVSFSLRPGETLGLVGESGSGKSTTGLALLRL------ITSQGSIVFDGL 347
Cdd:PRK14239 4 PILQVSDLSVYYNKKKAL-----------NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 348 ALHTlNRRQLLPVRHRIQVVFQDPNSSlnPrLSVLQIIEEGLR---VHQPTLSAEQREAQVK--AVMAEVgldSETRHRY 422
Cdd:PRK14239 73 NIYS-PRTDTVDLRKEIGMVFQQPNPF--P-MSIYENVVYGLRlkgIKDKQVLDEAVEKSLKgaSIWDEV---KDRLHDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLayIFISHDLHVVRALCHQVIVLRQG 502
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|
gi 2551249897 503 EVVEQGQCEHVFNAPQQAYT 522
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKET 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
306-486 |
2.06e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTlnrrqllPVRHRiQVVFQdpNSSLNPRLS 380
Cdd:PRK11248 21 NLTLESGELLVVLGPSGCGKTT----LLNLIAgfvpyQHGSITLDGKPVEG-------PGAER-GVVFQ--NEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVhqPTLSAEQREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK11248 87 VQDNVAFGLQL--AGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*.
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDL 486
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-238 |
2.10e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.46 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESllhaNEQTLRDVRgNKIAMIFQEPmvs 104
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT----KDKYIRPVR-KRIGMVFQFP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 105 lnplhnlEKQLYEVlSLHR---------GMRREAARAEILTCLDRVGIRQAAKRLAdyPHQLSGGERQRVMIAMALLTRP 175
Cdd:PRK13646 95 -------ESQLFED-TVEReiifgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQS--PFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 176 ELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-215 |
2.32e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILR----LLPsppvvYPSGDIRFHgesllha 81
Cdd:COG4178 363 LALEDLTLRTPDG---RPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWP-----YGSGRIARP------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 neqtlrdvRGNKIAMIFQEPMVslnPLHNLEKQLyevlsLHRGMRREAARAEILTCLDRVGIRQAAKRL---ADYPHQLS 158
Cdd:COG4178 424 --------AGARVLFLPQRPYL---PLGTLREAL-----LYPATAEAFSDAELREALEAVGLGHLAERLdeeADWDQVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqhEL-NMGLLFITH 215
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELpGTTVISVGH 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
306-508 |
2.38e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 92.09 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP-------NSSLNP 377
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDL---RSSLTIIPQDPtlfsgtiRSNLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 --RLSVLQIIeEGLRVhqptlsaeqreaqvkavmAEVGLDsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:cd03369 105 fdEYSDEEIY-GALRV------------------SEGGLN----------LSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 456 LDRTVQAQIltlLKSLQEKHRLAYIF-ISHDLHVVrALCHQVIVLRQGEVVEQG 508
Cdd:cd03369 156 IDYATDALI---QKTIREEFTNSTILtIAHRLRTI-IDYDKILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-262 |
2.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSV-----TALsilrLLPSppvvypSGDIRFHGESL-LHANEQTLRDVRgNKIAMIFQEP 101
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTlmqhfNAL----LKPS------SGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 mvslnplhnlEKQLYE--VLS------LHRGMRREAARAEILTCLDRVGIRQaakRLADY-PHQLSGGERQRVMIAMALL 172
Cdd:PRK13641 95 ----------EAQLFEntVLKdvefgpKNFGFSEDEAKEKALKWLKKVGLSE---DLISKsPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 173 TRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLfITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPThpY 252
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE--W 238
|
250
....*....|
gi 2551249897 253 TKKLLNSEPS 262
Cdd:PRK13641 239 LKKHYLDEPA 248
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-233 |
3.02e-21 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 92.09 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 23 TVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLLHANEQTLRDVRgNKIAMIFQE 100
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKS-TLLKLIykEELPT------SGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 P--MVSLNPLHNLEKQLYEVLSLHRGMRREAARAeiltcLDRVGIRQAAKrlaDYPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:cd03292 87 FrlLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR---ALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 179 IADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-238 |
3.07e-21 |
|
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: 91.87 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTlALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLhANEQT 85
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMY-GLLGPNGAGKT-TLMRILATLTPPS----SGTIRIDGQDVL-KQPQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVrgnkIAMIFQEPMVSlnPLHNLEKQLYEVLSLHrGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQRV 165
Cdd:cd03264 70 LRRR----IGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-227 |
3.65e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.87 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILrllpsppvvypsgdirfhgeSLLHANE 83
Cdd:PRK09544 3 SLVSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL--------------------GLVAPDE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRGNKIAMIFQEpmVSLNPlhNLEKQLYEVLSLHRGMRReaarAEILTCLDRVgirQAAKrLADYPHQ-LSGGER 162
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQK--LYLDT--TLPLTVNRFLRLRPGTKK----EDILPALKRV---QAGH-LIDAPMQkLSGGET 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTV 227
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-215 |
3.90e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTvvntLSLRVDAGQTLALVGESGSGKSvTALS-ILRLLPSppvvypsgDIRFHGESLLHANEQ 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAP----LSLTVAPGEILTLMGPSGSGKS-TLLAaIAGTLSP--------AFSASGEVLLNGRRL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRGNKIAMIFQEPMvsLNP----LHNLekqlyeVLSLHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGG 160
Cdd:COG4136 69 TALPAEQRRIGILFQDDL--LFPhlsvGENL------AFALPPTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITH 215
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
208-508 |
3.97e-21 |
|
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: 96.71 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 208 MGLLFithnlSIVKKLADTVAVMQNGQCveqnrAAQLLTApthpytkkLLNSEPSGDPVPLPVGQAP-LLEVEKLRVAFP 286
Cdd:TIGR02203 280 MIALI-----RPLKSLTNVNAPMQRGLA-----AAESLFT--------LLDSPPEKDTGTRAIERARgDVEFRNVTFRYP 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 287 IRKgilkrvvdhNVVVNDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLN----RRQL 357
Cdd:TIGR02203 342 GRD---------RPALDSISLVIEPGETVALVGRSGSGKST----LVNLIPrfyepDSGQILLDGHDLADYTlaslRRQV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 358 LPVRHRIqVVFQDpnsslnprlSVLQIIEEGLRVHQPtlSAEQREAQVKAVMAEV------GLDSETRHRyPAEFSGGQR 431
Cdd:TIGR02203 409 ALVSQDV-VLFND---------TIANNIAYGRTEQAD--RAEIERALAAAYAQDFvdklplGLDTPIGEN-GVLLSGGQR 475
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 432 QRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHrlAYIFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-246 |
4.94e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.95 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 29 SLRVDAGQTLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESllHANEQTLRdvrgNKIAMIFQEPmvSLN 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIAgfLTPA------SGSLTLNGQD--HTTTPPSR----RPVSMLFQEN--NLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 107 PLHNLEKQLyeVLSLHRGMRREAA-RAEILTCLDRVGIRQAAKRLadyPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:PRK10771 84 SHLTVAQNI--GLGLNPGLKLNAAqREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 186 ALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLT 246
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
4.98e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.62 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESLLHA 81
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT-TLLNLIAgfLAPS------SGEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 neqtlrdvrGNKIAMIFQEP--MVSLNPLHNLEkqlyevLSLH-RGMRREAARAEILTCLDRVGIRQAAKRladYPHQLS 158
Cdd:COG4525 75 ---------GADRGVVFQKDalLPWLNVLDNVA------FGLRlRGVPKAERRARAEELLALVGLADFARR---RIWQLS 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITH 215
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
306-517 |
6.25e-21 |
|
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: 91.45 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGLALHTLNRRQllpvRHRIQVVFQDPNSSLNPRLS 380
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTT----FYMIVglvkpDSGKILLDGQDITKLPMHK----RARLGIGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVMAEVGLDSeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:cd03218 92 VEENILAVLEIR--GLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 461 QAQILTLLKSLqeKHRLAYIFIS-HDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:cd03218 169 VQDIQKIIKIL--KDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
254-513 |
7.82e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 95.88 E-value: 7.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 254 KKLLNSEPSGDP-VPLPVGQAPLlEVEKLRVAFPI-RKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTtgla 331
Cdd:TIGR01842 295 NELLANYPSRDPaMPLPEPEGHL-SVENVTIVPPGgKKPTLR----------GISFSLQAGEALAIIGPSGSGKST---- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 332 LLRLIT-----SQGSIVFDGLALHTLNRRQL------LP---------VRHRIQVVFQDPNSSlnprlsvlQIIEEGL-- 389
Cdd:TIGR01842 360 LARLIVgiwppTSGSVRLDGADLKQWDRETFgkhigyLPqdvelfpgtVAENIARFGENADPE--------KIIEAAKla 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 390 RVHQPTLSAEQreaqvkavmaevGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLK 469
Cdd:TIGR01842 432 GVHELILRLPD------------GYDTVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK 498
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2551249897 470 SLQEKHRLAyIFISHDLHVVrALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:TIGR01842 499 ALKARGITV-VVITHRPSLL-GCVDKILVLQDGRIARFGERDEV 540
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-245 |
9.23e-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: 95.66 E-value: 9.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHANEQTLRDVrgnkIAM 96
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVT------SGRILIDGQDIRDVTQASLRAA----IGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 97 IFQEPMvslnpLHN---LEKQLYevlslhrGmRREAARAEIltcldrvgiRQAAK--RLADY----PHQ----------- 156
Cdd:COG5265 437 VPQDTV-----LFNdtiAYNIAY-------G-RPDASEEEV---------EAAARaaQIHDFieslPDGydtrvgerglk 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLS-IVKklADTVAVMQNGQC 235
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStIVD--ADEILVLEAGRI 570
|
250
....*....|
gi 2551249897 236 VEQNRAAQLL 245
Cdd:COG5265 571 VERGTHAELL 580
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
306-517 |
9.60e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 95.55 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLnrrQLLPVRHRIQVVFQDP--------- 371
Cdd:PRK10789 335 NFTLKPGQMLGICGPTGSGKST----LLSLIqrhfdVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPflfsdtvan 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 372 NSSLNPRLSVLQIIEEGLR---VHQPTLSAEQreaqvkavmaevGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLII 448
Cdd:PRK10789 408 NIALGRPDATQQEIEHVARlasVHDDILRLPQ------------GYDTEVGER-GVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 449 LDEPTSSLDRTVQAQILTLLKSLQEKHRlayIFIShdLHVVRAL--CHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRT---VIIS--AHRLSALteASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-236 |
1.05e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSVTAL---SILRllPSppvvypSGDIRFHGESLLHANeQTLRDVRgNKIAMIFQE 100
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLhfnGILK--PT------SGEVLIKGEPIKYDK-KSLLEVR-KTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 PMVSLNPLHNLEKQLYEVLSLhrGMRREAARAEILTCLDRVGIRQAAKRLadyPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:PRK13639 87 PDDQLFAPTVEEDVAFGPLNL--GLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 181 DEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
272-502 |
1.07e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 272 QAPLLEVEKLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVfdg 346
Cdd:COG4178 359 EDGALALEDLTLRTPDGRPLLE----------DLSLSLKPGERLLITGPSGSGKST----LLRAIAglwpyGSGRIA--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 lalhtlnrrqlLPVRHRIQVVFQDPnsslnprlsvlQIIEEGLR--VHQPTLSAEQREAQVKAVMAEVGLDS-----ETR 419
Cdd:COG4178 422 -----------RPAGARVLFLPQRP-----------YLPLGTLReaLLYPATAEAFSDAELREALEAVGLGHlaerlDEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 420 HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKslQEKHRLAYIFISHDlHVVRALCHQVIVL 499
Cdd:COG4178 480 ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHR-STLAAFHDRVLEL 556
|
...
gi 2551249897 500 RQG 502
Cdd:COG4178 557 TGD 559
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
306-508 |
1.09e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 89.29 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRqllpVRHRIQVVFQDP---NSSLNP 377
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKST----LLQLLTgdlkpQQGEITLDGVPVSDLEKA----LSSLISVLNQRPylfDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLsvlqiieeGLRvhqptlsaeqreaqvkavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03247 94 NL--------GRR-----------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 458 RTVQAQIL-TLLKSLQEKhrlAYIFISHDLHVVRALcHQVIVLRQGEVVEQG 508
Cdd:cd03247 131 PITERQLLsLIFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-247 |
1.17e-20 |
|
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: 91.01 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 13 VGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHANEQTLRdvrgN 92
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP-----ENGRVLVDGHDLALADPAWLR----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 93 KIAMIFQEpmvslNPLHNleKQLYEVLSLHR---GMRR--EAAR---AEILTCLDRVGIRQAakrLADYPHQLSGGERQR 164
Cdd:cd03252 77 QVGVVLQE-----NVLFN--RSIRDNIALADpgmSMERviEAAKlagAHDFISELPEGYDTI---VGEQGAGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQL 244
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
...
gi 2551249897 245 LTA 247
Cdd:cd03252 224 LAE 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
312-504 |
1.35e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTlnrrqllpVRHRIQVVFQDpnSSLNPRLSVLQIIE 386
Cdd:PRK11247 38 GQFVAVVGRSGCGKST----LLRLLagletPSAGELLAGTAPLAE--------AREDTRLMFQD--ARLLPWKKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 387 EGLRVHQptlsaeqREAQVKAvMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILT 466
Cdd:PRK11247 104 LGLKGQW-------RDAALQA-LAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 2551249897 467 LLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:PRK11247 175 LIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
259-486 |
1.54e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 94.73 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 259 SEPSGDPVPLPVGQAPL----------LEVEKLRVAFPIRKGILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKSTT 328
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAagavglgkptLELRDLSAGYPGAPPVLDGV----------SLDLPPGERVAILGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 329 GLALLRLI-TSQGSIVFDGLALHTLNRRQllpVRHRIQVVFQDPN---SSlnprlsvlqiIEEGLRVHQPTLSaeqrEAQ 404
Cdd:TIGR02868 378 LATLAGLLdPLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAHlfdTT----------VRENLRLARPDAT----DEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 405 VKAVMAEVGLDSETR----------HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL-TLLKSLQE 473
Cdd:TIGR02868 441 LWAALERVGLADWLRalpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLeDLLAALSG 520
|
250
....*....|...
gi 2551249897 474 KhrlAYIFISHDL 486
Cdd:TIGR02868 521 R---TVVLITHHL 530
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-245 |
1.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVvNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQ 84
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQL-NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRdvrgNKIAMIFQEP-------MVSLNPLHNLEKQlyevlslhrGMRREAARAEILTCLDRVGIRQAAKRladYPHQL 157
Cdd:PRK13642 78 NLR----RKIGMVFQNPdnqfvgaTVEDDVAFGMENQ---------GIPREEMIKRVDEALLAVNMLDFKTR---EPARL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQNGQCVE 237
Cdd:PRK13642 142 SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
....*...
gi 2551249897 238 QNRAAQLL 245
Cdd:PRK13642 221 EAAPSELF 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-238 |
1.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHAnEQTLRDVRGNkIAMIFQEPMV 103
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPS------SGRILFDGKPIDYS-RKGLMKLRES-VGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 104 SLNPLHNLEKQLYEVLSLhrGMRREAARAEILTCLDRVGIrqaaKRLADYP-HQLSGGERQRVMIAMALLTRPELLIADE 182
Cdd:PRK13636 94 QLFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 183 PTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
312-507 |
2.18e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.60 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGlalhtlnRR--QLLPVRHRIQVVFQdpNSSLNPRLSVLQI 384
Cdd:PRK11650 30 GEFIVLVGPSGCGKST----LLRMVaglerITSGEIWIGG-------RVvnELEPADRDIAMVFQ--NYALYPHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQptLSAEQREAQVKAV--MAEVG--LDsetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK11650 97 MAYGLKIRG--MPKAEIEERVAEAarILELEplLD-----RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 461 QAQILTLLKSLQEKHRLAYIFISHDLhvVRA--LCHQVIVLRQGeVVEQ 507
Cdd:PRK11650 170 RVQMRLEIQRLHRRLKTTSLYVTHDQ--VEAmtLADRVVVMNGG-VAEQ 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-259 |
2.21e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDV----SLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQPT----AGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTlrdvrgNKIAMIFQEpmVSLNPLHNLEKQLYEVLSLHRGMRRE-AAR-AEILTCldrVGIRQAAKRladYPHQLS 158
Cdd:PRK11607 86 VPPYQ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEiASRvNEMLGL---VHMQEFAKR---KPHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|.
gi 2551249897 239 NRAAQLLTAPTHPYTKKLLNS 259
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGS 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-254 |
2.67e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvtalSILR-------LLPSPPVvypSGDIRFH 74
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNV----WLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRV---EGKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 75 GESLlHANEQTLRDVRgNKIAMIFQEPmvslNPLhnlEKQLYEVLSLhrGMRREAARAEILTCLDRvGIRQAA------K 148
Cdd:PRK14243 76 GKNL-YAPDVDPVEVR-RRIGMVFQKP----NPF---PKSIYDNIAY--GARINGYKGDMDELVER-SLRQAAlwdevkD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 149 RLADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVKKLADTVA 228
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT--IIIVTHNMQQAARVSDMTA 221
|
250 260 270
....*....|....*....|....*....|....*
gi 2551249897 229 VM---------QNGQCVEQNRAAQLLTAPTHPYTK 254
Cdd:PRK14243 222 FFnveltegggRYGYLVEFDRTEKIFNSPQQQATR 256
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
306-508 |
3.02e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.32 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGlalHTLNRRQLLPVRHRIQVVFQdpnsslNPRLSVLQI 384
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYdIDEGEILLDG---HDLRDYTLASLRNQVALVSQ------NVHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTLSAEQREAQVKAVMA-------EVGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK11176 434 ANNIAYARTEQYSREQIEEAARMAYAmdfinkmDNGLDTVIGEN-GVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 458 ----RTVQAQILTLLK---SLQEKHRLAYIFIShdlhvvralcHQVIVLRQGEVVEQG 508
Cdd:PRK11176 513 teseRAIQAALDELQKnrtSLVIAHRLSTIEKA----------DEILVVEDGEIVERG 560
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-233 |
3.25e-20 |
|
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: 89.45 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaneqtlrDVRGNKIAMIFQEpmVSLNP 107
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKS-TLLNLISGLAQPT----SGGVILEGKQI---------TEPGPDRMVVFQN--YSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 108 LHNLEKQLY-EVLSLHRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
Cdd:TIGR01184 68 WLTVRENIAlAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK---RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 187 LDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-249 |
3.36e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.90 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRqqetvrtvVNTLSLRVDAGQTLALVGESGSGKSvTALSILR-LLPSppvvypSGDIRFHGESLLHANEQ 84
Cdd:COG4138 1 LQLNDVAVAGR--------LGPISAQVNAGELIHLIGPNGAGKS-TLLARMAgLLPG------QGEILLNGRPLSDWSAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRgnkiAMIFQEPMvslnPLHNLekQLYEVLSLHR--GMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSGGER 162
Cdd:COG4138 66 ELARHR----AYLSQQQS----PPFAM--PVFQYLALHQpaGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 163 QRVMIAMALLT-------RPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:COG4138 133 QRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
250
....*....|....
gi 2551249897 236 VEQNRAAQLLTAPT 249
Cdd:COG4138 212 VASGETAEVMTPEN 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-236 |
4.54e-20 |
|
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: 88.96 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTalsiLRLLPSppVVYPS-GDIRFHGESLLHANE 83
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAG--LLEPDaGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVrgnkiamifqepmvslnPLHNLEKQLYEVLS----------LHrGMRREAARAEILTCLDRVGIRQAAKRLADy 153
Cdd:cd03266 75 EARRRL-----------------GFVSDSTGLYDRLTarenleyfagLY-GLKGDELTARLEELADRLGMEELLDRRVG- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:cd03266 136 --GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
...
