|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-532 |
0e+00 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 978.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlARHPSGTIEYSGQNLL 80
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDP-AAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKEKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHELSG 160
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQA 240
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 241 SCEQLFRAPQHPYTRELLAAEPSGTPA-TNVVGPPMLTVEDLKVWFPIKKGLLKKTVDYVKAVDGINFSLPQGQTLGIVG 319
Cdd:COG4172 240 PTAELFAAPQHPYTRKLLAAEPRGDPRpVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 320 ESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMG-TEA 398
Cdd:COG4172 320 ESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 399 EQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTY 478
Cdd:COG4172 400 ERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 479 LFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAAFLVP 532
Cdd:COG4172 480 LFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-528 |
0e+00 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 719.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNLLNLKEK 85
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHELSGGQRQR 165
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 246 FRAPQHPYTRELLAAEPSGTP-ATNVVGPPMLTVEDLKVWFPIKKGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSG 324
Cdd:PRK15134 245 FSAPTHPYTQKLLNSEPSGDPvPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 325 KSTLGLAILRLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIH-KMGTEAEQEQA 403
Cdd:PRK15134 325 KSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 404 IIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISH 483
Cdd:PRK15134 405 VIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1834229548 484 DLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAA 528
Cdd:PRK15134 485 DLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-528 |
0e+00 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 643.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLarHPSGTIEYSGQNLLNLK 83
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDV--PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG--RISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EktirHIRGNRIAMIFQEPMTSLNPLhSIEKQINEVLGIHkGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQR 163
Cdd:COG1123 78 E----ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENL-GLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCE 243
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 244 QLFRAPQHPYTRELLAAEPSGTPATNVVGPPMLTVEDLKVWFPIKKGllkktvDYVKAVDGINFSLPQGQTLGIVGESGS 323
Cdd:COG1123 229 EILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESGS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 324 GKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQ 402
Cdd:COG1123 303 GKSTLARLLLGLLRpTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 403 AIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFIS 482
Cdd:COG1123 383 RVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFIS 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1834229548 483 HDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAA 528
Cdd:COG1123 463 HDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-527 |
4.45e-163 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 477.04 E-value: 4.45e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQN-- 78
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 ---LLNLKEKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALP 155
Cdd:PRK10261 87 vieLSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGC 235
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 236 IVEQASCEQLFRAPQHPYTRELLAA---------------------------EPSGTPATNVVGPPMLTVEDLKVWFPIK 288
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAvpqlgamkgldyprrfplislehpakqEPPIEQDTVVDGEPILQVRNLVTRFPLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 289 KGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQVRPLRREMQVV 367
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGeIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 368 FQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALIL 447
Cdd:PRK10261 407 FQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 448 LDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEA 527
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
274-528 |
7.49e-136 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 396.79 E-value: 7.49e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPIKKGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSL 352
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEpTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 353 TQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQR 432
Cdd:COG4608 86 SGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 433 IAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
250
....*....|....*.
gi 1834229548 513 FAAPQHPYTQQLLEAA 528
Cdd:COG4608 246 YARPLHPYTQALLSAV 261
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-266 |
3.93e-134 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 392.11 E-value: 3.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLarHPSGTIEYSGQNLLNLKEK 85
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG--ITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHELSGGQRQR 165
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260
....*....|....*....|.
gi 1834229548 246 FRAPQHPYTRELLAAEPSGTP 266
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDP 259
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-527 |
2.99e-122 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 361.68 E-value: 2.99e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI----GSKGGIRFEGKQLD 350
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-------VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 351 SLTQQQVRPLR-REMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGL-DPETR-HRYPHEFSG 427
Cdd:COG0444 74 KLSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpDPERRlDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 428 GQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|
gi 1834229548 508 DAQSIFAAPQHPYTQQLLEA 527
Cdd:COG0444 234 PVEELFENPRHPYTRALLSS 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-507 |
6.79e-107 |
|
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: 319.07 E-value: 6.79e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLT 353
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGT-EAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQR 432
Cdd:cd03257 74 RRLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 433 IAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-529 |
3.20e-103 |
|
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: 310.20 E-value: 3.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGLlkktvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKqldSLT 353
Cdd:COG1124 1 MLEVRNLSVSYGQGGRR-------VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGR---PVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGteaEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRI 433
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 434 AIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIF 513
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*.