gi 2551249897 234 QCV 236
Cdd:cd03266 213 RVV 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
306-508 |
5.61e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQllpVRHRIQVVFQDPNSSLNPrLSVLQI 384
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLpQRGRVKVMGREVNAENEKW---VRSKVGLVFQDPDDQVFS-STVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRvhQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PRK13647 101 VAFGPV--NMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2551249897 465 LTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13647 178 MEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
306-508 |
5.90e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 88.11 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITS-QGSIVFDGLALHTLnrrqllpVRHRIQVVFQDpnSSLNPRLSVLQI 384
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGKPLDIA-------ARNRIGYLPEE--RGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHqpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:cd03269 91 LVYLAQLK--GLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2551249897 465 LTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03269 168 KDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-238 |
7.32e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 86.98 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESLlhane 83
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKS-TLLQLLTgdLKPQ------QGEITLDGVPV----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRGNKIAMIFQEPmvslnplhnlekQLYEVlslhrgmrreaaraeilTCLDRVGIRqaakrladyphqLSGGERQ 163
Cdd:cd03247 67 SDLEKALSSLISVLNQRP------------YLFDT-----------------TLRNNLGRR------------FSGGERQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQHELNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQ 238
Cdd:cd03247 106 RLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
306-509 |
7.70e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSIVF------------------DGLALHTLNRRQLLPV-- 360
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTfiehlNAL----LLPDTGTIEWifkdeknkkktkekekvlEKLVIQKTRFKKIKKIke 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 361 -RHRIQVVFQDPNSSLnprlsVLQIIEEGLRVHQPTLSAEQREAQVKA--VMAEVGLDSETRHRYPAEFSGGQRQRIAIA 437
Cdd:PRK13651 103 iRRRVGVVFQFAEYQL-----FEQTIEKDIIFGPVSMGVSKEEAKKRAakYIELVGLDESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 438 RALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
306-527 |
9.85e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 87.97 E-value: 9.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTL--NRRqllpVRHRIQVVFQdpNSSLNPR 378
Cdd:TIGR03410 20 SLEVPKGEVTCVLGRNGVGKTT----LLKTLmgllpVKSGSIRLDGEDITKLppHER----ARAGIAYVPQ--GREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVLQIIEEGLrvhqptlsaEQREAQVKAVMAEVgLD-----SETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:TIGR03410 90 LTVEENLLTGL---------AALPRRSRKIPDEI-YElfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 454 SSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVfnapQQAYTRQLLA 527
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
306-508 |
1.23e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.40 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGSIVFDGLALHTLNRRQL--LP-VRhriqvvfqdpnsSLNP 377
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTT----IRIILgilapDSGEVLWDGEPLDPEDRRRIgyLPeER------------GLYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:COG4152 85 KMKVGEQLVYLARLKG--LSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 458 rTVQAQIL-TLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4152 162 -PVNVELLkDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
288-512 |
2.56e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 288 RKGILKRVvdhnvvvndvSFSLRPGETLGLVGESGSGKST--TGLALLRL--ITSQGSIVFDGlalHTLNRRQLlpvRHR 363
Cdd:TIGR00955 37 RKHLLKNV----------SGVAKPGELLAVMGSSGAGKTTlmNALAFRSPkgVKGSGSVLLNG---MPIDAKEM---RAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 364 IQVVFQDpnsSLN-PRLSVLQ--IIEEGLRVHQpTLSAEQREAQVKAVMAEVGLDS--ETRHRYPAE---FSGGQRQRIA 435
Cdd:TIGR00955 101 SAYVQQD---DLFiPTLTVREhlMFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 436 IARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEH 512
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-248 |
3.93e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRqqeTVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANeq 84
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKS-TLFRHFNGILKPT----SGSVLIRGEPITKEN-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 tLRDVRgNKIAMIFQEPMVSLnpLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLadyPHQLSGGERQR 164
Cdd:PRK13652 73 -IREVR-KFVGLVFQNPDDQI--FSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQL 244
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 2551249897 245 LTAP 248
Cdd:PRK13652 226 FLQP 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
306-508 |
5.13e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.57 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNSSLNPRLSVLqI 384
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDIDRHTL---RQFINYLPQEPYIFSGSILENL-L 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQ 463
Cdd:TIGR01193 570 LGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTElSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 464 ILTLLKSLQEKhrlAYIFISHDLHVVRaLCHQVIVLRQGEVVEQG 508
Cdd:TIGR01193 650 IVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-508 |
5.35e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.84 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 277 EVEKLRVAFPIR----------KGILKRVVDHNVVVNDVSFSLRPGETLGLVGESGSGKSTTglalLRLIT-----SQGS 341
Cdd:COG4586 3 EVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLTgilvpTSGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 342 IVFDGLALHtLNRRQLLpvrHRIQVVF-QdpNSSLNPRLSVLqiieEGLRVHQ-----PTLSAEQREAQVKAVMaEVG-- 413
Cdd:COG4586 79 VRVLGYVPF-KRRKEFA---RRIGVVFgQ--RSQLWWDLPAI----DSFRLLKaiyriPDAEYKKRLDELVELL-DLGel 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 414 LDSETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALC 493
Cdd:COG4586 148 LDTPVR-----QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALC 222
|
250
....*....|....*
gi 2551249897 494 HQVIVLRQGEVVEQG 508
Cdd:COG4586 223 DRVIVIDHGRIIYDG 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
318-524 |
5.49e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 318 VGESGSGKSTtglaLLR-------LITS---QGSIVFDGlalHTLNRRQLLP--VRHRIQVVFQDPNS---------SLN 376
Cdd:PRK14243 42 IGPSGCGKST----ILRcfnrlndLIPGfrvEGKVTFHG---KNLYAPDVDPveVRRRIGMVFQKPNPfpksiydniAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 377 PRLSVLQ-----IIEEGLRvhQPTLSAEqreaqVKAVMAEVGLdsetrhrypaEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK14243 115 ARINGYKgdmdeLVERSLR--QAALWDE-----VKDKLKQSGL----------SLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 452 PTSSLDRTVQAQILTLLKSLQEKHRLayIFISHDLHVVRALCHQVIVL---------RQGEVVEQGQCEHVFNAPQQAYT 522
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255
|
..
gi 2551249897 523 RQ 524
Cdd:PRK14243 256 RD 257
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-234 |
7.12e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 85.30 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 29 SLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTlrdvrgNKIAMIFQEPmvslNPL 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPA----SGSIKVNDQSHTGLAPYQ------RPVSMLFQEN----NLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 109 HNLEKQLYEVLSLHRGMRREAARAE-ILTCLDRVGIRQAAKRLadyPHQLSGGERQRVMIAMALLTRPELLIADEPTTAL 187
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLKLNAEQQEkVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 188 DVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
306-508 |
8.87e-19 |
|
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: 84.52 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITSQ-------GSIVFDGLALHTLNrrqllpVRHRIQVVFQDpnSSLNPR 378
Cdd:cd03213 29 SGKAKPGELTAIMGPSGAGKST----LLNALAGRrtglgvsGEVLINGRPLDKRS------FRKIIGYVPQD--DILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVlqiiEEGLRVhqptlSAEQReaqvkavmaevGLdsetrhrypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:cd03213 97 LTV----RETLMF-----AAKLR-----------GL------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 459 TVQAQILTLLKSLQEKHRLayIFIShdLHVVRA----LCHQVIVLRQGEVVEQG 508
Cdd:cd03213 145 SSALQVMSLLRRLADTGRT--IICS--IHQPSSeifeLFDKLLLLSQGRVIYFG 194
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-247 |
1.02e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPL----LAIENLSVGFRQQetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGES 77
Cdd:PRK10790 333 DRPLqsgrIDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 78 LLHANEQTLRdvrgNKIAMIFQEPMVslnplhnLEKQLYEVLSLHRGMRREAaraeILTCLDRVGIRQAAKRLADYPH-- 155
Cdd:PRK10790 405 LSSLSHSVLR----QGVAMVQQDPVV-------LADTFLANVTLGRDISEEQ----VWQALETVQLAELARSLPDGLYtp 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 ------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLS-IVKklADTVA 228
Cdd:PRK10790 470 lgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStIVE--ADTIL 545
|
250
....*....|....*....
gi 2551249897 229 VMQNGQCVEQNRAAQLLTA 247
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAA 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-249 |
1.19e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHANEQTLRdvrgNKIAMIFQEPM 102
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPT------GGQVLLDGVPLVQYDHHYLH----RQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 V-SLNPLHNLekqLYEVLSLHRGMRREAARAEilTCLDRVGIRQAAKRLADYPH--QLSGGERQRVMIAMALLTRPELLI 179
Cdd:TIGR00958 566 LfSGSVRENI---AYGLTDTPDEEIMAAAKAA--NAHDFIMEFPNGYDTEVGEKgsQLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 180 ADEPTTALDVSVQaQILQLLRELQhelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQLLTAPT 249
Cdd:TIGR00958 641 LDEATSALDAECE-QLLQESRSRA---SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
319-518 |
1.64e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 319 GESGSGKSTTGLALLRLITSQ-GSIVFDGlalHTL----NRRQLLPVRHRIQVVFQDpnSSLNPRLSVLQIIEEGLrvhq 393
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQkGRIVLNG---RVLfdaeKGICLPPEKRRIGYVFQD--ARLFPHYKVRGNLRYGM---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 394 ptlsAEQREAQVKAVMAEVGLDSETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQE 473
Cdd:PRK11144 102 ----AKSMVAQFDKIVALLGIEPLLD-RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 474 KHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-271 |
1.64e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.59 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPS--PPvvyPSGDIRFHGESLLHANEQT 85
Cdd:PRK11831 8 VDMRGVSFTRGN--RCIFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGqiAP---DHGEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEP--MVSLNPLHNLEKQLYEvlslHRGMRREAARAEILTCLDRVGIRQAAKRLadyPHQLSGGERQ 163
Cdd:PRK11831 79 LYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNrAAQ 243
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG-SAQ 229
|
250 260 270
....*....|....*....|....*....|
gi 2551249897 244 LLTAPTHPYTKKLLNSEPSGdPVPL--PVG 271
Cdd:PRK11831 230 ALQANPDPRVRQFLDGIADG-PVPFryPAG 258
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-245 |
1.76e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.32 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGFRQQET-VRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFH-GESLLH 80
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT-----SGEVNVRvGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLrDVRGNK---IAMIFQEpmVSLNPLHNLEKQLYEVLSLHrgMRREAARAEILTCLDRVGI--RQAAKRLADYPH 155
Cdd:TIGR03269 352 MTKPGP-DGRGRAkryIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFdeEKAEEILDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|
gi 2551249897 236 VEQNRAAQLL 245
Cdd:TIGR03269 507 VKIGDPEEIV 516
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-234 |
1.83e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 39 ALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHgESLLHANEQTLRDVRGN--------KIAMIFQEpmVSLNPlHn 110
Cdd:PRK11144 28 AIFGRSGAGKT----SLINAI--------SGLTRPQ-KGRIVLNGRVLFDAEKGiclppekrRIGYVFQD--ARLFP-H- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 111 lekqlYEVL-SLHRGMRREAaRAEILTCLDRVGIRQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
Cdd:PRK11144 91 -----YKVRgNLRYGMAKSM-VAQFDKIVALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 190 SVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
317-515 |
2.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 317 LVGESGSGKST-----TGLallrLITSQG-SIVFDGLALHTLNR-RQLLPVRHRIQVVFQDPNSSLnprlsVLQIIEEGL 389
Cdd:PRK13645 42 VIGTTGSGKSTmiqltNGL----IISETGqTIVGDYAIPANLKKiKEVKRLRKEIGLVFQFPEYQL-----FQETIEKDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 390 RVHQPTLSAEQREA--QVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTL 467
Cdd:PRK13645 113 AFGPVNLGENKQEAykKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 468 LKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK13645 193 FERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-249 |
2.54e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLrdvrGNKIAMIFQEp 101
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPPS----EGEILLDAQPLESWSSKAF----ARKVAYLPQQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 mvsLNPLHNLekQLYEVLSLHR-------GMRREAARAEILTCLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTR 174
Cdd:PRK10575 94 ---LPAAEGM--TVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD---SLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 175 PELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAPT 249
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-234 |
2.83e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFrQQETV--RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGESLLHA 81
Cdd:COG1101 2 LELKNLSKTF-NPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLNAIagSLPPD------SGSILIDGKDVTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEqtlrDVRGNKIAMIFQEPMV----SLNPLHNLekqlyeVLSLHRGMRREAARA----------EILTCLDRvGIrqaA 147
Cdd:COG1101 74 PE----YKRAKYIGRVFQDPMMgtapSMTIEENL------ALAYRRGKRRGLRRGltkkrrelfrELLATLGL-GL---E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 148 KRLADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTV 227
Cdd:COG1101 140 NRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRL 219
|
....*..
gi 2551249897 228 AVMQNGQ 234
Cdd:COG1101 220 IMMHEGR 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
306-526 |
2.88e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQ-GSIVFDGLALHTLNRRQllpVRHRIQVVFQdpNSSLNPRLSVLQI 384
Cdd:PRK10253 27 TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAhGHVWLDGEHIQHYASKE---VARRIGLLAQ--NATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTLSA--EQREAQVKAVMAEVGLDSETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:PRK10253 102 VARGRYPHQPLFTRwrKEDEEAVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 463 QILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGqcehvfnAPQQAYTRQLL 526
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELI 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
306-514 |
3.19e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-----TGLallrLITSQGSI-----------VFDGLALHTLNRR--QLLPVRHRIQVV 367
Cdd:PRK13631 46 SYTFEKNKIYFIIGNSGSGKSTlvthfNGL----IKSKYGTIqvgdiyigdkkNNHELITNPYSKKikNFKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 368 FQDPNSSLnprlsVLQIIEEGLRVHQPTLSAEQREAQVKAV--MAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPS 445
Cdd:PRK13631 122 FQFPEYQL-----FKDTIEKDIMFGPVALGVKKSEAKKLAKfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 446 LIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIfISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
306-521 |
3.25e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQGSIVFDGLALHTLNRRQLlpVRHRIQVVFQDPNSSLNPrlsVLQIi 385
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAEL--ARHRAYLSQQQTPPFAMP---VFQY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 eegLRVHQPTLSAE-QREAQVKAVMAEVGLDSETrHRYPAEFSGGQRQRIAIArALILK--PS------LIILDEPTSSL 456
Cdd:PRK03695 90 ---LTLHQPDKTRTeAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRVRLA-AVVLQvwPDinpagqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRlAYIFISHDL-HVVRAlCHQVIVLRQGEVVEQGQCEHVFNAP--QQAY 521
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGI-AVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRRDEVLTPEnlAQVF 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-249 |
3.27e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.36 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL-RLLPSPpvvypSGDIRFHGESLLHANEQTL 86
Cdd:COG4604 4 IKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMIsRLLPPD-----SGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 87 rdvrGNKIAMIFQEPMVSLNplhnlekqL--YEVLSL-----HRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSG 159
Cdd:COG4604 74 ----AKRLAILRQENHINSR--------LtvRELVAFgrfpySKGRLTAEDREIIDEAIAYLDLEDLADR---YLDELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQN 239
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
250
....*....|
gi 2551249897 240 RAAQLLTAPT 249
Cdd:COG4604 219 TPEEIITPEV 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
306-508 |
3.32e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 85.24 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRqllpVRHRIQVVFQDPNssLNPRLSVlqi 384
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARH----ARQRVGVVPQFDN--LDPDFTV--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 iEEGLRVHQP--TLSAEQREAQVKAVMAEVGLDSETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:PRK13537 98 -RENLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2551249897 463 QILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13537 176 LMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
315-517 |
4.94e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 315 LGLVGESGSGKSTtglaLLR-----LITSQGSIVFDGLALHTLNRRQllpVRHRIQVVFQDPNSSL-NPrlSVLQIIEEG 388
Cdd:PRK13652 33 IAVIGPNGAGKST----LFRhfngiLKPTSGSVLIRGEPITKENIRE---VRKFVGLVFQNPDDQIfSP--TVEQDIAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 389 lrvhqPT---LSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL 465
Cdd:PRK13652 104 -----PInlgLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 466 TLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP 517
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
306-508 |
5.03e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.97 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalhtlnrrqllpvrhRIQVVFqDPNSSLNPRLS 380
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKST----LLRLLAgiyppDSGTVTVRG----------------RVSSLL-GLGGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHqpTLSAEQREAQVKAVM--AEVG--LDSETRHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:cd03220 101 GRENIYLNGRLL--GLSRKEIDEKIDEIIefSELGdfIDLPVKT-----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 457 DRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
312-518 |
5.39e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTtglaLLRLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQdpNSSLNPRLSVLQIIEEGLRV 391
Cdd:PRK11000 29 GEFVVFVGPSGCGKST----LLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ--SYALYPHLSVAENMSFGLKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 392 hqPTLSAEQREAQVKAVmAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSL 471
Cdd:PRK11000 103 --AGAKKEEINQRVNQV-AEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 472 QEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:PRK11000 180 HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-259 |
7.43e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.55 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH--A 81
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGV----SMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYErrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRdvrgNKIAMIFQEPmvSLNPLHNLEKQLYEVLSLhrGMRREAARAEIL-TCLDRVGIRQAAK-RLADYPHQLSG 159
Cdd:PRK14258 82 NLNRLR----RQVSMVHPKP--NLFPMSVYDNVAYGVKIV--GWRPKLEIDDIVeSALKDADLWDEIKhKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNgqcvEQN 239
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG----NEN 229
|
250 260
....*....|....*....|
gi 2551249897 240 RAAQLLTAPThpyTKKLLNS 259
Cdd:PRK14258 230 RIGQLVEFGL---TKKIFNS 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-236 |
8.08e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 15 FRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESLlHANEQTLRdvrgN 92
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLTgiLVPT------SGEVRVLGYVP-FKRRKEFA----R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 93 KIAMIF-QE--------PMVSLNplhnLEKQLYEVlslhrgmRREAARAEILTCLDRVGIRQaakrLADYP-HQLSGGER 162
Cdd:COG4586 96 RIGVVFgQRsqlwwdlpAIDSFR----LLKAIYRI-------PDAEYKKRLDELVELLDLGE----LLDTPvRQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
8.22e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.80 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPVVypSGDIRFHGESLLHAnEQT 85
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGV----NLTIKKGEVHALMGPNGSGKS-TLAKTIMGHPKYEVT--EGEILFKGEDITDL-PPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGnkIAMIFQEPmvslnplhnlekqlyevlslhrgmrreaarAEIltcldrVGIRqaakrLADYPHQL----SGGE 161
Cdd:cd03217 73 ERARLG--IFLAFQYP------------------------------PEI------PGVK-----NADFLRYVnegfSGGE 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKL-ADTVAVMQNGQCVE 237
Cdd:cd03217 110 KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
8.39e-18 |
|
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: 81.32 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGfrqqetvrTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHANe 83
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPVTRRS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 qtLRDVRGNKIAMifqepmVSLNPLHN---LEKQLYEVLSLhrgmrreaaraeiltcldrvgirqaakrladyPHQLSGG 160
Cdd:cd03215 69 --PRDAIRAGIAY------VPEDRKREglvLDLSVAENIAL--------------------------------SSLLSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-236 |
9.46e-18 |
|
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: 81.44 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 10 NLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILR-LLPSPPVvypSGDIRFHGESLlhaNEQTLRd 88
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS-TLLNALAgRRTGLGV---SGEVLINGRPL---DKRSFR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 89 vrgNKIAMIFQEPMvslnplhnlekqLYEVLSLhrgmrREAaraeiltcldrvgIRQAAK-RladyphQLSGGERQRVMI 167
Cdd:cd03213 82 ---KIIGYVPQDDI------------LHPTLTV-----RET-------------LMFAAKlR------GLSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSI-VKKLADTVAVMQNGQCV 236
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSeIFELFDKLLLLSQGRVI 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-236 |
1.04e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 82.32 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 9 ENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVypSGDIRFHGESLlhaNEQTLRD 88
Cdd:cd03234 7 WDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTT--SGQILFNGQPR---KPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 89 vrgnKIAMIFQEPMvsLNPLHNLEKQLY--EVLSLHRGM--RREAARAEILTcLDRVGIRQAAKRLADYphqLSGGERQR 164
Cdd:cd03234 82 ----CVAYVRQDDI--LLPGLTVRETLTytAILRLPRKSsdAIRKKRVEDVL-LRDLALTRIGGNLVKG---ISGGERRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
312-526 |
1.06e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTtglaLLRLITSQ-----GSIVFDGLALHTLNRRQLLPVRHRIQVVFQdpNSSLNPRLSVLQIIE 386
Cdd:PRK11831 33 GKITAIMGPSGIGKTT----LLRLIGGQiapdhGEILFDGENIPAMSRSRLYTVRKRMSMLFQ--SGALFTDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 387 EGLRVHQpTLSAEQREAQVKAVMAEVGLDSETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILT 466
Cdd:PRK11831 107 YPLREHT-QLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 467 LLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVfNAPQQAYTRQLL 526
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPDPRVRQFL 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-220 |
1.23e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyPSGDirfhgesllhaneqTLRDVRGNKIAMIFQEP 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------PTSG--------------TVRRAGGARVAYVPQRS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 MVSlnplHNLEKQLYEVLSL----HRGMRRE---AARAEILTCLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTR 174
Cdd:NF040873 65 EVP----DSLPLTVRDLVAMgrwaRRGLWRRltrDDRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2551249897 175 PELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIV 220
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELV 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-237 |
1.29e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 81.30 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVgfRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHANEQT 85
Cdd:cd03369 7 IEVENLSV--RYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRdvrgNKIAMIFQEPMV-------SLNPL-HNLEKQLYEVLSLHRGmrreaaraeiltcldrvgirqaakrladyPHQL 157
Cdd:cd03369 80 LR----SSLTIIPQDPTLfsgtirsNLDPFdEYSDEEIYGALRVSEG-----------------------------GLNL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKLaDTVAVMQNGQCVE 237
Cdd:cd03369 127 SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
306-518 |
1.48e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDG-----LALHTLNRRQL--LPvrhriqvvfqdPNSSLNP 377
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDedislLPLHARARRGIgyLP-----------QEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLQIIEEGLRVHQpTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK10895 92 RLSVYDNLMAVLQIRD-DLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 458 RTVQAQILTLLKSLQEkHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:PRK10895 170 PISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-238 |
1.70e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 84.23 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHG 75
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIagfetPD------SGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 76 ESLLHAN-EQtlRDVRgnkiaMIFQEpmVSLNPlHnleKQLYEVLSLhrGMR-REAARAEILTcldRVgiRQAAK--RLA 151
Cdd:PRK09452 76 QDITHVPaEN--RHVN-----TVFQS--YALFP-H---MTVFENVAF--GLRmQKTPAAEITP---RV--MEALRmvQLE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 152 DY----PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTV 227
Cdd:PRK09452 136 EFaqrkPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRI 215
|
250
....*....|.
gi 2551249897 228 AVMQNGQcVEQ 238
Cdd:PRK09452 216 VVMRDGR-IEQ 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-234 |
1.90e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLRDVRgNKIAMIFQEp 101
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLICGIERPS----AGKIWFSGHDITRLKNREVPFLR-RQIGMIFQD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 mvslnplHNL--EKQLYEVLSLH---RGMRREAARAEILTCLDRVGIRQAAKrlaDYPHQLSGGERQRVMIAMALLTRPE 176
Cdd:PRK10908 88 -------HHLlmDRTVYDNVAIPliiAGASGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 177 LLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-248 |
2.17e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYpSGDIRFHGESLLHANEQTLRdvrgNKIAMIFQEPMVslnp 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----Y-QGSLKINGIELRELDPESWR----KHLSWVGQNPQL---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 108 lhnLEKQLYEVLSLHRGmrrEAARAEILTCLDRVGIRQAAKRLA---DYPHQ-----LSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK11174 435 ---PHGTLRDNVLLGNP---DASDEQLQQALENAWVSEFLPLLPqglDTPIGdqaagLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 180 ADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVKKLaDTVAVMQNGQCVEQNRAAQLLTAP 248
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQT--TLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
311-509 |
2.39e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 85.32 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 311 PGETLGLVGESGSGKSTTGLALLRLITSQGsivFDGLALhTLNRRQLLPVRHRIQVVFQDpnSSLNPRLSVLQ--IIEEG 388
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTIL-ANNRKPTKQILKRTGFVTQD--DILYPHLTVREtlVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 389 LRVHQpTLSAEQREAQVKAVMAEVGL----DSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PLN03211 167 LRLPK-SLTKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 465 LTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-234 |
2.43e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 79.57 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSvgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLlhanEQT 85
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--PT---SGRVRLDGADI----SQW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGNKIAMIFQEpmvslnplhnlekqlyevLSLHRGMRREAAraeiltcldrvgirqaakrladyphqLSGGERQRV 165
Cdd:cd03246 70 DPNELGDHVGYLPQD------------------DELFSGSIAENI--------------------------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVkKLADTVAVMQNGQ 234
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-247 |
2.55e-17 |
|
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: 81.05 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 30 LRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQtlrdvrgnkIAMIFQEPMVSLNPLH 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPA-----KGTVKVAGASPGKGWRH---------IGYVPQRHEFAWDFPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 110 NLEKQLYEVLSLHRGMRREAARAE---ILTCLDRVGIRQaakrLADYP-HQLSGGERQRVMIAMALLTRPELLIADEPTT 185
Cdd:TIGR03771 67 SVAHTVMSGRTGHIGWLRRPCVADfaaVRDALRRVGLTE----LADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFT 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 186 ALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVaVMQNGQCVEQNRAAQLLTA 247
Cdd:TIGR03771 143 GLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDP 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-217 |
2.71e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLlhaneq 84
Cdd:PRK11248 1 MLQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKT----TLLNLI-AGFVPYQHGSITLDGKPV------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 tlrDVRGNKIAMIFQEPmvSLNPLHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIRQAAKRladYPHQLSGGERQR 164
Cdd:PRK11248 66 ---EGPGAERGVVFQNE--GLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNL 217
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-245 |
2.87e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLlpsppvvYP--SGDIRFHGESLlhaNEQT 85
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF-------YDidEGEILLDGHDL---RDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEpmVSL------NPLHNLEKQLYevlslhrgmrreaARAEIltcldrvgirQAAKRLA---DYPHQ 156
Cdd:PRK11176 412 LASLR-NQVALVSQN--VHLfndtiaNNIAYARTEQY-------------SREQI----------EEAARMAyamDFINK 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 ---------------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVK 221
Cdd:PRK11176 466 mdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIE 543
|
250 260
....*....|....*....|....
gi 2551249897 222 KlADTVAVMQNGQCVEQNRAAQLL 245
Cdd:PRK11176 544 K-ADEILVVEDGEIVERGTHAELL 566
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
306-505 |
3.51e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGlalHTLNRrqlLPVRHR---IQVVFQDPNSSLNP 377
Cdd:COG1101 26 NLTIEEGDFVTVIGSNGAGKST----LLNAIAgslppDSGSILIDG---KDVTK---LPEYKRakyIGRVFQDPMMGTAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSvlqiIEE------------GLRvhqPTLSAEQREaQVKAVMAEVGLDSETRHRYPAEF-SGGQRQRIAIARALILKP 444
Cdd:COG1101 96 SMT----IEEnlalayrrgkrrGLR---RGLTKKRRE-LFRELLATLGLGLENRLDTKVGLlSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 445 SLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-200 |
4.36e-17 |
|
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: 79.84 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLP--SPPVvypSGDIRFHGESLlhaneQTLRDVRGNKIAMIFQ 99
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKT----TLLRILAglSPPL---AGRVLLNGGPL-----DFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 100 EPMV--SLNPLHNLekqlyevlslhRGMRREAARAEILTCLDRVGIRQAAKRLAdypHQLSGGERQRVMIAMALLTRPEL 177
Cdd:cd03231 81 APGIktTLSVLENL-----------RFWHADHSDEQVEEALARVGLNGFEDRPV---AQLSAGQQRRVALARLLLSGRPL 146
|
170 180
....*....|....*....|...
gi 2551249897 178 LIADEPTTALDVSVQAQILQLLR 200
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMA 169
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-248 |
4.93e-17 |
|
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: 80.40 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQt 85
Cdd:TIGR04406 2 LVAENLIKSYKK----RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILIDGQDITHLPMH- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGnkIAMIFQEPMV--SLNPLHNLEKqlyeVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLAdypHQLSGGERQ 163
Cdd:TIGR04406 72 ERARLG--IGYLPQEASIfrKLTVEENIMA----VLEIRKDLDRAEREERLEALLEEFQISHLRDNKA---MSLSGGERR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQ 243
Cdd:TIGR04406 143 RVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLK-ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAE 221
|
....*
gi 2551249897 244 LLTAP 248
Cdd:TIGR04406 222 IVANE 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
306-521 |
6.41e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLNRRQLlpVRHRIQVVFQDPNSSlnpRLS 380
Cdd:PRK10575 31 SLTFPAGKVTGLIGHNGSGKST----LLKMLgrhqpPSEGEILLDAQPLESWSSKAF--ARKVAYLPQQLPAAE---GMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPTL---SAEQREaQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK10575 102 VRELVAIGRYPWHGALgrfGAADRE-KVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 458 RTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFNAP--QQAY 521
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGEtlEQIY 245
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
306-508 |
6.65e-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: 80.38 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALL---RLITSQGSIVFDG---LALHTLNRrqllpVRHRIQVVFQDPNSSlnPRL 379
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGqdlLELEPDER-----ARAGLFLAFQYPEEI--PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVH-----QPTLSAEQREAQVKAVMAEVGLDSETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:TIGR01978 93 SNLEFLRSALNARrsargEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 454 SSLD----RTVQAQIltllKSLQEKHRlAYIFISHDLHVVRALCHQVI-VLRQGEVVEQG 508
Cdd:TIGR01978 173 SGLDidalKIVAEGI----NRLREPDR-SFLIITHYQRLLNYIKPDYVhVLLDGRIVKSG 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
273-505 |
6.67e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFPIRKGILKrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKST--TGLALLRLITSqGSIVFDGLALH 350
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVE-------VLKGISLDIYAGEMVAIVGASGSGKSTlmNILGCLDKPTS-GTYRVAGQDVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 351 TLNRRQLLPVRHR-IQVVFQdpNSSLNPRLSVLQIIEeglrvhQPTLSA----EQREAQVKAVMAEVGLdSETRHRYPAE 425
Cdd:PRK10535 74 TLDADALAQLRREhFGFIFQ--RYHLLSHLTAAQNVE------VPAVYAglerKQRLLRAQELLQRLGL-EDRVEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEK-HRLayIFISHDLHVVrALCHQVIVLRQGEV 504
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTV--IIVTHDPQVA-AQAERVIEIRDGEI 221
|
.
gi 2551249897 505 V 505
Cdd:PRK10535 222 V 222
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-201 |
7.83e-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: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVgfrqQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLP--SPPVvypSGDIRFHGEsllHANE 83
Cdd:TIGR01189 1 LAARNLAC----SRGERMLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILAglLRPD---SGEVRWNGT---PLAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QtlRDVRGNKIAMIFQEPMV--SLNPLHNLekQLYEvlSLHRGMRREaaraeILTCLDRVGIRQAAKRLAdypHQLSGGE 161
Cdd:TIGR01189 67 Q--RDEPHENILYLGHLPGLkpELSALENL--HFWA--AIHGGAQRT-----IEDALAAVGLTGFEDLPA---AQLSAGQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2551249897 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-237 |
8.89e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.73 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSVTALSIL-RllPSPPVVypSGDIRFHGESLLH--AN 82
Cdd:COG0396 1 LEIKNLHVSVEGKE----ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgH--PKYEVT--SGSILLDGEDILElsPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EqtlrdvRGNK-IAMIFQEPM----VSLNPLhnlekqLYEVLSLHRG--MRREAARAEILTCLDRVGIRQA-AKRLADYp 154
Cdd:COG0396 73 E------RARAgIFLAFQYPVeipgVSVSNF------LRTALNARRGeeLSAREFLKLLKEKMKELGLDEDfLDRYVNE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 hQLSGGERQRVMIA-MALLtRPELLIADEPTTALDV-SVQAqILQLLRELQHElNMGLLFITHN---LSIVKklADTVAV 229
Cdd:COG0396 140 -GFSGGEKKRNEILqMLLL-EPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYqriLDYIK--PDFVHV 213
|
....*...
gi 2551249897 230 MQNGQCVE 237
Cdd:COG0396 214 LVDGRIVK 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
307-515 |
9.12e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 307 FSLRPGETLGLVGESGSGKSTTGLALLRLIT---SQGSIVfdGLALHTLNR-----RQLLPVRHRIQVVFQDPNssLNPR 378
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHI--ELLGRTVQRegrlaRDIRKSRANTGYIFQQFN--LVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVLQIIEEGLRVHQPT-------LSAEQREAQVKAvMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:PRK09984 101 LSVLENVLIGALGSTPFwrtcfswFTREQKQRALQA-LTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 452 PTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-248 |
1.23e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 79.12 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHANEQT 85
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-----VKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 lRDVRGnkIAMIFQEPMV--SLNPLHNLEKQLyEVLSLHRGMRREaaRAEILtcLDRVGIRQAAKRLADyphQLSGGERQ 163
Cdd:cd03218 72 -RARLG--IGYLPQEASIfrKLTVEENILAVL-EIRGLSKKEREE--KLEEL--LEEFHITHLRKSKAS---SLSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALD-VSVQaQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAA 242
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
....*.
gi 2551249897 243 QLLTAP 248
Cdd:cd03218 219 EIAANE 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
306-468 |
1.32e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLnrrqllpvRHRIQVVFQDPNSSLNPRLS 380
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTT----LLRLIagllpPAAGTIKLDGGDIDDP--------DVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQptlsaeQREAQVKAVMAEVGLDSETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK13539 90 VAENLEFWAAFLG------GEELDIAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*...
gi 2551249897 461 QAQILTLL 468
Cdd:PRK13539 163 VALFAELI 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
273-504 |
1.36e-16 |
|
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: 77.86 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 273 APLLEVEKLRVAFPIRkGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLAL--LRLITSqGSIVFDGLALH 350
Cdd:cd03215 2 EPVLEVRGLSVKGAVR-DV--------------SFEVRAGEIVGIAGLVGNGQTELAEALfgLRPPAS-GEITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 351 TLNRRQLlpVRHRIQVVFQDPNSS-LNPRLSVLQIIeeGLRVHqptlsaeqreaqvkavmaevgldsetrhrypaeFSGG 429
Cdd:cd03215 66 RRSPRDA--IRAGIAYVPEDRKREgLVLDLSVAENI--ALSSL---------------------------------LSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 430 QRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKhRLAYIFISHDLHVVRALCHQVIVLRQGEV 504
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
306-470 |
1.49e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.17 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLN---RRQLLPVRHRiqvvfqdpnSSLNP 377
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTT----LLRILAgllrpDSGEVRWNGTPLAEQRdepHENILYLGHL---------PGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLqiieEGLRVHQPTLSAEQREaqVKAVMAEVGLDSETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:TIGR01189 87 ELSAL----ENLHFWAAIHGGAQRT--IEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|...
gi 2551249897 458 RTVQAQILTLLKS 470
Cdd:TIGR01189 160 KAGVALLAGLLRA 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
274-508 |
1.55e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFD 345
Cdd:PRK15439 10 PLLCARSISKQYsgvEVLKGI--------------DFTLHAGEVHALLGGNGAGKST----LMKIIAgivppDSGTLEIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 346 GLALHTLNrrqllPVR-HR--IQVVFQDPNssLNPRLSVLQIIEEGLRVHQPTlsaeqrEAQVKAVMAEVG----LDSET 418
Cdd:PRK15439 72 GNPCARLT-----PAKaHQlgIYLVPQEPL--LFPNLSVKENILFGLPKRQAS------MQKMKQLLAALGcqldLDSSA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 419 rhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIV 498
Cdd:PRK15439 139 -----GSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISV 212
|
250
....*....|
gi 2551249897 499 LRQGEVVEQG 508
Cdd:PRK15439 213 MRDGTIALSG 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
1.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGF-RQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRF-------HGE 76
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-----YGTIQVgdiyigdKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 77 SLLHANEQTLRDVRGNK-----IAMIFQEPMVSLNPlHNLEKQL-YEVLSLhrGMRREAARAEILTCLDRVGIRQAAkrL 150
Cdd:PRK13631 96 NHELITNPYSKKIKNFKelrrrVSMVFQFPEYQLFK-DTIEKDImFGPVAL--GVKKSEAKKLAKFYLNKMGLDDSY--L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 151 ADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVM 230
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*....
gi 2551249897 231 QNGQCVEQNRAAQLLTAPT 249
Cdd:PRK13631 250 DKGKILKTGTPYEIFTDQH 268
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-272 |
1.67e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 9 ENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH-ANEQTLR 87
Cdd:PRK10253 11 EQLTLGYGK----YTVAENLTVEIPDGHFTAIIGPNGCGKS-TLLRTLSRLMTPA----HGHVWLDGEHIQHyASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 dvrgnKIAMIFQEPM----VSLNPLhnLEKQLYEVLSLHRGMRREAARAeILTCLDRVGIRQAAKRLADyphQLSGGERQ 163
Cdd:PRK10253 82 -----RIGLLAQNATtpgdITVQEL--VARGRYPHQPLFTRWRKEDEEA-VTKAMQATGITHLADQSVD---TLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQ 243
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
250 260 270
....*....|....*....|....*....|...
gi 2551249897 244 LLTAP----THPYTKKLLNSEPSGDPVPLPVGQ 272
Cdd:PRK10253 231 IVTAElierIYGLRCMIIDDPVAGTPLVVPLGR 263
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
156-457 |
1.80e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 81.98 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 236 VEQNRAAQLLTAPTHP---YTKKLLNS------EPSGDPvPLPVGQaPLLEVEKLRVAFPIRKgILKRvvdhnvvvndVS 306
Cdd:PRK10938 214 AETGEREEILQQALVAqlaHSEQLEGVqlpepdEPSARH-ALPANE-PRIVLNNGVVSYNDRP-ILHN----------LS 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 307 FSLRPGETLGLVGESGSGKSTtglaLLRLITS---QGSivfdGLALHTLNRRQ-----LLPVRHRIQVVfqdpNSSL--N 376
Cdd:PRK10938 281 WQVNPGEHWQIVGPNGAGKST----LLSLITGdhpQGY----SNDLTLFGRRRgsgetIWDIKKHIGYV----SSSLhlD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 377 PRLS--VLQIIEEG----LRVHQPTLSAEQREAQvkAVMAEVGLDSETRHRYPAEFSGGQrQRIA-IARALILKPSLIIL 449
Cdd:PRK10938 349 YRVStsVRNVILSGffdsIGIYQAVSDRQQKLAQ--QWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLIL 425
|
....*...
gi 2551249897 450 DEPTSSLD 457
Cdd:PRK10938 426 DEPLQGLD 433
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-234 |
2.07e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVgfrQQETVRTVVNTLSLRVDAGQTLALVGESGSGKS--VTALSILRllpsPPVvypSGDIRFHGESLLHA 81
Cdd:COG3845 256 VVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSelAEALAGLR----PPA---SGSIRLDGEDITGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 neqTLRDVRGNKIAMIFQEPMV-----SLNPLHNLekqlyeVLSLHRgmRREAARAEILtclDRVGIRQAAKRL-ADY-- 153
Cdd:COG3845 326 ---SPRERRRLGVAYIPEDRLGrglvpDMSVAENL------ILGRYR--RPPFSRGGFL---DRKAIRAFAEELiEEFdv 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 ----PHQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLAD 225
Cdd:COG3845 392 rtpgPDTparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSD 470
|
....*....
gi 2551249897 226 TVAVMQNGQ 234
Cdd:COG3845 471 RIAVMYEGR 479
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-233 |
2.09e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQetvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL-- 78
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKT-TVFNCLTGFYKPT----GGTILLRGQHIeg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 79 -------LHANEQTLRDVRgnkiamIFQEPMVSLNPL---H-----NLEKQLYEVLSLHRGMRREAARAeiLTCLDRVGI 143
Cdd:PRK11300 72 lpghqiaRMGVVRTFQHVR------LFREMTVIENLLvaqHqqlktGLFSGLLKTPAFRRAESEALDRA--ATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 144 RQAAKRLADyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKL 223
Cdd:PRK11300 144 LEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGI 220
|
250
....*....|
gi 2551249897 224 ADTVAVMQNG 233
Cdd:PRK11300 221 SDRIYVVNQG 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-236 |
2.23e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.40 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLL-HANEQTLRDVRgNKIAMIFQEPmvsln 106
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKS-TIMQLLNGLHVPT----QGSVRVDDTLITsTSKNKDIKQIR-KKVGLVFQFP----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 107 plhnlEKQLYEVLSL--------HRGMRREAARAEILTCLDRVGIrqaAKRLADY-PHQLSGGERQRVMIAMALLTRPEL 177
Cdd:PRK13649 95 -----ESQLFEETVLkdvafgpqNFGVSQEEAEALAREKLALVGI---SESLFEKnPFELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 178 LIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK13649 167 LVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
317-508 |
2.26e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 317 LVGESGSGKSTtglaLL----RLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPNssLNPRLSVLQIIEEGlRV 391
Cdd:COG4604 32 LIGPNGAGKST----LLsmisRLLPpDSGEVLVDGLDVATTPSREL---AKRLAILRQENH--INSRLTVRELVAFG-RF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 392 --HQPTLSAEQREAqVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLK 469
Cdd:COG4604 102 pySKGRLTAEDREI-IDEAIAYLDLE-DLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLR 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 2551249897 470 SLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:COG4604 180 RLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-217 |
2.30e-16 |
|
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: 82.02 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVVntlSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANE 83
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGV---SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVrgnkIAMIFQEPmvslnplHNLEKQLYEVLSLHRGmrrEAARAEILTCLDRVGIRQAAKRLADYPH-------- 155
Cdd:TIGR02868 405 DEVRRR----VSVCAQDA-------HLFDTTVRENLRLARP---DATDEELWAALERVGLADWLRALPDGLDtvlgegga 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELnmGLLFITHNL 217
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
25-267 |
2.56e-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: 81.86 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHANEQTLRdvrgNKIAMIFQEPMVs 104
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKT-TLINLLQRVYDPTV----GQILIDGIDINTVTRESLR----KSIATVFQDAGL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 105 lnplhnLEKQLYEVLSLHRGMRR-----EAARAEILTCLDRVGIRQAAKRLADYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:TIGR01192 421 ------FNRSIRENIRLGREGATdeevyEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 180 ADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQLLTAPTHPY----TKK 255
Cdd:TIGR01192 495 LDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRN-ADLVLFLDQGRLIEKGSFQELIQKDGRFYkllrRSG 571
|
250
....*....|..