gi 1834229548 514 AAPQHPYTQQLLEAAF 529
Cdd:COG1124 228 AGPKHPYTRELLAASL 243
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-240 |
8.37e-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: 308.28 E-value: 8.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplarHP-SGTIEYSGQNLLNLKE 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL------KPtSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KtIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKvATKRTLELLEMVGIPEPEKRLKALPHELSGGQRQ 164
Cdd:cd03257 75 R-LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKK-EARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQA 240
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-267 |
7.37e-99 |
|
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: 308.37 E-value: 7.37e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVV-GERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLK 83
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR------PtSGSILFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRGnRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQR 163
Cdd:COG1123 334 RRSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPP--DLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCE 243
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|....
gi 1834229548 244 QLFRAPQHPYTRELLAAEPSGTPA 267
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
272-528 |
1.16e-94 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 291.10 E-value: 1.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 272 GPPMLTVEDLKVWFPIKKGLLKKTvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAiLRLIG--SKGGIRFEGKQL 349
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPE-RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARL-LTMIEtpTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQ 429
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250
....*....|....*....
gi 1834229548 510 QSIFAAPQHPYTQQLLEAA 528
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSAT 258
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
274-532 |
2.24e-88 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 275.05 E-value: 2.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPIKKGLL-----KKTVdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGK 347
Cdd:PRK15079 7 VLLEVADLKVHFDIKDGKQwfwqpPKTL---KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 QLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIVGEGLRIH--KMgTEAEQEQAIIAALKEVGLDPETRHRYPHEF 425
Cdd:PRK15079 84 DLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpKL-SRQEVKDRVKAMMLKVGLLPNLINRYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 426 SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVE 505
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
250 260
....*....|....*....|....*..
gi 1834229548 506 QGDAQSIFAAPQHPYTQQLLEAaflVP 532
Cdd:PRK15079 243 LGTYDEVYHNPLHPYTKALMSA---VP 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-267 |
3.42e-88 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 274.69 E-value: 3.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFVV-----GERCQRV--VEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTI 72
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVrgglfGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE------PtSGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 73 EYSGQNLLNLKEKTIRHIRgNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPePEkRLK 152
Cdd:COG4608 76 LFDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PE-HAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 ALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260 270
....*....|....*....|....*....|....*
gi 1834229548 233 RGCIVEQASCEQLFRAPQHPYTRELLAAEPSGTPA 267
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSAVPVPDPE 267
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-262 |
7.93e-84 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 263.14 E-value: 7.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlARHPSGTIEYSGQNLLNLKEK 85
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHELSGGQRQR 165
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*..
gi 1834229548 246 FRAPQHPYTRELLAAEP 262
Cdd:PRK11022 242 FRAPRHPYTQALLRALP 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-262 |
1.59e-83 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 262.74 E-value: 1.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplAR--HPSGTIEYSGQNL 79
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL----AAngRIGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 LNLKEKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHELS 159
Cdd:PRK09473 84 LNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ 239
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260
....*....|....*....|...
gi 1834229548 240 ASCEQLFRAPQHPYTRELLAAEP 262
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGLLNAVP 266
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-260 |
4.73e-80 |
|
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: 250.49 E-value: 4.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLlnlKEK 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKS----TLLRALA-GLERPWSGEVTFDGRPV---TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGnRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLigkVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQR 165
Cdd:COG1124 73 RRKAFRR-RVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP---DREERIAELLEQVGLPP--SFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*
gi 1834229548 246 FRAPQHPYTRELLAA 260
Cdd:COG1124 227 LAGPKHPYTRELLAA 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
274-529 |
4.14e-77 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 243.59 E-value: 4.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPIKKGLLKKTvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSL 352
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQ--QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGeILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 353 -TQQQVRPLRreMqvVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQ 431
Cdd:COG4167 81 dYKYRCKHIR--M--IFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 432 RIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQS 511
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*...
gi 1834229548 512 IFAAPQHPYTQQLLEAAF 529
Cdd:COG4167 237 VFANPQHEVTKRLIESHF 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
265-527 |
3.85e-73 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 235.77 E-value: 3.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 265 TPATNVVGPPMLTVEDLKVWFPIKKGLlkktvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI-- 342
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDGD-------VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIgg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 343 --RFEGKQLDSLTQQQVRPLRRE-MQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLdPETRH 419
Cdd:PRK09473 75 saTFNGREILNLPEKELNKLRAEqISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 420 R---YPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLM 496
Cdd:PRK09473 154 RmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 233
|
250 260 270
....*....|....*....|....*....|.