gi 2551249897 256 LLNSEPSGDPVP 267
Cdd:TIGR01192 572 LLTNQPATKPLR 583
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-249 |
2.57e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 17 QQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALS-ILRLLPSppvvypSGDIRFHGESLLHANEQTLRDVRgnkiA 95
Cdd:PRK03695 4 NDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKS-TLLArMAGLLPG------SGSIQFAGQPLEAWSAAELARHR----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 96 MIFQepmvSLNPLHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIrqaAKRLADYPHQLSGGERQRVMIAMALL--- 172
Cdd:PRK03695 73 YLSQ----QQTPPFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVLqvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 173 --TRPE--LLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAP 248
Cdd:PRK03695 146 pdINPAgqLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
.
gi 2551249897 249 T 249
Cdd:PRK03695 225 N 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
306-518 |
2.78e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITS-QGSIVFDGLALHTL--NRR-QL----LPvrhriqvvfQDPnsSLNP 377
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEDITHLpmHKRaRLgigyLP---------QEA--SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:COG1137 92 KLTVEDNILAVLELRK--LSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 458 RTVQAQILTLLKSLqeKHRLAYIFIShDlHVVR---ALCHQVIVLRQGEVVEQGQCEHVFNAPQ 518
Cdd:COG1137 169 PIAVADIQKIIRHL--KERGIGVLIT-D-HNVRetlGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
306-509 |
3.50e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRqllpVRHRIQVVFQDPNssLNPRLSVlqi 384
Cdd:PRK13536 61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARL----ARARIGVVPQFDN--LDLEFTV--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 iEEGLRVHQP--TLSAEQREAQVKAVMAEVGLDSETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:PRK13536 132 -RENLLVFGRyfGMSTREIEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 463 QILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:PRK13536 210 LIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
309-514 |
4.49e-16 |
|
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: 78.03 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 309 LRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDG-----LALHTLnrrqllpvRHRIQVVFQDP-------NSSL 375
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVdIFDGKIVIDGidiskLPLHTL--------RSRLSIILQDPilfsgsiRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 NPRLSVL-QIIEEGLRVHQPTLSAEQREAQVKAVMAEVGldsetrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:cd03288 116 DPECKCTdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 455 SLDRTVQaQILTLLKSLQEKHRlAYIFISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVF 514
Cdd:cd03288 186 SIDMATE-NILQKVVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-234 |
5.56e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLS-VGFRQqetvrtvvntLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGesllha 81
Cdd:PRK15439 266 APVLTVEDLTgEGFRN----------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR-----GGRIMLNG------ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 neqtlRDVRGNKIAMIFQEPMVSL------------NPLH-NLEKQLYEVLSLHRGMRREAARaeiltcLDR----VGIR 144
Cdd:PRK15439 325 -----KEINALSTAQRLARGLVYLpedrqssglyldAPLAwNVCALTHNRRGFWIKPARENAV------LERyrraLNIK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 145 -----QAAKRLadyphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSI 219
Cdd:PRK15439 394 fnhaeQAARTL-------SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEE 465
|
250
....*....|....*
gi 2551249897 220 VKKLADTVAVMQNGQ 234
Cdd:PRK15439 466 IEQMADRVLVMHQGE 480
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-233 |
5.76e-16 |
|
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: 77.37 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANEQTLR 87
Cdd:cd03267 20 IGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKT-TTLKILSGLLQPT----SGEVRVAGLVPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 dvrgnKIAMIFQE---------PMVSLNplhnLEKQLYEVLSLHRGMRREAArAEILTCldrvgirqaaKRLADYP-HQL 157
Cdd:cd03267 95 -----RIGVVFGQktqlwwdlpVIDSFY----LLAAIYDLPPARFKKRLDEL-SELLDL----------EELLDTPvRQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-234 |
6.76e-16 |
|
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: 76.74 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyPSGdirfhGESLLHANEQTLRDVR--GNKIAMIFQ 99
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ------PQG-----GQVLLDGKPISQYEHKylHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 100 EPMVSLNPLHNleKQLYEVLSLHRGMRREAAraeiltclDRVGIRQAAKRLADYPH--------QLSGGERQRVMIAMAL 171
Cdd:cd03248 96 EPVLFARSLQD--NIAYGLQSCSFECVKEAA--------QKAHAHSFISELASGYDtevgekgsQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQHelNMGLLFITHNLSIVKKlADTVAVMQNGQ 234
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-237 |
8.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLpsppVVYPSGDIrFHGESLLHANEQTLRDVRG--NKIAMIFQEPM 102
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKS-TMIQLTNGL----IISETGQT-IVGDYAIPANLKKIKEVKRlrKEIGLVFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 VSLNPlHNLEKQLyEVLSLHRGMRREAARAEILTCLDRVGI-RQAAKRladYPHQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:PRK13645 101 YQLFQ-ETIEKDI-AFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 182 EPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-236 |
8.98e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESllhaNEQTLRDVRgNKIAMIFQEPmvslnp 107
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 108 lhnlEKQLYEVLSL--------HRGMRREAARAEILTCLDRVGIRQaaKRLADYPHQLSGGERQRVMIAMALLTRPELLI 179
Cdd:PRK13643 94 ----ESQLFEETVLkdvafgpqNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 180 ADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
306-485 |
1.01e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITS-----QGSIVFDGLALHTLNrrqllPVRHRIQV--VFQDP---NSSL 375
Cdd:PRK10247 27 SFSLRAGEFKLITGPSGCGKST----LLKIVASlisptSGTLLFEGEDISTLK-----PEIYRQQVsyCAQTPtlfGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 NPRLsvlqIIEEGLRVHQPtlsaeqREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PRK10247 98 YDNL----IFPWQIRNQQP------DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190
....*....|....*....|....*....|
gi 2551249897 456 LDRTVQAQILTLLKSLQEKHRLAYIFISHD 485
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
308-497 |
1.01e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.35 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 308 SLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLAlhtlnRRQLLPVRHRIQVVFQdpnsslnprLSVL 382
Cdd:NF040873 14 TIPAGSLTAVVGPNGSGKST----LLKVLAgvlrpTSGTVRRAGGA-----RVAYVPQRSEVPDSLP---------LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEEGLRVHQPT---LSAEQReAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRT 459
Cdd:NF040873 76 DLVAMGRWARRGLwrrLTRDDR-AAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2551249897 460 VQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVI 497
Cdd:NF040873 154 SRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVL 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
306-503 |
1.08e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.02 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITSQgsivfdglalhtlnrrqllpvrhriqvvfqdpnssLNPrlsvlqii 385
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKST----LLKLIAGE-----------------------------------LEP-------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 EEGlrvhqptlsaeqreaqvkavmaEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL 465
Cdd:cd03221 53 DEG----------------------IVTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 2551249897 466 TLLKSLQEkhrlAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:cd03221 111 EALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
306-516 |
1.08e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALHTLNRRQLlpvrhrIQVVFQDPNSSLNPRLSVLQI 384
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVrLASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTL---SAEQREAqVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQ 461
Cdd:PRK15056 101 VMMGRYGHMGWLrraKKRDRQI-VTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 462 AQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRqGEVVEQGQCEHVFNA 516
Cdd:PRK15056 179 ARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTA 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-486 |
1.53e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 35 GQTLALVGESGSGKSvTALSIL--RLLP------SPP----VVYpsgdiRFHGESLlhaneQT-LRDVRGN------KIA 95
Cdd:PRK13409 99 GKVTGILGPNGIGKT-TAVKILsgELIPnlgdyeEEPswdeVLK-----RFRGTEL-----QNyFKKLYNGeikvvhKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 96 MIFQEPMVSLNPLHNLEKQLYEvlslhRGMRRE-AARAEILTCLDRvGIRQaakrladyphqLSGGERQRVMIAMALLTR 174
Cdd:PRK13409 168 YVDLIPKVFKGKVRELLKKVDE-----RGKLDEvVERLGLENILDR-DISE-----------LSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 175 PELLIADEPTTALDVSVQAQILQLLRELQHELNMglLFITHNLSIVKKLADTVAVMQnGQcveqnraaqlltaP------ 248
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHDLAVLDYLADNVHIAY-GE-------------Pgaygvv 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 249 THPY-TKKLLNSEPSG-----------DPV-----PLPVGQ--APLLEVEKLRVAFPirkgilkrvvdhnvvvndvSFSL 309
Cdd:PRK13409 295 SKPKgVRVGINEYLKGylpeenmrirpEPIefeerPPRDESerETLVEYPDLTKKLG-------------------DFSL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 310 -------RPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDglalhtlnrrqlLPVRHRIQVVFQDPNSSlnp 377
Cdd:PRK13409 356 eveggeiYEGEVIGIVGPNGIGKTT----FAKLLAgvlkpDEGEVDPE------------LKISYKPQYIKPDYDGT--- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 rlsvlqiIEEGLRVHQPTLSAEQREAQV-KAVMAEVGLDSETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK13409 417 -------VEDLLRSITDDLGSSYYKSEIiKPLQLERLLDKNVK-----DLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
490 500 510
....*....|....*....|....*....|..
gi 2551249897 457 DrtVQAQILT--LLKSLQEKHRLAYIFISHDL 486
Cdd:PRK13409 485 D--VEQRLAVakAIRRIAEEREATALVVDHDI 514
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-236 |
1.75e-15 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 75.70 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 7 AIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaneQTL 86
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS-TLLKLLAGLYKPT----SGSVLLDGTDI-----RQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 87 --RDVRGNkIAMIFQEPMVslnplhnLEKQLYEVLSLHRGmrrEAARAEILTCLDRVGIRQAAKRLAD-YPHQ------- 156
Cdd:cd03245 72 dpADLRRN-IGYVPQDVTL-------FYGTLRDNITLGAP---LADDERILRAAELAGVTDFVNKHPNgLDLQigergrg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVkKLADTVAVMQNGQCV 236
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT--LIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-250 |
2.26e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPV---VYPSGDIRFHGESLLHA 81
Cdd:PRK13547 1 MLTADHLHVARRH----RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAprgARVTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NEQTLRDVRgnkiAMIFQ--EPMVSLNplhnlekqLYEVLSLhrGMRREAARAEILTCLDRvGIRQAAKRLADYP----- 154
Cdd:PRK13547 77 DAPRLARLR----AVLPQaaQPAFAFS--------AREIVLL--GRYPHARRAGALTHRDG-EIAWQALALAGATalvgr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 --HQLSGGERQRVMIAMAL---------LTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKL 223
Cdd:PRK13547 142 dvTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARH 221
|
250 260
....*....|....*....|....*..
gi 2551249897 224 ADTVAVMQNGQCVEQNRAAQLLTaPTH 250
Cdd:PRK13547 222 ADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
306-508 |
2.93e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSLnpRLSV 381
Cdd:PTZ00243 1330 SFRIAPREKVGIVGRTGSGKSTLLLTFMRMVeVCGGEIRVNGREIGAYGLREL---RRQFSMIPQDPvlfDGTV--RQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 lqiieeglrvhQPTLSAEqrEAQVKAVMAEVGLdsetRHRYPAE--------------FSGGQRQRIAIARALILKPS-L 446
Cdd:PTZ00243 1405 -----------DPFLEAS--SAEVWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARALLKKGSgF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 447 IILDEPTSS----LDRTVQAQILTLLKslqekhrlAY--IFISHDLHVVrALCHQVIVLRQGEVVEQG 508
Cdd:PTZ00243 1468 ILMDEATANidpaLDRQIQATVMSAFS--------AYtvITIAHRLHTV-AQYDKIIVMDHGAVAEMG 1526
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
306-515 |
2.99e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRqlLPVRHRIQVVFQDpnSSLNPRLS 380
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKST----LMKVLSgihepTKGTITINNINYNKLDHK--LAAQLGIGIIYQE--LSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPTLSA---EQREAQVKAVMA--EVGL--DSETRhryPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
Cdd:PRK09700 97 VLENLYIGRHLTKKVCGVniiDWREMRVRAAMMllRVGLkvDLDEK---VANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 454 SSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFN 515
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-245 |
3.87e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvyP-SGDIRFHGESL---- 78
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK------PdSGRIFLDGEDIthlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 79 LHaneqtLRDVRGnkIAMIFQEPMV--SLNPLHNLEKQLyEVLSLHRGMRREaaRAEILtcLDRVGIRQAAKRLADyphQ 156
Cdd:COG1137 72 MH-----KRARLG--IGYLPQEASIfrKLTVEDNILAVL-ELRKLSKKEREE--RLEEL--LEEFGITHLRKSKAY---S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVqAQILQLLRELQhELNMGLLfIT-HN----LSIVkklaDTVAVM 230
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVL-ITdHNvretLGIC----DRAYII 209
|
250
....*....|....*
gi 2551249897 231 QNGQCVEQNRAAQLL 245
Cdd:COG1137 210 SEGKVLAEGTPEEIL 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
35-245 |
4.60e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 35 GQTLALVGESGSGKSvTALSILRLLPSPPVVYpSGDIRFHGESLlHANEQTLRDvrgnkiAMIFQEPMvsLNPLHNLEKQ 114
Cdd:TIGR00955 51 GELLAVMGSSGAGKT-TLMNALAFRSPKGVKG-SGSVLLNGMPI-DAKEMRAIS------AYVQQDDL--FIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 115 LY--EVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLADYPHQ---LSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
Cdd:TIGR00955 120 LMfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 190 SVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLL 245
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-238 |
5.10e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.16 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHANEQTLRdvrgNKIAMIFQEPM---- 102
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQ------RGRVKVMGREVNAENEKWVR----SKVGLVFQDPDdqvf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 -------VSLNPLhNLEKQLYEVLSlhrgmRREAAraeiltcLDRVGIRQAAKRLadyPHQLSGGERQRVMIAMALLTRP 175
Cdd:PRK13647 94 sstvwddVAFGPV-NMGLDKDEVER-----RVEEA-------LKAVRMWDFRDKP---PYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 176 ELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQ 238
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
306-508 |
6.27e-15 |
|
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: 74.23 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI--------TSQGSIVFDGLALHtlnrRQLlpVRHRIQVVFQDPNssLNP 377
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTT----LLDAIsgrvegggTTSGQILFNGQPRK----PDQ--FQKCVAYVRQDDI--LLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVlqiiEEGLR-VHQPTLSAEQREAQVKAVMAEVGL----DSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:cd03234 95 GLTV----RETLTyTAILRLPRKSSDAIRKKRVEDVLLrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 453 TSSLDRTVQAQILTLLKSLQEKHRLAYIFIshdlHVVRA----LCHQVIVLRQGEVVEQG 508
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTI----HQPRSdlfrLFDRILLLSSGEIVYSG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-247 |
7.71e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLsvgfRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTalsiLRLLPSppVVYP-SGDIRFHGESLL 79
Cdd:PRK13537 3 MSVAPIDFRNV----EKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTT----LRMLLG--LTHPdAGSISLCGEPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANEQTLRdvrgnKIAMIFQepMVSLNPLHNLEKQLyEVLSLHRGMRREAARAEILTCLDRVGIRQAAkrlaDYP-HQLS 158
Cdd:PRK13537 73 SRARHARQ-----RVGVVPQ--FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKA----DAKvGELS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqheLNMG--LLFITHNLSIVKKLADTVAVMQNGQCV 236
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL---LARGktILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
250
....*....|.
gi 2551249897 237 EQNRAAQLLTA 247
Cdd:PRK13537 218 AEGAPHALIES 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-215 |
8.08e-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: 72.19 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVgfrQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL----PsppvvYPSGDIRFHgesllha 81
Cdd:cd03223 1 IELENLSL---ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRALaglwP-----WGSGRIGMP------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 neqtlrdvRGNKIAMIFQEPMVslnPLHNLEKQLYevlslhrgmrreaaraeiltcldrvgirqaakrladYP--HQLSG 159
Cdd:cd03223 62 --------EGEDLLFLPQRPYL---PLGTLREQLI------------------------------------YPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhelnMGLLFITH 215
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
306-529 |
8.82e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLI-TSQGSIVFDGlalHTLNRRQLLPVRHRIQVVFQDPN-SSLNPRLSVLQ 383
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVeLEKGRIMIDD---CDVAKFGLTDLRRVLSIIPQSPVlFSGTVRFNIDP 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 384 IIEEglrvHQPTLSAEQREAQVKAVMAE--VGLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQ 461
Cdd:PLN03232 1333 FSEH----NDADLWEALERAHIKDVIDRnpFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 462 AQIltlLKSLQEKHR-LAYIFISHDLHVVRAlCHQVIVLRQGEVVEqgqcehvFNAPQQAYTRQLLALS 529
Cdd:PLN03232 1408 SLI---QRTIREEFKsCTMLVIAHRLNTIID-CDKILVLSSGQVLE-------YDSPQELLSRDTSAFF 1465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
307-505 |
9.67e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.91 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 307 FSLRPGETLGLVGESGSGKSTtglaLLRLITS----------------------------QGSiVFDGLALHTLNRRQLL 358
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKST----LMKILNGevllddgriiyeqdlivarlqqdpprnvEGT-VYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 359 PVRHRI-QVVFQDPNSSLNPRLSVLQIIEEglrvHQptlSAEQREAQVKAVMAEVGLDSETRHrypAEFSGGQRQRIAIA 437
Cdd:PRK11147 99 KRYHDIsHLVETDPSEKNLNELAKLQEQLD----HH---NLWQLENRINEVLAQLGLDPDAAL---SSLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 438 RALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEkhrlAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
306-484 |
1.11e-14 |
|
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: 71.80 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVfdglalhtlnrrqlLPVRHRIQVVFQDPnssLNPRLS 380
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSS----LFRALAglwpwGSGRIG--------------MPEGEDLLFLPQRP---YLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIeeglrvhqptlsaeqreaqvkavmaevgldsetrhRYP--AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDR 458
Cdd:cd03223 80 LREQL-----------------------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*.
gi 2551249897 459 TVQAQILTLLKslqeKHRLAYIFISH 484
Cdd:cd03223 125 ESEDRLYQLLK----ELGITVISVGH 146
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-237 |
1.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRfHGESLlha 81
Cdd:COG0488 314 KVLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKS-TLLKLLagELEPD------SGTVK-LGETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 neqtlrdvrgnKIAMIFQEPMvSLNPlhnlEKQLYEVLslhRGMRREAARAEILTCLDRVGIR--QAAKRLADyphqLSG 159
Cdd:COG0488 379 -----------KIGYFDQHQE-ELDP----DKTVLDEL---RDGAPGGTEQEVRGYLGRFLFSgdDAFKPVGV----LSG 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhelnmG-LLFITHNLSIVKKLADTVAVMQNGQCVE 237
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-----GtVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
153-234 |
2.48e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.17 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelnmGLLFITHNLSIVKKLADTVAVMQN 232
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELED 142
|
..
gi 2551249897 233 GQ 234
Cdd:cd03221 143 GK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-229 |
2.82e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVrtvVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLH 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-----VRLASGKISILGQPTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLrdvrgnkIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRREAA---RAEILTCLDRVGirqaakrLADYPH-- 155
Cdd:PRK15056 74 ALQKNL-------VAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKkrdRQIVTAALARVD-------MVEFRHrq 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLAD-TVAV 229
Cdd:PRK15056 140 igELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDyTVMV 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
306-492 |
5.09e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITsqgsivfdglalhtlNRRQLLPVRHRIQVvfqdPNSSLNPRLSVLQII 385
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKST----LLRLLA---------------GALKGTPVAGCVDV----PDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 eeglrvhqptlSAEQREAQVKAVMAEVGL-DSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVqAQI 464
Cdd:COG2401 107 -----------GRKGDFKDAVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT-AKR 174
|
170 180
....*....|....*....|....*....
gi 2551249897 465 LTL-LKSLQEKHRLAYIFISHDLHVVRAL 492
Cdd:COG2401 175 VARnLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-201 |
6.69e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvtalSILRLLP--SPPVvypSGDIRFHGESLLHANEQTLRDV------RGNKIAmifq 99
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKT----SLLRILAglARPD---AGEVLWQGEPIRRQRDEYHQDLlylghqPGIKTE---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 100 epmvsLNPLHNLekqlyevLSLHRgMRREAARAEILTCLDRVGIRqaakRLADYP-HQLSGGERQRVMIAMALLTRPELL 178
Cdd:PRK13538 89 -----LTALENL-------RFYQR-LHGPGDDEALWEALAQVGLA----GFEDVPvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|...
gi 2551249897 179 IADEPTTALDVSVQAQILQLLRE 201
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQ 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
272-521 |
7.06e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.56 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 272 QAPLLEVEKLRVAFpirKGILkrvvdhnvVVNDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDG 346
Cdd:PRK11300 2 SQPLLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTT----VFNCLTgfykpTGGTILLRG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 347 LALHTLNRRQLlpVRHRIQVVFQdpNSSLNPRLSVLqiieEGLRVHQ---------------PTLSAEQREAQVKAV--M 409
Cdd:PRK11300 67 QHIEGLPGHQI--ARMGVVRTFQ--HVRLFREMTVI----ENLLVAQhqqlktglfsgllktPAFRRAESEALDRAAtwL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 410 AEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVV 489
Cdd:PRK11300 139 ERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
250 260 270
....*....|....*....|....*....|....
gi 2551249897 490 RALCHQVIVLRQGEVVEQGQCEHVFNAPQ--QAY 521
Cdd:PRK11300 218 MGISDRIYVVNQGTPLANGTPEEIRNNPDviKAY 251
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
317-509 |
8.34e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 317 LVGESGSGKSTtgLALLRL---ITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnsslnprlsvlQIIEEGLRVHQ 393
Cdd:PRK10790 372 LVGHTGSGKST--LASLLMgyyPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDP-----------VVLADTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 394 pTLSAEQREAQVKAVMAEVGLDSETR------HRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQ 463
Cdd:PRK10790 436 -TLGRDISEEQVWQALETVQLAELARslpdglYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 464 ILTLLKSLQEKHRLayIFISHDLH-VVRAlcHQVIVLRQGEVVEQGQ 509
Cdd:PRK10790 515 IQQALAAVREHTTL--VVIAHRLStIVEA--DTILVLHRGQAVEQGT 557
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
306-506 |
1.12e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-------TSQGSIVFDGlalhtlNRRQllpvrhriqvvFQDPNSSlnPR 378
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKST----LMKVLsgvyphgSYEGEILFDG------EVCR-----------FKDIRDS--EA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 379 LSVLqIIeeglrvHQ-----PTLS-AE-----------------QREAQVKAVMAEVGLDsETRHRYPAEFSGGQRQRIA 435
Cdd:NF040905 78 LGIV-II------HQelaliPYLSiAEniflgnerakrgvidwnETNRRARELLAKVGLD-ESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 436 IARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEkHRLAYIFISHDLHVVRALCHQVIVLRQGEVVE 506
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-504 |
1.15e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 30 LRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaNEQTLRDVRGNKIAMIFQEPMVSL--NP 107
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKS-TLLKCLFGIYQKD----SGSILFQGKEI---DFKSSKEALENGISMVHQELNLVLqrSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 108 LHNLEKQLYEVLSL---HRGMRREAARaeILTCLDrVGIRQAAKrLADyphqLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:PRK10982 91 MDNMWLGRYPTKGMfvdQDKMYRDTKA--IFDELD-IDIDPRAK-VAT----LSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 185 TALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLTAP--THPYTKKLLNSEPS 262
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKiiAMMVGRSLTQRFPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 263 GDPVPLPVgqapLLEVEKLrvafpirkgilkrVVDHNVVVNDVSFSLRPGETLGLVGESGSgKSTTGLALLRLI--TSQG 340
Cdd:PRK10982 242 KENKPGEV----ILEVRNL-------------TSLRQPSIRDVSFDLHKGEILGIAGLVGA-KRTDIVETLFGIreKSAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 341 SIVFDGLALHtlNRRQLLPVRHRIQVVFQDPNSS---------LNPRLSVLQIIEEGLRVhqptLSAEQREAQVKAVMAE 411
Cdd:PRK10982 304 TITLHGKKIN--NHNANEAINHGFALVTEERRSTgiyayldigFNSLISNIRNYKNKVGL----LDNSRMKSDTQWVIDS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 412 VGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRA 491
Cdd:PRK10982 378 MRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLG 456
|
490
....*....|...
gi 2551249897 492 LCHQVIVLRQGEV 504
Cdd:PRK10982 457 ITDRILVMSNGLV 469
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
306-468 |
2.00e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITS-----QGSIVFDGLALHTLN---RRQLLPVRHRiqvvfqdpnSSLNP 377
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRILAGlarpdAGEVLWQGEPIRRQRdeyHQDLLYLGHQ---------PGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVlqiiEEGLRVHQPtLSAEQREAQVKAVMAEVGLDSetRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK13538 88 ELTA----LENLRFYQR-LHGPGDDEALWEALAQVGLAG--FEDVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|..
gi 2551249897 457 DRTVQAQILTLL 468
Cdd:PRK13538 161 DKQGVARLEALL 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-485 |
2.03e-13 |
|
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: 72.66 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILR-------------------LLPSPPVVYPSGDIRFHGESLLHAN 82
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMAgvdkdfngearpqpgikvgYLPQEPQLDPTKTVRENVEEGVAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRdvRGNKIAMIFQEPMVSLNPLhnLEKQ--LYEVLslhrgmrrEAARAEiltCLDRvGIRQAAKRL------ADYP 154
Cdd:TIGR03719 97 KDALD--RFNEISAKYAEPDADFDKL--AAEQaeLQEII--------DAADAW---DLDS-QLEIAMDALrcppwdADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhelnmG-LLFITHNLSIVKKLADTVAVMQNG 233
Cdd:TIGR03719 161 K-LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP-----GtVVAVTHDRYFLDNVAGWILELDRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 234 QCV----------EQNRAAQLLTAPTHPYTKKLLNSE-------PSG--------------------------DPVPLPV 270
Cdd:TIGR03719 235 RGIpwegnysswlEQKQKRLEQEEKEESARQKTLKRElewvrqsPKGrqakskarlaryeellsqefqkrnetAEIYIPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 271 GQ---APLLEVEKLRVAFPIRKGIlkrvvdhnvvvNDVSFSLRPGETLGLVGESGSGKSTtglaLLRLITSQ-----GSI 342
Cdd:TIGR03719 315 GPrlgDKVIEAENLTKAFGDKLLI-----------DDLSFKLPPGGIVGVIGPNGAGKST----LFRMITGQeqpdsGTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 343 VfdglalhtlnrrqllpVRHRIQVVFQDPN-SSLNPRLSVLQIIEEGLRVhqptLSAEQREAQVKAVMAEVGLDSETRHR 421
Cdd:TIGR03719 380 E----------------IGETVKLAYVDQSrDALDPNKTVWEEISGGLDI----IKLGKREIPSRAYVGRFNFKGSDQQK 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-RTVQAqiltLLKSLQEKHRLAYIfISHD 485
Cdd:TIGR03719 440 KVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDvETLRA----LEEALLNFAGCAVV-ISHD 499
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-236 |
2.10e-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: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 10 NLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPS--PPVVYPSGDIRFHGESLLHANEQTLR 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCS----TLLKALANrtEGNVSVEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVrgnkiamIFqepmVSLNPLHNLEKQLYEVLSLhrgmrreAARAeiltcldrvgirqaakRLADYPHQLSGGERQRVMI 167
Cdd:cd03233 84 EI-------IY----VSEEDVHFPTLTVRETLDF-------ALRC----------------KGNEFVRGISGGERKRVSI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLS-IVKKLADTVAVMQNGQCV 236
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-237 |
2.52e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPVVypSGDIRFHGESLLH 80
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKS-TLSKVIAGHPAYKIL--EGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 AnEQTLRDVRGnkIAMIFQEPmVSLNPLHNLekqlyEVLSLHRGMRREAARAE----------ILTCLDRVGIRQaaKRL 150
Cdd:CHL00131 76 L-EPEERAHLG--IFLAFQYP-IEIPGVSNA-----DFLRLAYNSKRKFQGLPeldplefleiINEKLKLVGMDP--SFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 151 ADYPHQ-LSGGERQRVMI-AMALLtRPELLIADEPTTALDVSVqaqilqlLRELQHELNM------GLLFITHN---LSI 219
Cdd:CHL00131 145 SRNVNEgFSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDA-------LKIIAEGINKlmtsenSIILITHYqrlLDY 216
|
250
....*....|....*...
gi 2551249897 220 VKklADTVAVMQNGQCVE 237
Cdd:CHL00131 217 IK--PDYVHVMQNGKIIK 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
306-501 |
2.64e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVfdglalhtlnRRQLLPVRHRIQVVFQDPNSSLNprlsvlqi 384
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIK----------RNGKLRIGYVPQKLYLDTTLPLT-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLRVHQPTLSAEQREAqVKAVMAEVGLDSETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:PRK09544 86 VNRFLRLRPGTKKEDILPA-LKRVQAGHLIDAPMQ-----KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2551249897 465 LTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQ 501
Cdd:PRK09544 160 YDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-234 |
3.35e-13 |
|
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: 72.00 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHANEQT 85
Cdd:TIGR01842 317 LSVENVTIVPPGGK--KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP-----PTSGSVRLDGADLKQWDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LrdvrGNKIAMIFQEpmVSLNP---LHNLEKqlyevlslhrgMRREAARAEILtcldrvgirqAAKRLADYpHQ------ 156
Cdd:TIGR01842 390 F----GKHIGYLPQD--VELFPgtvAENIAR-----------FGENADPEKII----------EAAKLAGV-HElilrlp 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 -------------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVkKL 223
Cdd:TIGR01842 442 dgydtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLL-GC 519
|
250
....*....|.
gi 2551249897 224 ADTVAVMQNGQ 234
Cdd:TIGR01842 520 VDKILVLQDGR 530
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
5.08e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.27 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPPVvyPSGDIRFHGESLLHAN 82
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAV----DLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS--AGSHIELLGRTVQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 eQTLRDVRGNK--IAMIFQEPMVsLNPLHNLEKQLYEVLSLHRGMR------REAARAEILTCLDRVGirqaakrLADYP 154
Cdd:PRK09984 76 -RLARDIRKSRanTGYIFQQFNL-VNRLSVLENVLIGALGSTPFWRtcfswfTREQKQRALQALTRVG-------MVHFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVM 230
Cdd:PRK09984 147 HQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
....
gi 2551249897 231 QNGQ 234
Cdd:PRK09984 227 RQGH 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
306-490 |
6.01e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLalHTLNRRQLLPVRHRIQVVFQDP--------- 371
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKST----ILKLIErlydpTEGDIIINDS--HNLKDINLKWWRSKIGVVSQDPllfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 372 --------------------------NSSLNPRLSVLQIIEEGLRVHQPTLSAEQ-----------REAQVKAVMAEVGL 414
Cdd:PTZ00265 479 nikyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLNDMSNTTDSNEliemrknyqtiKDSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 415 D---SETRHRY-------PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISH 484
Cdd:PTZ00265 559 HdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
....*.
gi 2551249897 485 DLHVVR 490
Cdd:PTZ00265 639 RLSTIR 644
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
24-238 |
6.64e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLlhaNEQTLRDvRGnkIAMIFQEpmV 103
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVAGLERI-TSGEIWIGGRVV---NELEPAD-RD--IAMVFQN--Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 104 SLNPlH-----NLEKQLYevlslHRGM------RR--EAARA-EILTCLDRvgirqaakrladYPHQLSGGERQRVMIAM 169
Cdd:PRK11650 86 ALYP-HmsvreNMAYGLK-----IRGMpkaeieERvaEAARIlELEPLLDR------------KPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQcVEQ 238
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQ 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
308-505 |
7.18e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 308 SLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLNRRQLLpvRHRIQVVFQDPNSSLnpRLSVL 382
Cdd:PRK10982 20 KVRPHSIHALMGENGAGKST----LLKCLfgiyqKDSGSILFQGKEIDFKSSKEAL--ENGISMVHQELNLVL--QRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QII------EEGLRVHQPTLSAEqreaqVKAVMAEVGLDSETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:PRK10982 92 DNMwlgrypTKGMFVDQDKMYRD-----TKAIFDELDIDIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2551249897 457 DRTVQAQILTLLKSLQEKHrLAYIFISHDLHVVRALCHQVIVLRQGEVV 505
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-248 |
7.22e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 15 FRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALS-ILRLLPSPpvvypSGDIRFHGESLLHANeqtLRDVRGnK 93
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKS-TLLSlIQRHFDVS-----EGDIRFHDIPLTKLQ---LDSWRS-R 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 94 IAMIFQEPMVSLNPLHNlekqlyevlSLHRGmRREAARAEIltcldrvgirQAAKRLAD-----------YPHQ------ 156
Cdd:PRK10789 391 LAVVSQTPFLFSDTVAN---------NIALG-RPDATQQEI----------EHVARLASvhddilrlpqgYDTEvgergv 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNmgLLFITHNLSIVKKlADTVAVMQNGQC 235
Cdd:PRK10789 451 mLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT--VIISAHRLSALTE-ASEILVMQHGHI 527
|
250
....*....|...
gi 2551249897 236 VEQNRAAQLLTAP 248
Cdd:PRK10789 528 AQRGNHDQLAQQS 540
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
156-498 |
9.71e-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: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQnGQc 235
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELA-EEGKYVLVVEHDLAILDYLADYVHILY-GE- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 236 veqnraaqlltaP------THPY-TKKLLNSEPSG-----------DPVPLPVGQAPLLEVEKLRVAFP-IRKgilkrvv 296
Cdd:COG1245 289 ------------PgvygvvSKPKsVRVGINQYLDGylpeenvrirdEPIEFEVHAPRREKEEETLVEYPdLTK------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 297 dhnvvvNDVSFSL-------RPGETLGLVGESGSGKSTtglaLLRLITS-----QGSIVFDglalhtlnrrqlLPVRHRI 364
Cdd:COG1245 350 ------SYGGFSLeveggeiREGEVLGIVGPNGIGKTT----FAKILAGvlkpdEGEVDED------------LKISYKP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 365 QVVFQDPNSSlnprlsvlqiIEEGLR-VHQPTLSAEQREAQvkaVMAEVGLDsETRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:COG1245 408 QYISPDYDGT----------VEEFLRsANTDDFGSSYYKTE---IIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRD 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 444 PSLIILDEPTSSLD---RTVQAQIltlLKSLQEKHRLAYIFISHDLHVVRALCHQVIV 498
Cdd:COG1245 474 ADLYLLDEPSAHLDveqRLAVAKA---IRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-245 |
1.04e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLsvGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHAnE 83
Cdd:PRK13638 1 MLATSDL--WFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ------KGAVLWQGKPLDYS-K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRgNKIAMIFQEPmvslnplhnlEKQLYEV-------LSLhRGMrrEAARAEILTCLDRVGIRQAAKRLADYPHQ 156
Cdd:PRK13638 70 RGLLALR-QQVATVFQDP----------EQQIFYTdidsdiaFSL-RNL--GVPEAEITRRVDEALTLVDAQHFRHQPIQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 -LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMgLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:PRK13638 136 cLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQI 214
|
250
....*....|
gi 2551249897 236 VEQNRAAQLL 245
Cdd:PRK13638 215 LTHGAPGEVF 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-245 |
1.26e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIEnlSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLlpSPPvvyPSGDIRFHGESLlh 80
Cdd:PRK13536 35 GSMSTVAID--LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM--TSP---DAGKITVLGVPV-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 anEQTLRDVRGnKIAMIFQepMVSLNPLHNLEKQLYeVLSLHRGMRREAARAEILTCLDRVGI-RQAAKRLADyphqLSG 159
Cdd:PRK13536 106 --PARARLARA-RIGVVPQ--FDNLDLEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLeSKADARVSD----LSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQN 239
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
....*.
gi 2551249897 240 RAAQLL 245
Cdd:PRK13536 255 RPHALI 260
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
306-508 |
2.04e-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: 66.13 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITSQ--------GSIVFDGLALHTLNRRqllpvrHRIQVVF---QDpnss 374
Cdd:cd03233 27 SGVVKPGEMVLVLGRPGSGCST----LLKALANRtegnvsveGDIHYNGIPYKEFAEK------YPGEIIYvseED---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 375 lnprlsvlqiieeglrVHQPTLSAEQReaqvkavmaevgLDSETR---HRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03233 93 ----------------VHFPTLTVRET------------LDFALRckgNEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 452 PTSSLDRTVQAQILTLLKSLQEKHRLAYIFI----SHDLHvvrALCHQVIVLRQGEVVEQG 508
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSDEIY---DLFDKVLVLYEGRQIYYG 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
306-470 |
2.38e-12 |
|
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: 65.98 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLN---RRQLLPVRHRiqvvfqdpnSSLNP 377
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTT----LLRILAglsppLAGRVLLNGGPLDFQRdsiARGLLYLGHA---------PGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 378 RLSVLqiieEGLRVHQPTLSAEQreaqVKAVMAEVGLDSeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:cd03231 87 TLSVL----ENLRFWHADHSDEQ----VEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|...
gi 2551249897 458 RTVQAQILTLLKS 470
Cdd:cd03231 158 KAGVARFAEAMAG 170
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
306-515 |
2.57e-12 |
|
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: 69.06 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTgLALLRLITS----QGSIV----------------FDG--------------LALHT 351
Cdd:TIGR03269 20 SFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQyeptSGRIIyhvalcekcgyverpsKVGepcpvcggtlepeeVDFWN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 352 LNRRQLLPVRHRIQVVFQDpNSSLNPRLSVLQIIEEGLrvhqPTLSAEQREAQVKAV--MAEVGLDSETRHrYPAEFSGG 429
Cdd:TIGR03269 99 LSDKLRRRIRKRIAIMLQR-TFALYGDDTVLDNVLEAL----EEIGYEGKEAVGRAVdlIEMVQLSHRITH-IARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 430 QRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQ 509
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGT 252
|
....*.
gi 2551249897 510 CEHVFN 515
Cdd:TIGR03269 253 PDEVVA 258
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
306-508 |
2.89e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.59 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITS-QGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDP---NSSLNPRLSV 381
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPvlfSGSLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 L-QIIEEGLRVhqpTLSAEQREAQVKAVMAevGLDSETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSL 456
Cdd:TIGR00957 1383 FsQYSDEEVWW---ALELAHLKTFVSALPD--KLDHEC-----AEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 457 ----DRTVQAQILTLLKSlqekhrLAYIFISHDLHVVRALChQVIVLRQGEVVEQG 508
Cdd:TIGR00957 1453 dletDNLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-249 |
3.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.93 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQETVRTVVNtlsLRVDAGQTLALVGESGSGKSVTALSILRLL-PSPPVVYPSGdirfhgesLLHANE 83
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENIN---LVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSG--------IDTGDF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRgNKIAMIFQEPmvslnplhnlEKQLyevlsLHRGMRREAARAEILTCLDRVGIRQAAKR------LADY---- 153
Cdd:PRK13644 70 SKLQGIR-KLVGIVFQNP----------ETQF-----VGRTVEEDLAFGPENLCLPPIEIRKRVDRalaeigLEKYrhrs 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVkKLADTVAVMQNG 233
Cdd:PRK13644 134 PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRG 211
|
250
....*....|....*.
gi 2551249897 234 QCVEQNRAAQLLTAPT 249
Cdd:PRK13644 212 KIVLEGEPENVLSDVS 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-231 |
3.57e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENlsVGFRQQETVrtVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHANE 83
Cdd:PRK10247 6 PLLQLQN--VGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISPT----SGTLLFEGEDISTLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRdvrgNKIAMIFQEPMVslnplhnLEKQLYEVLSLHRGMRREAA-RAEILTCLDRVGIRQA--AKRLADyphqLSGG 160
Cdd:PRK10247 77 EIYR----QQVSYCAQTPTL-------FGDTVYDNLIFPWQIRNQQPdPAIFLDDLERFALPDTilTKNIAE----LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQ 231
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-233 |
4.69e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 30 LRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVyPSGDirfhgeslLHANEQTLRDV----RGnkIAMIFQEpmVSL 105
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDI-TSGD--------LFIGEKRMNDVppaeRG--VGMVFQS--YAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 106 NPLHNLekqlYEVLSLhrGMR-REAARAEILTCLDRVG-IRQAAKRLADYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:PRK11000 87 YPHLSV----AENMSF--GLKlAGAKKEEINQRVNQVAeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 184 TTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-457 |
7.31e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvTALSIL---RLLPSPPVVYPSGDI--RFHGESLLHaneqtlrdvrgnKIAMIFQepm 102
Cdd:NF033858 20 VSLDIPAGCMVGLIGPDGVGKS-SLLSLIagaRKIQQGRVEVLGGDMadARHRRAVCP------------RIAYMPQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 vslnplhNLEKQLYEVLSL------------HRGMRREAARAEIL--TCLDRVGIRQAAKrladyphqLSGGERQRVMIA 168
Cdd:NF033858 84 -------GLGKNLYPTLSVfenldffgrlfgQDAAERRRRIDELLraTGLAPFADRPAGK--------LSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQHEL-NMGLLFIThnlsivkklA--------DTVAVMQNGQCVEQN 239
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT---------AymeeaerfDWLVAMDAGRVLATG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 240 RAAQLLtAPTHPYT-----KKLLNSEPSGDPVPLPV-------GQAPLLEVEKL-----------RVAFPIRKGilkrvv 296
Cdd:NF033858 220 TPAELL-ARTGADTleaafIALLPEEKRRGHQPVVIpprpaddDDEPAIEARGLtmrfgdftavdHVSFRIRRG------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 297 dhnvvvndvsfslrpgETLGLVGESGSGKSTT-----GLallrLITSQGSivfdglAL---HTLNRRQLlPVRHRI---- 364
Cdd:NF033858 293 ----------------EIFGFLGSNGCGKSTTmkmltGL----LPASEGE------AWlfgQPVDAGDI-ATRRRVgyms 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 365 QVvFqdpnsSLNPRLSVLQIIEEGLRVHQptLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKP 444
Cdd:NF033858 346 QA-F-----SLYGELTVRQNLELHARLFH--LPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
490
....*....|...