gi 1834229548 497 VVKQGQVVEQGDAQSIFAAPQHPYTQQLLEA 527
Cdd:PRK09473 234 VMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-263 |
5.69e-65 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 214.38 E-value: 5.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhPSGTIE-----YSGQNL 79
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK------DNWHVTadrfrWNGIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 LNLKEKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVL--GIHKGLIGKVAT---KRTLELLEMVGIPEPEKRLKAL 154
Cdd:COG4170 76 LKLSPRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIpsWTFKGKWWQRFKwrkKRAIELLHRVGIKDHKDIMNSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellkeLQ-----ARL----GMALLLISHDLNLVKRIA 225
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQ---------AQifrllARLnqlqGTSILLISHDLESISQWA 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 1834229548 226 HRVCVMQRGCIVEQASCEQLFRAPQHPYTRELLAAEPS 263
Cdd:COG4170 227 DTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-527 |
1.58e-64 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 213.06 E-value: 1.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGLLKktvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI-----RFEGKQL 349
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQQVRPL-RREMQVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGL-DPETR-HRYPHEFS 426
Cdd:PRK11022 76 QRISEKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpDPASRlDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 427 GGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQ 506
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260
....*....|....*....|.
gi 1834229548 507 GDAQSIFAAPQHPYTQQLLEA 527
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRA 256
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-267 |
3.27e-63 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 209.82 E-value: 3.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 3 QDNLIEVRDLAVEFVV------GERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAhsilRLLPypLARHP-SGTIEYS 75
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLA----RLLT--MIETPtGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 76 GQNLLNlKEKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGI-PEPEKRLkal 154
Cdd:PRK11308 76 GQDLLK-ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRY--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLG 231
|
250 260 270
....*....|....*....|....*....|...
gi 1834229548 235 CIVEQASCEQLFRAPQHPYTRELLAAEPSGTPA 267
Cdd:PRK11308 232 RCVEKGTKEQIFNNPRHPYTQALLSATPRLNPD 264
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
302-527 |
1.32e-62 |
|
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: 206.19 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMC 380
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQ 460
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 461 RQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAApQHPYTQQLLEA 527
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSA 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
272-525 |
7.18e-62 |
|
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: 203.29 E-value: 7.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 272 GPPMLTVEDLKVWFpikkGllKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEG 346
Cdd:COG1127 2 SEPMIEVRNLTKSF----G--DRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVL----LKLIIgllrpDSGEILVDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 347 KQLDSLTQQQVRPLRREMQVVFQDP--FGSLSprmcvsqiVGE----GLRIHKMGTEAEQEQAIIAALKEVGLdPETRHR 420
Cdd:COG1127 67 QDITGLSEKELYELRRRIGMLFQGGalFDSLT--------VFEnvafPLREHTDLSEAEIRELVLEKLELVGL-PGAADK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 421 YPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQ 500
Cdd:COG1127 138 MPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
250 260
....*....|....*....|....*
gi 1834229548 501 GQVVEQGDAQSIFAAPqHPYTQQLL 525
Cdd:COG1127 218 GKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-262 |
2.33e-61 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 204.94 E-value: 2.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDN--LIEVRDLAVEFVVGERCQ---------RVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPS 69
Cdd:PRK15079 1 VTEGKkvLLEVADLKVHFDIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 70 GTIEYSGQNLLNLKEKTIRHIRgNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATK-RTLELLEMVGI-PEP 147
Cdd:PRK15079 76 GEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKdRVKAMMLKVGLlPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 148 EKRLkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHR 227
Cdd:PRK15079 155 INRY---PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDR 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1834229548 228 VCVMQRGCIVEQASCEQLFRAPQHPYTRELLAAEP 262
Cdd:PRK15079 232 VLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
269-524 |
8.25e-60 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 198.50 E-value: 8.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 269 NVVGPPMLTVEDLKVWFpikkgllKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-LRLIGSKGGIRF--- 344
Cdd:COG4107 2 TNEEQPLLSVRGLSKRY-------GPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLyFDLAPTSGSVYYrdr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 345 EGKQLD--SLTQQQVRPLRR-EMQVVFQDPFGSLspRMCVSQI--VGEGL------RIHKMGTEAEQeqaiiaALKEVGL 413
Cdd:COG4107 75 DGGPRDlfALSEAERRRLRRtDWGMVYQNPRDGL--RMDVSAGgnIAERLmaagerHYGDIRARALE------WLERVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 414 DPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSH 493
Cdd:COG4107 147 PLERIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLAD 226
|
250 260 270
....*....|....*....|....*....|.