gi 2551249897 445 SLIILDEPTSSLD 457
Cdd:NF033858 417 ELLILDEPTSGVD 429
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
306-523 |
7.35e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnsslnprlsVL-- 382
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKFGLMDL---RKVLGIIPQAP---------VLfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 383 QIIEEGLRVHQPTLSAEQREAQVKAVMAEV------GLDSETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEP 452
Cdd:PLN03130 1327 GTVRFNLDPFNEHNDADLWESLERAHLKDVirrnslGLDAEV-----SEagenFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 453 TSSLDRTVQAQIltlLKSLQEKHR-LAYIFISHDLHVVRAlCHQVIVLRQGEVVEQGQCEHVFNAPQQAYTR 523
Cdd:PLN03130 1402 TAAVDVRTDALI---QKTIREEFKsCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-230 |
7.54e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLpsppvvypsgdirfhgesllhaneqtLR 87
Cdd:COG2401 31 LEAFGVELRVVE--RYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL--------------------------AG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 88 DVRGNKIAMIFQEPMVSLNPLHNLEKQLYEVLSLHRGMRReaaraeiltcLDRVGIRQAAKRLADYPHqLSGGERQRVMI 167
Cdd:COG2401 79 ALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVEL----------LNAVGLSDAVLWLRRFKE-LSTGQKFRFRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 168 AMALLTRPELLIADEPTTALDVSVqAQILQL-LRELQHELNMGLLFITHNLSIVKKLADTVAVM 230
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
306-504 |
8.09e-12 |
|
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: 65.65 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQ-------------DPN 372
Cdd:cd03289 24 SFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKW---RKAFGVIPQkvfifsgtfrknlDPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 373 SSLNPRlSVLQIIEE-GLRvhqptLSAEQREAQVKAVMAEVGldsetrhrypAEFSGGQRQRIAIARALILKPSLIILDE 451
Cdd:cd03289 101 GKWSDE-EIWKVAEEvGLK-----SVIEQFPGQLDFVLVDGG----------CVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 452 PTSSLDrTVQAQILTllKSLqeKHRLAYIFISHDLHVVRAL--CHQVIVLRQGEV 504
Cdd:cd03289 165 PSAHLD-PITYQVIR--KTL--KQAFADCTVILSEHRIEAMleCQRFLVIEENKV 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-234 |
9.03e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 67.47 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQEtvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLH 80
Cdd:COG4618 331 LSVENLTVVPPGSK--RPILRGVSFSLEPGEVLGVIGPSGSGKS----TLARLLvgvwpPT------AGSVRLDGADLSQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRD---------------VRGNkIAMiFQEPmvslNPlhnlEKqlyeVLslhrgmrrEAARAeiltcldrVGIRQ 145
Cdd:COG4618 399 WDREELGRhigylpqdvelfdgtIAEN-IAR-FGDA----DP----EK----VV--------AAAKL--------AGVHE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 146 AAKRLAD-Y-------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQhELNMGLLFITHNL 217
Cdd:COG4618 449 MILRLPDgYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRP 527
|
250
....*....|....*..
gi 2551249897 218 SIVkKLADTVAVMQNGQ 234
Cdd:COG4618 528 SLL-AAVDKLLVLRDGR 543
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-234 |
1.05e-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: 64.03 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQQETVRT-VVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGeSLLHANEQ 84
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKL-----SGSVSVPG-SIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 ------TLRDvrgNkiaMIFQEPMvslnplhnlEKQLYE-VL---SLHRGMrreaaraEILTCLDR--VGIRQAAkrlad 152
Cdd:cd03250 75 pwiqngTIRE---N---ILFGKPF---------DEERYEkVIkacALEPDL-------EILPDGDLteIGEKGIN----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 yphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQHELNMG--LLFITHNLSIVKKlADTVAVM 230
Cdd:cd03250 128 ----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLLNNktRILVTHQLQLLPH-ADQIVVL 200
|
....
gi 2551249897 231 QNGQ 234
Cdd:cd03250 201 DNGR 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
306-504 |
1.06e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.01 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLITSQGSIVFDGLALHTLN----RRQLLPVRHRIQVVFQDPNSSLNPRlsv 381
Cdd:TIGR01271 1239 SFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTlqtwRKAFGVIPQKVFIFSGTFRKNLDPY--- 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 lqiieeglrvhqptlsAEQREAQVKAVMAEVGLDSETrHRYPAE-----------FSGGQRQRIAIARALILKPSLIILD 450
Cdd:TIGR01271 1316 ----------------EQWSDEEIWKVAEEVGLKSVI-EQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 451 EPTSSLDrTVQAQILTllKSLQEKHRLAYIFISHdlHVVRAL--CHQVIVLRQGEV 504
Cdd:TIGR01271 1379 EPSAHLD-PVTLQIIR--KTLKQSFSNCTVILSE--HRVEALleCQQFLVIEGSSV 1429
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-246 |
1.16e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 1 MTQPLLAIENLSVGFRQQETVRTVvntlSLRVDAGQTLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLlh 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEV----SLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRA-TSGRIVFDGKDI-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRgNKIAMIFQEpmvslnplhnleKQLYEVLSLHRGMRRE---AARAEILTCLDRVgiRQAAKRLADYPHQ- 156
Cdd:PRK11614 70 TDWQTAKIMR-EAVAIVPEG------------RRVFSRMTVEENLAMGgffAERDQFQERIKWV--YELFPRLHERRIQr 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNG 233
Cdd:PRK11614 135 agtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENG 213
|
250
....*....|...
gi 2551249897 234 QCVEQNRAAQLLT 246
Cdd:PRK11614 214 HVVLEDTGDALLA 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-232 |
1.63e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 8 IENLSVGFRQQETVRT-VVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLL--------------------------- 59
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 60 ----------------------PSPPVVYPSGDIRFHGESLLHANeqtLRDVRgNKIAMIFQEPMvslnpLHNLekQLYE 117
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgEDSTVFKNSGKILLDGVDICDYN---LKDLR-NLFSIVSQEPM-----LFNM--SIYE 1314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 118 VLSLHR--GMRREAARAEILTCLDRVgIRQAAKR----LADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSV 191
Cdd:PTZ00265 1315 NIKFGKedATREDVKRACKFAAIDEF-IESLPNKydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2551249897 192 QAQILQLLRELQHELNMGLLFITHNLSIVKKlADTVAVMQN 232
Cdd:PTZ00265 1394 EKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-508 |
1.66e-11 |
|
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: 63.31 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 276 LEVEKLRVA---FPIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALL---RLITSQGSIVFDGLAL 349
Cdd:cd03217 1 LEIKDLHVSvggKEILKGV--------------NLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 350 htLNrrqlLPVRHR----IQVVFQDPnsslnPRLsvlqiieEGLRVhqptlsaeqreaqvkavmaevgldsETRHRYPAE 425
Cdd:cd03217 67 --TD----LPPEERarlgIFLAFQYP-----PEI-------PGVKN-------------------------ADFLRYVNE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 426 -FSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVI-VLRQGE 503
Cdd:cd03217 104 gFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIKPDRVhVLYDGR 182
|
....*
gi 2551249897 504 VVEQG 508
Cdd:cd03217 183 IVKSG 187
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
274-511 |
1.85e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 274 PLLEVEKLRVA---FPIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTtglaLLRLITS-------QGSIV 343
Cdd:CHL00131 6 PILEIKNLHASvneNEILKGL--------------NLSINKGEIHAIMGPNGSGKST----LSKVIAGhpaykilEGDIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 344 FDGLALHTLN---RRQLlpvrhRIQVVFQDP----------------NS--------SLNPrLSVLQIIEEGLRVhqptl 396
Cdd:CHL00131 68 FKGESILDLEpeeRAHL-----GIFLAFQYPieipgvsnadflrlayNSkrkfqglpELDP-LEFLEIINEKLKL----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 397 saeqreaqvkavmaeVGLDSETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLD----RTVQAQILTLLKSL 471
Cdd:CHL00131 137 ---------------VGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSE 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2551249897 472 QekhrlAYIFISH-----DlHVVRALCHqviVLRQGEVVEQGQCE 511
Cdd:CHL00131 202 N-----SIILITHyqrllD-YIKPDYVH---VMQNGKIIKTGDAE 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-262 |
5.53e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 13 VGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHANEQTLRDVrgn 92
Cdd:PLN03232 1240 VHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI-----VELEKGRIMIDDCDVAKFGLTDLRRV--- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 93 kIAMIFQEPMV-------SLNPL--HNlEKQLYEVLSlhrgmrreaaRAEILTCLDRVGIRQAAKrLADYPHQLSGGERQ 163
Cdd:PLN03232 1312 -LSIIPQSPVLfsgtvrfNIDPFseHN-DADLWEALE----------RAHIKDVIDRNPFGLDAE-VSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMglLFITHNLSIVKKlADTVAVMQNGQCVEQNRAAQ 243
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
250
....*....|....*....
gi 2551249897 244 LLTAPTHPYTKKLLNSEPS 262
Cdd:PLN03232 1456 LLSRDTSAFFRMVHSTGPA 1474
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-230 |
5.73e-11 |
|
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: 62.77 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 35 GQTLALVGESGSGKSvTALSIL--RLLP------SPPvvypSGD--IRFHGESLLHaneQTLRDVRGNKIAMIFQEPMVS 104
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALKILagKLKPnlgkfdDPP----DWDeiLDEFRGSELQ---NYFTKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 105 LNPlhnleKQLY-EVLSLhrgMRREAARAEILTCLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTRPELLIADEP 183
Cdd:cd03236 98 LIP-----KAVKgKVGEL---LKKKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2551249897 184 TTALDVSVQAQILQLLRELQHELNmGLLFITHNLSIVKKLADTVAVM 230
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-232 |
9.45e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHgesllhaNEQTLRDVR----GNKIAMIFQEPMV 103
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDPT----EGDIIIN-------DSHNLKDINlkwwRSKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 104 --------------SLNPLHNLEKQL-------YEVLSLHRGMRREAAR--------------------------AEILT 136
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEALSNYYnedgndsQENKNKRNSCRAKCAGdlndmsnttdsneliemrknyqtikdSEVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 137 CLDRVGIRQAAKRLADY--------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNM 208
Cdd:PTZ00265 552 VSKKVLIHDFVSALPDKyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|....
gi 2551249897 209 GLLFITHNLSIVkKLADTVAVMQN 232
Cdd:PTZ00265 632 ITIIIAHRLSTI-RYANTIFVLSN 654
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
306-523 |
1.04e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTglallrLITSQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDPnssLNPRLSVLQII 385
Cdd:PTZ00265 1249 NVGMKNVNEFSLTKEGGSGEDST------VFKNSGKILLDGVDICDYNLKDL---RNLFSIVSQEP---MLFNMSIYENI 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 386 EEGLRvhQPTLSAEQREAQVKAV---MAEVGLDSETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQ 461
Cdd:PTZ00265 1317 KFGKE--DATREDVKRACKFAAIdefIESLPNKYDTNvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 462 AQILTLLKSLQEKHRLAYIFISHDLHVVRAlCHQVIVL----RQGEVVE-QGQCEHVFNAPQQAYTR 523
Cdd:PTZ00265 1395 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKK 1460
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
309-513 |
1.40e-10 |
|
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: 64.26 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 309 LRPGETLGLVGESGSGKSTTglalLRLITSQgSIVFDGLAlhTLNRRQLLPvrhRIQVVFQdpNSSLNPRLSVLQIIEEG 388
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTT----FKMLTGD-TTVTSGDA--TVAGKSILT---NISDVHQ--NMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 389 -----LRVHQPTLSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQ 463
Cdd:TIGR01257 2030 rehlyLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 464 ILTLLKSLQEKHRlAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:TIGR01257 2109 LWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
306-474 |
1.50e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLI-----TSQGSIVFDGLALHTLNRRQLLpvRHRIQVVfqdPNSSlnpRLS 380
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTT----LLGTLcgdprATSGRIVFDGKDITDWQTAKIM--REAVAIV---PEGR---RVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIEEGLRVHQPTLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTV 460
Cdd:PRK11614 93 SRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170
....*....|....
gi 2551249897 461 QAQILTLLKSLQEK 474
Cdd:PRK11614 173 IQQIFDTIEQLREQ 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
1.67e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLP--SPPVvypSGDIRFHGEsllhanEQTLRDVR------GNK 93
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKT----TLLRLIAglLPPA---AGTIKLDGG------DIDDPDVAeachylGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 94 IAMifqEPMVSLNplhnlekqlyEVLSLHRGMRReAARAEILTCLDRVGIRQAAKRLADYphqLSGGERQRVMIAMALLT 173
Cdd:PRK13539 82 NAM---KPALTVA----------ENLEFWAAFLG-GEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVS 144
|
170 180
....*....|....*....|....*...
gi 2551249897 174 RPELLIADEPTTALDVSVQAQILQLLRE 201
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-236 |
1.91e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 3 QPLLAIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILrllpsppvvypSGdiRFHGESL---L 79
Cdd:PLN03211 62 KRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKS-TLLNAL-----------AG--RIQGNNFtgtI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 80 HANEQTLRDVRGNKIAMIFQEPMvsLNPLHNLEKQLY--EVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLA--DYPH 155
Cdd:PLN03211 128 LANNRKPTKQILKRTGFVTQDDI--LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIgnSFIR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQC 235
Cdd:PLN03211 206 GISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRC 285
|
.
gi 2551249897 236 V 236
Cdd:PLN03211 286 L 286
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
309-513 |
2.02e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 309 LRPGETLGLVGESGSGKSTtglaLLRLITSQ---------GSIVFDGLALHTLNRRqllpvrHRIQVVFQDPNSSLNPRL 379
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCST----LLKTIASNtdgfhigveGVITYDGITPEEIKKH------YRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 380 SVLQIIEEGLRVHQPT-----LSAEQREAQVKAV-MAEVGLDSETRHRYPAEF----SGGQRQRIAIARALILKPSLIIL 449
Cdd:TIGR00956 154 TVGETLDFAARCKTPQnrpdgVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 450 DEPTSSLDrtvQAQILTLLKSLQEKHRlayifISHDLHVVRAL-CHQ--------VIVLRQGEVVEQGQCEHV 513
Cdd:TIGR00956 234 DNATRGLD---SATALEFIRALKTSAN-----ILDTTPLVAIYqCSQdayelfdkVIVLYEGYQIYFGPADKA 298
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-243 |
2.05e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQC- 235
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVa 470
|
90
....*....|
gi 2551249897 236 --VEQNRAAQ 243
Cdd:PRK10982 471 giVDTKTTTQ 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
280-457 |
2.12e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.03 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 280 KLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTtglaLLRLITSQGSiVFDGLALHTLNRR-QLL 358
Cdd:TIGR03719 9 RVSKVVPPKKEILK----------DISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDK-DFNGEARPQPGIKvGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 359 PvrhriqvvfQDPnsSLNPRLSVLQIIEEGLrvhQPTLSAEQREAQVKAVMAEVG------------------------L 414
Cdd:TIGR03719 74 P---------QEP--QLDPTKTVRENVEEGV---AEIKDALDRFNEISAKYAEPDadfdklaaeqaelqeiidaadawdL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 415 DSETRH-----RYP------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:TIGR03719 140 DSQLEIamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-238 |
2.36e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLP--SPPVVYPSGDIrfhgeSLLHAN 82
Cdd:PRK10895 3 TLTAKNLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrdAGNIIIDDEDI-----SLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDvrgnkIAMIFQEPMV--SLNPLHNLekqlYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLAdypHQLSGG 160
Cdd:PRK10895 74 ARARRG-----IGYLPQEASIfrRLSVYDNL----MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALD-VSVQ--AQILQLLRelqhELNMGLLFITHNLSivkklaDTVAVMQNGQCVE 237
Cdd:PRK10895 142 ERRRVEIARALAANPKFILLDEPFAGVDpISVIdiKRIIEHLR----DSGLGVLITDHNVR------ETLAVCERAYIVS 211
|
.
gi 2551249897 238 Q 238
Cdd:PRK10895 212 Q 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
23-236 |
4.05e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 23 TVVNTLSLRVDAGQTLALVGESGSGKS--VTALSILrLLPSppvvypSGDIRFhgesllhaneqTLRDVRGNKIAMIFQE 100
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTtfIEHLNAL-LLPD------TGTIEW-----------IFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 101 PMVSLN-------PLHNL--------------EKQLYEV----------LSLhrGMRREAARAEILTCLDRVGIRQAAkr 149
Cdd:PRK13651 83 VLEKLViqktrfkKIKKIkeirrrvgvvfqfaEYQLFEQtiekdiifgpVSM--GVSKEEAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 150 LADYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqHELNMGLLFITHNLSIVKKLADTVAV 229
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*..
gi 2551249897 230 MQNGQCV 236
Cdd:PRK13651 238 FKDGKII 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-504 |
7.61e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 21 VRTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILR--------------------------LLPSPPVVYP-SGDIRF 73
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKS-TLLALLKneisadggsytfpgnwqlawvnqetpALPQPALEYViDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 74 HG--ESLLHANEQTlrdvRGNKIAMIFQEpmvsLNPLHNLEKQlyevlslhrgmrreaARAEILtcLDRVGIRQaaKRLA 151
Cdd:PRK10636 92 RQleAQLHDANERN----DGHAIATIHGK----LDAIDAWTIR---------------SRAASL--LHGLGFSN--EQLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELnmglLFITHNLSIVKKLADTVAVMQ 231
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVDKIIHIE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 232 ---------NGQCVEQNRAAQL---------------------------------------------LTAPTH---PYTK 254
Cdd:PRK10636 221 qqslfeytgNYSSFEVQRATRLaqqqamyesqqervahlqsyidrfrakatkakqaqsrikmlermeLIAPAHvdnPFHF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 255 KLLnsepsgDPVPLPvgqAPLLEVEKLRVAFPIRKgILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTtglaLLR 334
Cdd:PRK10636 301 SFR------APESLP---NPLLKMEKVSAGYGDRI-ILD----------SIKLNLVPGSRIGLLGRNGAGKST----LIK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 335 LITS-----QGSI-VFDGLALHTLNRRQLlpvrhriqvvfqdpnSSLNPRLSVLQiieeglrvHQPTLSAEQREAQVKAV 408
Cdd:PRK10636 357 LLAGelapvSGEIgLAKGIKLGYFAQHQL---------------EFLRADESPLQ--------HLARLAPQELEQKLRDY 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 409 MAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEkhrlAYIFISHDLHV 488
Cdd:PRK10636 414 LGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHL 489
|
570
....*....|....*.
gi 2551249897 489 VRALCHQVIVLRQGEV 504
Cdd:PRK10636 490 LRSTTDDLYLVHDGKV 505
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
156-247 |
8.14e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGqc 235
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEG-- 485
|
90
....*....|..
gi 2551249897 236 veqnRAAQLLTA 247
Cdd:PRK09700 486 ----RLTQILTN 493
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-247 |
1.02e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 16 RQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGeslLHANEQTLRDVRgNKIA 95
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDG---LNIAKIGLHDLR-FKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 96 MIFQEPMV-------SLNPLHNLEKQlyevlslhrgmrreaaraEILTCLDRVGIRQAAKRLAD-YPHQ-------LSGG 160
Cdd:TIGR00957 1364 IIPQDPVLfsgslrmNLDPFSQYSDE------------------EVWWALELAHLKTFVSALPDkLDHEcaeggenLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElQHElNMGLLFITHNLSIVKKLAdTVAVMQNGQCVEQNR 240
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
....*..
gi 2551249897 241 AAQLLTA 247
Cdd:TIGR00957 1503 PSNLLQQ 1509
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
306-508 |
1.05e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST---------TGLALLRLITSQGSIVFDGLALHTLNRRQLLpvrhRIQVVFQDPNSSLN 376
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTllkalagdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRLA----RLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 377 PrLSVLQIIEEGLRVHQPTLSAEQREAQ--VKAVMAEVGLDSETRhRYPAEFSGGQRQRIAIARAL---------ILKPS 445
Cdd:PRK13547 97 A-FSAREIVLLGRYPHARRAGALTHRDGeiAWQALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 446 LIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-234 |
1.08e-09 |
|
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: 60.61 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVgFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRllpsppvVYPSgdiRFHGESLLHANEQ 84
Cdd:TIGR02633 257 ILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-------AYPG---KFEGNVFINGKPV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLR---DVRGNKIAMIFQE-------PMVSLNplHNLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKRLAdyP 154
Cdd:TIGR02633 326 DIRnpaQAIRAGIAMVPEDrkrhgivPILGVG--KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP--I 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
396-457 |
1.22e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 1.22e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 396 LSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
427-503 |
1.40e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.86 E-value: 1.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILT-LLKSLQEKHRlAYIFISHDLHVVRAlCHQVIVLRQGE 503
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNK-TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
280-457 |
2.97e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 280 KLRVAFPIRKGILKrvvdhnvvvnDVSFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVF-DGLalhtln 353
Cdd:PRK11819 11 RVSKVVPPKKQILK----------DISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkeFEGEARPaPGI------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 354 RRQLLPvrhriqvvfQDPnsSLNPRLSVLQIIEEGLrvhQPTLSAEQR-----------EAQVKAVMAEVG--------- 413
Cdd:PRK11819 71 KVGYLP---------QEP--QLDPEKTVRENVEEGV---AEVKAALDRfneiyaayaepDADFDALAAEQGelqeiidaa 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 414 ----LDSETRH-----RYP------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK11819 137 dawdLDSQLEIamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
311-500 |
3.42e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 311 PGETLGLVGESGSGKSTTGLALLRLITSQGSIVFdglalhtlnrrqllpvrhriqvvfqdpnsslnprlsvlqiieeglr 390
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 391 vhqpTLSAEQREAQVKAVMAEVGldsetRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL----- 465
Cdd:smart00382 35 ----YIDGEDILEEVLDQLLLII-----VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleel 105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2551249897 466 TLLKSLQEKHRLAYIFISH------DLHVVRALCHQVIVLR 500
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLL 146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
306-513 |
3.59e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLAlhtlnrrQLLPVrhriqvvfqdpNSSLNPRLS 380
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKST----LSNLIAgvtmpNKGTVDIKGSA-------ALIAI-----------SSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 381 VLQIIE-EGLRVhqpTLSAEQREAQVKAVM--AEVGldsETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK13545 102 GIENIElKGLMM---GLTKEKIKEIIPEIIefADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 458 RTVQAQILTLLKSLQEKHRLAYiFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
125-246 |
6.62e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 125 MRREAARAEILTCLDRVGIRQAAKRLAdypHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQH 204
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAA---AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2551249897 205 ElNMGLLFITHNLSIVKKLADTVAVMQNGQCVEQNRAAQLLT 246
Cdd:NF000106 193 D-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-234 |
1.21e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFrqQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTaLSILRLLPSPPvvypSGDIRFHGESLlhanE 83
Cdd:TIGR01257 927 PGVCVKNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTT-LSILTGLLPPT----SGTVLVGGKDI----E 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRGNkiamifqepmVSLNPLHNLekqLYEVLSLH---------RGMRREAARAEILTCLDRVGIRQAAKRLAdyp 154
Cdd:TIGR01257 996 TNLDAVRQS----------LGMCPQHNI---LFHHLTVAehilfyaqlKGRSWEEAQLEMEAMLEDTGLHHKRNEEA--- 1059
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:TIGR01257 1060 QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-204 |
2.30e-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: 57.23 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFrqQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGESLLHANEQT 85
Cdd:TIGR01271 1218 MDVQGLTAKY--TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST------EGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRG---NKIAMIFQEPMVSLNPlhnlekqlYEVLSlhrgmrreaaRAEILTCLDRVGIRQAAKR--------LADYP 154
Cdd:TIGR01271 1290 WRKAFGvipQKVFIFSGTFRKNLDP--------YEQWS----------DEEIWKVAEEVGLKSVIEQfpdkldfvLVDGG 1351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQllRELQH 204
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIR--KTLKQ 1398
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-221 |
2.48e-08 |
|
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: 56.68 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPSppvVYPSgdirFHGesllhaneqTLRDVRGNKIAMIFQEPMV 103
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKS----SLFRILGE---LWPV----YGG---------RLTKPAKGKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 104 SLNPLHNlekQLYEVLSLHRGMRREAARAEILTCLDRVGIRQAAKR------LADYPHQLSGGERQRVMIAMALLTRPEL 177
Cdd:TIGR00954 527 TLGTLRD---QIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2551249897 178 LIADEPTTALDVSVQAQILQLLRelqhELNMGLLFITHNLSIVK 221
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSLWK 643
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
312-487 |
3.98e-08 |
|
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: 53.87 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 312 GETLGLVGESGSGKSTTGLALLRLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFqdpnSSLNPRLsVLQIIEEGLRV 391
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAY----AAQKPWL-LNATVEENITF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 392 HQPtLSAEQREAQVKAVMAEVGLD-------SETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQI 464
Cdd:cd03290 102 GSP-FNKQRYKAVTDACSLQPDIDllpfgdqTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 179
|
170 180
....*....|....*....|....*
gi 2551249897 465 LT--LLKSLQEKHRlAYIFISHDLH 487
Cdd:cd03290 180 MQegILKFLQDDKR-TLVLVTHKLQ 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-485 |
4.82e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 30 LRVDAGQTLALVGESGSGKSvTALSIL--------------------RLLPSPP-----VVYP--SGDIRFHGEsLLHAN 82
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKS-TLMKILngevllddgriiyeqdlivaRLQQDPPrnvegTVYDfvAEGIEEQAE-YLKRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 83 EQTLRDVRgnkiamifQEPMVSlnplhNLEK--QLYEVLSLHRGMRREAARAEILTCLDRvgirQAAKRLADyphqLSGG 160
Cdd:PRK11147 102 HDISHLVE--------TDPSEK-----NLNElaKLQEQLDHHNLWQLENRINEVLAQLGL----DPDAALSS----LSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHelnmGLLFITHNLSIVKKLADTVAVMQNGQCVeqnr 240
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 241 aaqlltapTHP--YTKKLLnsepsgdpvplpvGQAPLLEVEKLRVA-FP---------IRKGI-------------LKRV 295
Cdd:PRK11147 233 --------SYPgnYDQYLL-------------EKEEALRVEELQNAeFDrklaqeevwIRQGIkarrtrnegrvraLKAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 296 VDHNVVVNDV-------------------------------------SFSLRPGETLGLVGESGSGKSTtglaLLRLITS 338
Cdd:PRK11147 292 RRERSERREVmgtakmqveeasrsgkivfemenvnyqidgkqlvkdfSAQVQRGDKIALIGPNGCGKTT----LLKLMLG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 339 QgsivfdglalhtlnrrqLLPVRHRIQV-------VFQDPNSSLNPRLSVLQIIEEGlrvhQPTLSAEQREAQVKAVMAE 411
Cdd:PRK11147 368 Q-----------------LQADSGRIHCgtklevaYFDQHRAELDPEKTVMDNLAEG----KQEVMVNGRPRHVLGYLQD 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 412 VgLDSETRHRYPAE-FSGGQRQRIAIARaLILKPS-LIILDEPTSSLDrtvqAQILTLLKSLQEKHRLAYIFISHD 485
Cdd:PRK11147 427 F-LFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPSnLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-236 |
5.30e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGESLLhaneQTLRDVRGNkiaMIFQEPMVS 104
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTT----FKMLTGDTTV-TSGDATVAGKSIL----TNISDVHQN---MGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 105 LNPLHNLEKQLYEVLSLhRGMRREAARAEILTCLDRVGIRQAAKRLADyphQLSGGERQRVMIAMALLTRPELLIADEPT 184
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARL-RGVPAEEIEKVANWSIQSLGLSLYADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 185 TALDVSVQAQ----ILQLLRElqhelNMGLLFITHNLSIVKKLADTVAVMQNG--QCV 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 ... |
427-503 |
6.60e-08 |
|
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: 52.99 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQ------RIAIARALILKPSLIILDEPTSSLDR-TVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVL 499
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 2551249897 500 RQGE 503
Cdd:cd03240 197 KDGR 200
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
396-513 |
7.73e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 396 LSAEQREAQVKAVMAEVGLdSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQeKH 475
Cdd:NF000106 116 LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RD 193
|
90 100 110
....*....|....*....|....*....|....*...
gi 2551249897 476 RLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:NF000106 194 GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
306-525 |
1.04e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLAL---LRLITSQGSIVFDGLALHTLNRRQllpvrHRIQVVFQDPNSSL------N 376
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALageLPLLSGERQSQFSHITRLSFEQLQ-----KLVSDEWQRNNTDMlspgedD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 377 PRLSVLQIIEEGlrVHQPTLSAEqreaqvkaVMAEVGLDS--ETRHRYpaeFSGGQRQRIAIARALILKPSLIILDEPTS 454
Cdd:PRK10938 98 TGRTTAEIIQDE--VKDPARCEQ--------LAQQFGITAllDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 455 SLDRTVQAQILTLLKSLQeKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHVFnapQQAYTRQL 525
Cdd:PRK10938 165 GLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL---QQALVAQL 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-233 |
1.11e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 52.72 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHANEQTLRDVRGNKIAMIFQEPMVs 104
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL-----EGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 105 lnplhnLEKQLYEVLSLHRGMRREAARAEILTCLDRVGIR----QAAKRLADYPHQLSGGERQRVMIAMALLTRPELLIA 180
Cdd:cd03290 91 ------LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDllpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 181 DEPTTALDVSV-----QAQILQLLRELQHElnmgLLFITHNLSIVKKlADTVAVMQNG 233
Cdd:cd03290 165 DDPFSALDIHLsdhlmQEGILKFLQDDKRT----LVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-246 |
1.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 7 AIENLSVGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRL--LPSPPVVYPSGDIRFHGesllhaneq 84
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIveLERGRILIDGCDISKFG--------- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 tLRDVRGNkIAMIFQEPMV-------SLNPL--HNlEKQLYEvlSLHRGMRREAARAEILTcLDrvgirqaaKRLADYPH 155
Cdd:PLN03130 1308 -LMDLRKV-LGIIPQAPVLfsgtvrfNLDPFneHN-DADLWE--SLERAHLKDVIRRNSLG-LD--------AEVSEAGE 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMglLFITHNLSIVKKlADTVAVMQNGQC 235
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTIID-CDRILVLDAGRV 1450
|
250
....*....|.
gi 2551249897 236 VEQNRAAQLLT 246
Cdd:PLN03130 1451 VEFDTPENLLS 1461
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
309-471 |
1.49e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 51.86 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 309 LRPGETLGLVGESGSGKSTtglaLLRLI-------TSQGSIVFDGlalhtlnrrQLLPVRHRIQVVFQDPNSSLNPRLSV 381
Cdd:cd03232 30 VKPGTLTALMGESGAGKTT----LLDVLagrktagVITGEILING---------RPLDKNFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 382 lqiiEEGLRvhqptLSAEQReaqvkavmaevGLDSEtrhrypaefsggQRQRIAIARALILKPSLIILDEPTSSLDRTVQ 461
Cdd:cd03232 97 ----REALR-----FSALLR-----------GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170
....*....|
gi 2551249897 462 AQILTLLKSL 471
Cdd:cd03232 145 YNIVRFLKKL 154
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
308-518 |
1.66e-07 |
|
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: 52.41 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 308 SLRPGETLGLVGESGSGKSTtglaLLRLITsqGSIVFDGLALHTLnrrqLLPVRHRIQVVFQDPNSSLNPRLSvlqiiee 387
Cdd:cd03237 21 SISESEVIGILGPNGIGKTT----FIKMLA--GVLKPDEGDIEIE----LDTVSYKPQYIKADYEGTVRDLLS------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 388 glRVHQPTLSAEQREAQV-KAVMAEVGLDSETRhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILT 466
Cdd:cd03237 84 --SITKDFYTHPYFKTEIaKPLQIEQILDREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 467 LLKSLQEKHRLAYIFISHDLHVVRALCHQVIVLrQGEVVEQGQCehvfNAPQ 518
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVA----NPPQ 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
306-513 |
2.48e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKST-TGLALLRLITSQGSIVFDGlalhtlnrrqllpvrhriQVVFQDPNSSLNPRLSVLQI 384
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTlSNIIGGSLSPTVGKVDRNG------------------EVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 IEEGLrvhqptLSAEQREAQVKAVMAEVGLDSETR---HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQ 461
Cdd:PRK13546 106 IEFKM------LCMGFKRKEIKAMTPKIIEFSELGefiYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2551249897 462 AQILTLLKSLQEKHRLAYiFISHDLHVVRALCHQVIVLRQGEVVEQGQCEHV 513
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIF-FVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-215 |
2.79e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILrllpsppvvypSGDirfHGESllHANEQTL---RDVRGNKIAMIF 98
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKS-TLLSLI-----------TGD---HPQG--YSNDLTLfgrRRGSGETIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 99 QEPMVSLNPLHnLEkqlYEVLSlhrgmrreAARAEILT-CLDRVGIRQA------------------AKRLADYP-HQLS 158
Cdd:PRK10938 336 KHIGYVSSSLH-LD---YRVST--------SVRNVILSgFFDSIGIYQAvsdrqqklaqqwldilgiDKRTADAPfHSLS 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITH 215
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
306-490 |
3.63e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.40 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglallrlitsqgsIVFDGLALHTLNR-RQLLPVRHRIQVVFQDpnsslnprlsvlqi 384
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKST--------------LVNEGLYASGKARlISFLPKFSRNKLIFID-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 ieeglrvhqptlsaeqreaQVKAvMAEVGLDSETRHRYPAEFSGGQRQRIAIARALI--LKPSLIILDEPTSSLDRTVQA 462
Cdd:cd03238 67 -------------------QLQF-LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*....
gi 2551249897 463 QILTLLKSL-QEKHRLayIFISHDLHVVR 490
Cdd:cd03238 127 QLLEVIKGLiDLGNTV--ILIEHNLDVLS 153
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
306-370 |
3.93e-07 |
|
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: 52.49 E-value: 3.93e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLIT-----SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQD 370
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKST----LAKLLTglyrpESGEILLDGQPVTADNREAY---RQLFSAVFSD 414
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
427-514 |
4.58e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILT--LLKSLQEKHRlayIFISHDLHVVrALCHQVIVLRQGEV 504
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTR---VLVTNQLHFL-PLMDRIILVSEGMI 817
|
90
....*....|
gi 2551249897 505 VEQGQCEHVF 514
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-237 |
4.65e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 13 VGFRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLlhaNEQTLRDVRgN 92
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-----VEVCGGEIRVNGREI---GAYGLRELR-R 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 93 KIAMIFQEPMvslnplhnlekqlyevlsLHRGMRR-------EAARAEILTCLDRVGIRQ--AAK------RLADYPHQL 157
Cdd:PTZ00243 1385 QFSMIPQDPV------------------LFDGTVRqnvdpflEASSAEVWAALELVGLRErvASEsegidsRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 SGGERQRVMIAMALLTRPELLI-ADEPTT----ALDVSVQAQILQLLRelqhelNMGLLFITHNLSIVKKLaDTVAVMQN 232
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFIlMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDH 1519
|
....*
gi 2551249897 233 GQCVE 237
Cdd:PTZ00243 1520 GAVAE 1524
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-237 |
6.03e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 5 LLAIENLSVGFRQQEtvrtVVNTLSLRVDAGQTLALVGESGSGKSVTALSilrLLPSPPVVYPSGDIRFHGESLLhanEQ 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREDYEVTGGTVEFKGKDLL---EL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 85 TLRDVRGNKIAMIFQEPmVSLNPLHN---LEKQLYEVlslhrgmrREAARAEILTCLDRVGIRQAAKRLADYPHQL---- 157
Cdd:PRK09580 71 SPEDRAGEGIFMAFQYP-VEIPGVSNqffLQTALNAV--------RSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 158 -----SGGERQRVMI-AMALLtRPELLIADEPTTALDVSVQAQILQLLRELQHElNMGLLFITHNLSIVKKLA-DTVAVM 230
Cdd:PRK09580 142 vnvgfSGGEKKRNDIlQMAVL-EPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVL 219
|
....*..
gi 2551249897 231 QNGQCVE 237
Cdd:PRK09580 220 YQGRIVK 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-221 |
9.73e-07 |
|
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: 51.55 E-value: 9.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 157 LSGGERQRVMIAMALLTR---PELLIADEPTTALDVSVQAQILQLLRELQHELNMgLLFITHNLSIVK 221
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNT-VVVIEHNLDVIK 896
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-231 |
1.00e-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: 49.11 E-value: 1.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQ 231
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
310-471 |
1.06e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 310 RPGETLGLVGESGSGKSTTGLALLRLITsqGSIVFDGLALhtLNRRQLLPVRHRIQ--VVFQDPNSslnPRLSVLQIIEE 387
Cdd:TIGR00956 787 KPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRL--VNGRPLDSSFQRSIgyVQQQDLHL---PTSTVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 388 GLRVHQP-TLSAEQREAQVKAVMAEVGLDS--ETRHRYPAE-FSGGQRQRIAIARALILKPSLII-LDEPTSSLDRTVQA 462
Cdd:TIGR00956 860 SAYLRQPkSVSKSEKMEYVEEVIKLLEMESyaDAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939
|
....*....
gi 2551249897 463 QILTLLKSL 471
Cdd:TIGR00956 940 SICKLMRKL 948
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
427-515 |
1.21e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL-TLLK-SLQEKHRlayIFISHDLHVVRALcHQVIVLRQGEV 504
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKdELRGKTR---VLVTNQLHFLSQV-DRIILVHEGMI 817
|
90
....*....|.
gi 2551249897 505 VEQGQCEHVFN 515
Cdd:PLN03130 818 KEEGTYEELSN 828
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
157-229 |
1.28e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 1.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAV 229
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
306-502 |
2.78e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALL-RLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRlSVLQI 384
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYT-SVIKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 --IEEGLrvhqpTLSAEQReaqvKAVMAEVGLdsetrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:TIGR01271 525 cqLEEDI-----ALFPEKD----KTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2551249897 463 QIL--TLLKSLQEKHRlayIFISHDL-HVVRAlcHQVIVLRQG 502
Cdd:TIGR01271 586 EIFesCLCKLMSNKTR---ILVTSKLeHLKKA--DKILLLHEG 623
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
157-221 |
3.11e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.76 E-value: 3.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551249897 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVSVQAQILQLLRELQHElnmgLLFITHNLSIVK 221
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNT----VVVIEHNLDVIK 236
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-230 |
3.56e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 155 HQLSGGERQRVMIAMAL----LTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMgLLFITHNLsIVKKLADTVAVM 230
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLP-ELAELADKLIHI 153
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-234 |
3.73e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLPS--PPVvypSGDIRF-HGESLLH 80
Cdd:PRK10636 311 PLLKMEKVSAGYGD----RIILDSIKLNLVPGSRIGLLGRNGAGKS----TLIKLLAGelAPV---SGEIGLaKGIKLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 81 ANEQTLRDVRGNKIAMifqEPMVSLNPlHNLEKQLYEVLSlhrgmrreaaraeiltcldrvGIRQAAKRLADYPHQLSGG 160
Cdd:PRK10636 380 FAQHQLEFLRADESPL---QHLARLAP-QELEQKLRDYLG---------------------GFGFQGDKVTEETRRFSGG 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMR----QALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
306-488 |
6.07e-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: 47.75 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSL------RPGETLGLVGESGSGKSTTgLALL--RLITSQGS---------IV--FDGLALHTLNRRQL---LPVRHR 363
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTA-LKILagKLKPNLGKfddppdwdeILdeFRGSELQNYFTKLLegdVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 364 IQVVFQDPNSSlnpRLSVLQIIEEglrvhqptlsAEQREAQVKaVMAEVGLDSeTRHRYPAEFSGGQRQRIAIARALILK 443
Cdd:cd03236 93 PQYVDLIPKAV---KGKVGELLKK----------KDERGKLDE-LVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2551249897 444 PSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHDLHV 488
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAV 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-224 |
6.62e-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: 46.21 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 35 GQTLALVGESGSGKSVTALSILRLL--PSPPVVYPSGDIRFHGESLLHANEQTLRDvrgnkiamifqepmvslnplhnle 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELgpPGGGVIYIDGEDILEEVLDQLLLIIVGGK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 113 kqlyevlslhrgmrreaaraeiltcldrvgirqaakrladyPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQ 192
Cdd:smart00382 58 -----------------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180 190
....*....|....*....|....*....|....*..
gi 2551249897 193 AQILQLLR-----ELQHELNMGLLFITHNLSIVKKLA 224
Cdd:smart00382 97 ALLLLLEElrlllLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-227 |
6.79e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 6.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2551249897 157 LSGGERQRVMIAMALLT---RPELLIADEPTTAL---DVSVQAQILQLLRELQHElnmgLLFITHNLSIVkKLADTV 227
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHT----VVIIEHNMHVV-KVADYV 881
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-204 |
7.39e-06 |
|
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: 47.93 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVgfRQQETVRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLpsppvvYPSGDIRFHGESLlhaNEQT 85
Cdd:cd03289 3 MTVKDLTA--KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSW---NSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRgNKIAMIFQEPMVSLNPLH-NLEKqlYEVLSlhrgmrreaaRAEILTCLDRVGIRQAAKR--------LADYPHQ 156
Cdd:cd03289 72 LQKWR-KAFGVIPQKVFIFSGTFRkNLDP--YGKWS----------DEEIWKVAEEVGLKSVIEQfpgqldfvLVDGGCV 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQllRELQH 204
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIR--KTLKQ 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-508 |
7.51e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.86 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 316 GLVGESGSGKSTTgLALLR--LITSQGSIVFDGLALHTlnrrQLLPVRHRIQVVFQDpnsslNPRLSVLQIIEEGLRVHQ 393
Cdd:TIGR01257 960 AFLGHNGAGKTTT-LSILTglLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQH-----NILFHHLTVAEHILFYAQ 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 394 -PTLSAEQREAQVKAVMAEVGLDSEtRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLksLQ 472
Cdd:TIGR01257 1030 lKGRSWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106
|
170 180 190
....*....|....*....|....*....|....*.
gi 2551249897 473 EKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQG 508
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
306-503 |
7.82e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.54 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALL-RLITSQGSIVFDGLALHTLNRRQLLPVRHRIQVVFQDPNSSLNPRlSVLQI 384
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK-SVVKA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 --IEEGLrvhqpTLSAEQReaqvKAVMAEVGLDsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQA 462
Cdd:cd03291 136 cqLEEDI-----TKFPEKD----NTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2551249897 463 QIL--TLLKSLQEKHRlayIFISHDL-HVVRAlcHQVIVLRQGE 503
Cdd:cd03291 197 EIFesCVCKLMANKTR---ILVTSKMeHLKKA--DKILILHEGS 235
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
236-277 |
9.06e-06 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 43.54 E-value: 9.06e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2551249897 236 VEQNRAAQLLTAPTHPYTKKLLNSEPSGDP----VPLPVGQAPLLE 277
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPpkrpLYTIPGNVPSLL 46
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
143-215 |
9.71e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 143 IRQ--AAKRLADYPHQLSGGERQ------RVMIAMALLTRPELLIADEPTTALDV-SVQAQILQLLRELQHELNMGLLFI 213
Cdd:cd03240 100 CHQgeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVI 179
|
..
gi 2551249897 214 TH 215
Cdd:cd03240 180 TH 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
157-242 |
1.01e-05 |
|
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: 47.02 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSIVKKLADTVAVMQnGQCV 236
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPS 194
|
....*.
gi 2551249897 237 EQNRAA 242
Cdd:cd03237 195 VNGVAN 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-227 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 157 LSGGERQRVMIA--MALLTRPELLIADEPTTALDvsvQAQILQLLRELQHELNMG--LLFITHNLSIVkKLADTV 227
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLH---QQDINQLLEVIKGLIDLGntVILIEHNLDVL-SSADWI 158
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-235 |
1.25e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 21 VRTVVNTLSLRVDAGQTLALVGESGSGKSVTALSIL-RLLPSPPVVYPSGDIRFHGE-SLLHANeqTLRDvrgnkiamif 98
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISFSPQtSWIMPG--TIKD---------- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 99 qepmvslNPLHNLEKQLYEVLSLHRGMRREaaraEILTCLDRvgirQAAKRLADYPHQLSGGERQRVMIAMALLTRPELL 178
Cdd:TIGR01271 506 -------NIIFGLSYDEYRYTSVIKACQLE----EDIALFPE----KDKTVLGEGGITLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 179 IADEPTTALDVSVQAQILQ-LLRELQheLNMGLLFITHNLSIVKKlADTVAVMQNGQC 235
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFEsCLCKLM--SNKTRILVTSKLEHLKK-ADKILLLHEGVC 625
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
158-234 |
1.40e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQHELNMGLLFITHNLSI-VKKLADTVAVMQNGQ 234
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGY 288
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
425-499 |
1.45e-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: 45.64 E-value: 1.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFISHDLHVVRALCHQVIVL 499
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
427-501 |
1.49e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 1.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551249897 427 SGGQRQRIAIARALIL---KP-SLIILDEPTSSLDRTVQAQILTLLKSLQeKHRLAYIFISHDLHVVRALCHQVIVLRQ 501
Cdd:cd03227 79 SGGEKELSALALILALaslKPrPLYILDEIDRGLDPRDGQALAEAILEHL-VKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
408-508 |
1.71e-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: 46.45 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 408 VMAEVGLDSETRHRYPAEFSGGQRQRIAIARALiLKPS----LIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAyIFIS 483
Cdd:cd03271 152 TLCDVGLGYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTV-VVIE 229
|
90 100 110
....*....|....*....|....*....|.
gi 2551249897 484 HDLHVVRAlCHQVIVL------RQGEVVEQG 508
Cdd:cd03271 230 HNLDVIKC-ADWIIDLgpeggdGGGQVVASG 259
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-245 |
2.52e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 47.25 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 25 VNTLSLRVDAGQTLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGeSLLHANEQ------TLRDvrgnkiAMIF 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV-----EGHVHMKG-SVAYVPQQawiqndSLRE------NILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 99 QEPmvsLNPlhNLEKQLYEVLSLhrgmrreAARAEILTCLDRVGIRQAAKrladyphQLSGGERQRVMIAMALLTRPELL 178
Cdd:TIGR00957 722 GKA---LNE--KYYQQVLEACAL-------LPDLEILPSGDRTEIGEKGV-------NLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 179 IADEPTTALDVSVQAQIlqllreLQHELN-MGLL------FITHNLSIVKKLaDTVAVMQNGQCVEQNRAAQLL 245
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHI------FEHVIGpEGVLknktriLVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-521 |
2.81e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 275 LLEVEKLRVAF---PIRKGIlkrvvdhnvvvndvSFSLRPGETLGLVGESGSGKSTTGLALL---RLITSQGSIVFDGLA 348
Cdd:PRK09580 1 MLSIKDLHVSVedkAILRGL--------------NLEVRPGEVHAIMGPNGSGKSTLSATLAgreDYEVTGGTVEFKGKD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 349 LHTLNRRQllPVRHRIQVVFQDP------------NSSLNP-----------RLSVLQIIEEGLRVHQPTLSAEQREAQV 405
Cdd:PRK09580 67 LLELSPED--RAGEGIFMAFQYPveipgvsnqfflQTALNAvrsyrgqepldRFDFQDLMEEKIALLKMPEDLLTRSVNV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 406 KavmaevgldsetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISHD 485
Cdd:PRK09580 145 G-------------------FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHY 204
|
250 260 270
....*....|....*....|....*....|....*..
gi 2551249897 486 LHVVRALCHQ-VIVLRQGEVVEQGQCEHVFNAPQQAY 521
Cdd:PRK09580 205 QRILDYIKPDyVHVLYQGRIVKSGDFTLVKQLEEQGY 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
157-188 |
2.85e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 2.85e-05
10 20 30
....*....|....*....|....*....|..
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALD 188
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
157-221 |
3.07e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 3.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 157 LSGGERQRVMIAMALLTRP---ELLIADEPTTAL---DVSvqaqilQLLRELQHELNMG--LLFITHNLSIVK 221
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIR------KLLEVLHRLVDKGntVVVIEHNLDVIK 897
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
412-499 |
3.14e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 412 VGLDSETRHRYPAEFSGGQRQRIAIARALIL---KPSLIILDEPTSSL-DRTVQAQILTLLKSLQEKHRLayIFISHDLH 487
Cdd:PRK00635 796 LGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhTHDIKALIYVLQSLTHQGHTV--VIIEHNMH 873
|
90
....*....|..
gi 2551249897 488 VVRaLCHQVIVL 499
Cdd:PRK00635 874 VVK-VADYVLEL 884
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
427-513 |
3.19e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILK---PSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAyIFISHDLHVVRALCHqVIVL---- 499
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTV-VVIEHNLDVIKTADY-IIDLgpeg 908
|
90
....*....|....*.
gi 2551249897 500 --RQGEVVEQGQCEHV 513
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
306-484 |
3.32e-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: 46.67 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLItsqGSI--VFDGL-------ALHTLNRRQLLPVRH-RIQVVFQDpnssl 375
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSS----LFRIL---GELwpVYGGRltkpakgKLFYVPQRPYMTLGTlRDQIIYPD----- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 376 nprlSVLQIIEEGLRvhqptlsaeqrEAQVKAVMAEVGLDS--------ETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
Cdd:TIGR00954 540 ----SSEDMKRRGLS-----------DKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*..
gi 2551249897 448 ILDEPTSSLDRTVQAQILTLLKslqeKHRLAYIFISH 484
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
427-504 |
6.20e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD-RTVQAQI--LTLLKSlqekhrlAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIqgLVLFQG-------GVLMVSHDEHLISGSVDELWVVSEGK 701
|
.
gi 2551249897 504 V 504
Cdd:PLN03073 702 V 702
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
306-487 |
6.32e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLRLIT-SQGSIVFDGLALHTLNRRQLlpvRHRIQVVFQDpnsslnprlsvlqi 384
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQpQSGEILLDGKPVTAEQPEDY---RKLFSAVFTD-------------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 385 ieeglrVH--QPTLSAEQREAQVKAV---MAEVGLDSETRHR----YPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
Cdd:PRK10522 406 ------FHlfDQLLGPEGKPANPALVekwLERLKMAHKLELEdgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190
....*....|....*....|....*....|....*.
gi 2551249897 456 LD---RTVQAQIltLLKSLQEKHRLayIF-ISHDLH 487
Cdd:PRK10522 480 QDphfRREFYQV--LLPLLQEMGKT--IFaISHDDH 511
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
157-225 |
7.11e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 7.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551249897 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVSVQAQILQLLRELQHElnmgLLFITHNLSIVkKLAD 225
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhDIRKLLEVLHRLVDKGNT----VVVIEHNLDVI-KTAD 896
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-202 |
9.45e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 22 RTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPVVypSGDIRFhgesllhaneqtlrdVRGNKIAMIFQEP 101
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKT-TLLNVLAERVTTGVI--TGGDRL---------------VNGRPLDSSFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 M--VSLNPLHNLEKQLYEVLSLHRGMRR--EAARAEILTCLDRV----GIRQAAKRLADYPHQ-LSGGERQRVMIAMALL 172
Cdd:TIGR00956 838 IgyVQQQDLHLPTSTVRESLRFSAYLRQpkSVSKSEKMEYVEEVikllEMESYADAVVGVPGEgLNVEQRKRLTIGVELV 917
|
170 180 190
....*....|....*....|....*....|.
gi 2551249897 173 TRPELLI-ADEPTTALDVSVQAQILQLLREL 202
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-235 |
1.17e-04 |
|
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: 44.08 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 24 VVNTLSLRVDAGQTLALVGESGSGKSVTALSIL-RLLPSPPVVYPSGDIRFHGE-SLLHANeqTLRDvrgnkiamifqep 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISFSSQfSWIMPG--TIKE------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 102 mvslNPLHNLEKQLYEVLSLhrgmrreaaraeILTCldrvgirQAAKRLADYPHQ-----------LSGGERQRVMIAMA 170
Cdd:cd03291 117 ----NIIFGVSYDEYRYKSV------------VKAC-------QLEEDITKFPEKdntvlgeggitLSGGQRARISLARA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 171 LLTRPELLIADEPTTALDVSVQAQILQ-LLRELQheLNMGLLFITHNLSIVKKlADTVAVMQNGQC 235
Cdd:cd03291 174 VYKDADLYLLDSPFGYLDVFTEKEIFEsCVCKLM--ANKTRILVTSKMEHLKK-ADKILILHEGSS 236
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
306-457 |
1.54e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTtglaLLRLITSQ-----GSIVfdglalhtlnrrqllpVRHRIQVVFQDPN-SSLNPRL 379
Cdd:PRK11819 344 SFSLPPGGIVGIIGPNGAGKST----LFKMITGQeqpdsGTIK----------------IGETVKLAYVDQSrDALDPNK 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 380 SVLQIIEEGLRVhqptLSAEQREAQVKAVMAEVGLDSETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PRK11819 404 TVWEEISGGLDI----IKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
425-499 |
2.01e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551249897 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLD---RTVQAQiltLLKSLQEKHrlAYIFISHDLHVVRALCHQVIVL 499
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqRLNVAR---LIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
401-508 |
2.08e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 401 REAQVKAVMAEV--GLDSETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDRTVQAQIL--TLLKSLQEKHR 476
Cdd:PTZ00243 757 RVSQLEADLAQLggGLETEIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeeCFLGALAGKTR 835
|
90 100 110
....*....|....*....|....*....|..
gi 2551249897 477 layIFISHDLHVVrALCHQVIVLRQGEVVEQG 508
Cdd:PTZ00243 836 ---VLATHQVHVV-PRADYVVALGDGRVEFSG 863
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
306-508 |
2.25e-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: 44.17 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLGLVGESGSGKSTTGLALLR-------LITSQGSIVF---------DGLALHTLNRRQLLPVRHRiQVVfq 369
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAemdkvegHVHMKGSVAYvpqqawiqnDSLRENILFGKALNEKYYQ-QVL-- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 370 dPNSSLNPRLSVLQiieeglrvhqptlSAEQREAQVKAVmaevgldsetrhrypaEFSGGQRQRIAIARALILKPSLIIL 449
Cdd:TIGR00957 735 -EACALLPDLEILP-------------SGDRTEIGEKGV----------------NLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 450 DEPTSSLDRTVQAQILTLLKS----LQEKHRlayIFISHDLHVVRALcHQVIVLRQGEVVEQG 508
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVIGpegvLKNKTR---ILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
306-503 |
3.03e-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: 43.07 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 306 SFSLRPGETLgLVGESGSGKSTTgLALLRLITSQGS-----------------------IVFDGLALHTLNRRQLLPVRH 362
Cdd:COG3593 18 SIELSDDLTV-LVGENNSGKSSI-LEALRLLLGPSSsrkfdeedfylgddpdlpeieieLTFGSLLSRLLRLLLKEEDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 363 RIQVVFQDPNSSLNPRLSVLQ-----IIEEGLRVHQPTLSAEQREAQVKAVMAEVGLdsETRHRYPAEFSG-GQRQRIAI 436
Cdd:COG3593 96 ELEEALEELNEELKEALKALNellseYLKELLDGLDLELELSLDELEDLLKSLSLRI--EDGKELPLDRLGsGFQRLILL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551249897 437 ARALIL-------KPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHrlAYIFIS-HDLHVVRALC-HQVIVLRQGE 503
Cdd:COG3593 174 ALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKP--NQVIITtHSPHLLSEVPlENIRRLRRDS 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-234 |
4.94e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 28 LSLRVDAGQTLALVGESGSGKSvtalSILRLL-----PSPPVVYPSGDIRFHGESLLHANEQTLrdvrgnkiamifqepm 102
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKS----TILKLIsgelqPSSGTVFRSAKVRMAVFSQHHVDGLDL---------------- 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 103 vSLNPLhnlekqLYeVLSLHRGMRREAARAEiltcLDRVGIrqaAKRLADYP-HQLSGGERQRVMIAMALLTRPELLIAD 181
Cdd:PLN03073 588 -SSNPL------LY-MMRCFPGVPEQKLRAH----LGSFGV---TGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLD 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 182 EPTTALDVSVQAQILQLLRELQHelnmGLLFITHNLSIVKKLADTVAVMQNGQ 234
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
156-189 |
7.18e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 7.18e-04
10 20 30
....*....|....*....|....*....|....
gi 2551249897 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
397-525 |
8.76e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 397 SAEQREAQVkavMAEVGLDSEtRHRYP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-RTVQ--AQILTLLKSlq 472
Cdd:PRK15064 130 TAEARAGEL---LLGVGIPEE-QHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDiNTIRwlEDVLNERNS-- 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2551249897 473 ekhrlAYIFISHDLHVVRALCHQVIVLRQGEV-VEQGQCEHVFNAPQQAYTRQL 525
Cdd:PRK15064 204 -----TMIIISHDRHFLNSVCTHMADLDYGELrVYPGNYDEYMTAATQARERLL 252
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
427-457 |
9.18e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 9.18e-04
10 20 30
....*....|....*....|....*....|.
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD 457
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-224 |
1.02e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 6 LAIENLSVGFRQqetvRTVVNTLSLRVDAGQTLALVGESGSGKSvtalSILRLLpsppvvypSGDirfhgeslLHANEQT 85
Cdd:PRK15064 320 LEVENLTKGFDN----GPLFKNLNLLLEAGERLAIIGENGVGKT----TLLRTL--------VGE--------LEPDSGT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 86 LRDVRGNKIAMIFQEPmvslnplhnlEKQLYEVLSLHRGM---RRE-----AARAeiltCLDRV-----GIRQAAKrlad 152
Cdd:PRK15064 376 VKWSENANIGYYAQDH----------AYDFENDLTLFDWMsqwRQEgddeqAVRG----TLGRLlfsqdDIKKSVK---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAqilqllrelqheLNMGL-------LFITHNLSIVKKLA 224
Cdd:PRK15064 438 ---VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES------------LNMALekyegtlIFVSHDREFVSSLA 502
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
407-508 |
1.06e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 407 AVMAEVGLDSETRHRYPAEFSGGQRQRIAIARAL--ILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRlAYIFISH 484
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEH 197
|
90 100
....*....|....*....|....*....
gi 2551249897 485 DLHVVRALCHQVIV-----LRQGEVVEQG 508
Cdd:cd03270 198 DEDTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
427-505 |
1.22e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDrtvqaqiLTLLKSLQ---EKHRLAYIFISHDLHVVRALCHQVIVLRQGE 503
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNmalEKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
..
gi 2551249897 504 VV 505
Cdd:PRK15064 513 VV 514
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-244 |
1.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 4 PLLAIENLSVGFRQQETVRTVVNtLSLRVDAGQTLALVGESGSGKSVTALSILRLLPsppvvypsgdirfhgesllHAnE 83
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSKPTLSD-INLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-------------------HA-E 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 84 QTLRDVRGN-----KIAMIFQePMVSLNPL--HNLEKQLY----EVLSLHRGMRREAARAeiltcLDRVGIRQAakrlad 152
Cdd:PLN03232 672 TSSVVIRGSvayvpQVSWIFN-ATVRENILfgSDFESERYwraiDVTALQHDLDLLPGRD-----LTEIGERGV------ 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQHELN-MGLLFITHNLSIVkKLADTVAVMQ 231
Cdd:PLN03232 740 ---NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC--MKDELKgKTRVLVTNQLHFL-PLMDRIILVS 813
|
250
....*....|...
gi 2551249897 232 NGQCVEQNRAAQL 244
Cdd:PLN03232 814 EGMIKEEGTFAEL 826
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-188 |
2.37e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 2 TQPLLAIENLSvgFRQQETvrTVVNTLSLRVDAGQTLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHA 81
Cdd:PRK13543 8 APPLLAAHALA--FSRNEE--PVFGPLDFHVDAGEALLVQGDNGAGKT-TLLRVLAGLLHVE----SGQIQIDGKTATRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 82 NeqtlrdvRGNKIAMIFQEPMVSLNpLHNLEkQLYEVLSLHrGMRREAARAEILTCLDRVGIRQAAKRladyphQLSGGE 161
Cdd:PRK13543 79 D-------RSRFMAYLGHLPGLKAD-LSTLE-NLHFLCGLH-GRRAKQMPGSALAIVGLAGYEDTLVR------QLSAGQ 142
|
170 180
....*....|....*....|....*..
gi 2551249897 162 RQRVMIAMALLTRPELLIADEPTTALD 188
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
157-204 |
3.42e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 3.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2551249897 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQ--LLRELQH 204
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRG 790
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
441-493 |
3.56e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 40.10 E-value: 3.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2551249897 441 ILKPSLIILDEPTSSLDRTVQAQILTLLKSLQEKHRLAYIFiSHDLHVVRALC 493
Cdd:COG4694 515 DLKKKIVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIVL-THNLYFLKELR 566
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
408-491 |
5.14e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551249897 408 VMAEVGLDsetrhrY-----PA-EFSGGQRQRIAIARALIlKPS----LIILDEPTSSL---DrtvqaqILTLLKSLqek 474
Cdd:COG0178 809 TLQDVGLG------YiklgqPAtTLSGGEAQRVKLASELS-KRStgktLYILDEPTTGLhfhD------IRKLLEVL--- 872
|
90 100
....*....|....*....|..
gi 2551249897 475 HRLA-----YIFISHDLHVVRA 491
Cdd:COG0178 873 HRLVdkgntVVVIEHNLDVIKT 894
|
|
| |