gi 1834229548 494 QLMVVKQGQVVEQGDAQSIFAAPQHPYTQQL 524
Cdd:COG4107 227 RTMVMKNGRVVESGLTDQVLEDPQHPYTQLL 257
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
303-523 |
1.85e-58 |
|
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: 193.87 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDP--FGSL 375
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTL----LRLIVgllrpDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGalFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SprmcVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLdPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:cd03261 93 T----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAApQHPYTQQ 523
Cdd:cd03261 168 DPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQ 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-267 |
2.82e-58 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 204.32 E-value: 2.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVG----ERCQR---VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQN 78
Cdd:PRK10261 313 ILQVRNLVTRFPLRsgllNRVTRevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV-----ESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LLNLKEKTIRHIRGNrIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIpEPEKRLKaLPHEL 158
Cdd:PRK10261 388 IDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAWR-YPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260
....*....|....*....|....*....
gi 1834229548 239 QASCEQLFRAPQHPYTRELLAAEPSGTPA 267
Cdd:PRK10261 545 IGPRRAVFENPQHPYTRKLMAAVPVADPS 573
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
275-525 |
1.41e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 195.30 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGLlkktvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQL 349
Cdd:COG1135 1 MIELENLSKTFPTKGGP-------VTALDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINllerpTSGSVLVDGVDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQQVRPLRREMQVVFQDpFGSLSPRMcVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQ 429
Cdd:COG1135 70 TALSERELRAARRKIGMIFQH-FNLLSSRT-VAENVALPLEIAGV-PKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250
....*....|....*.
gi 1834229548 510 QSIFAAPQHPYTQQLL 525
Cdd:COG1135 226 LDVFANPQSELTRRFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-517 |
3.15e-57 |
|
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: 190.87 E-value: 3.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQL 349
Cdd:cd03258 1 MIELKNVSKVFGDTGG-------KVTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINglerpTSGSVLVDGTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQQVRPLRREMQVVFQDpFGSLSPRMcVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQ 429
Cdd:cd03258 70 TLLSGKELRKARRRIGMIFQH-FNLLSSRT-VFENVALPLEIAGVP-KAEIEERVLELLELVGLE-DKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*...
gi 1834229548 510 QSIFAAPQ 517
Cdd:cd03258 226 EEVFANPQ 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-514 |
4.66e-56 |
|
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: 196.18 E-value: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHsILRLLP----------YPLARHPS------- 69
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMDqyeptsgriiYHVALCEKcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 70 -----------GTIEYSGQNLLNLKEKTIRHIRgNRIAMIFQEPMTslnpLHSIEKQINEVL-GIHK-GLIGKVATKRTL 136
Cdd:TIGR03269 76 skvgepcpvcgGTLEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTFA----LYGDDTVLDNVLeALEEiGYEGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 137 ELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISH 216
Cdd:TIGR03269 151 DLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 217 DLNLVKRIAHRVCVMQRGCIVEQASCEQLfrapqhpyTRELLAAEPSGTPATNV-VGPPMLTVEDL-KVWFPIKKGLlkk 294
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECEVeVGEPIIKVRNVsKRYISVDRGV--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 295 tvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFE-GKQLDSLTQQqvRPL-----RREMQVV 367
Cdd:TIGR03269 297 ----VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLePTSGEVNVRvGDEWVDMTKP--GPDgrgraKRYIGIL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 368 FQDPfgSLSPRMCVSQIVGEGLRIhKMGTEAEQEQAIIaALKEVGLDPETR----HRYPHEFSGGQRQRIAIARALVLKP 443
Cdd:TIGR03269 371 HQEY--DLYPHRTVLDNLTEAIGL-ELPDELARMKAVI-TLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIKEP 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 444 ALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-260 |
4.95e-56 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 188.37 E-value: 4.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhpSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEPMTS 105
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-------AGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LNPLHSIEKQINEVLGIhkglIGKVATKRTL-ELLEMVGIPEPEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:PRK10418 92 FNPLHTMHTHARETCLA----LGKPADDATLtAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 185 TTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELLAA 260
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
273-520 |
4.39e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 189.15 E-value: 4.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKvwfpikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGK 347
Cdd:COG3842 3 MPALELENVS-----------KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMIAgfetpDSGRILLDGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 QLDSltqqqVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSG 427
Cdd:COG3842 68 DVTG-----LPPEKRNVGMVFQDY--ALFPHLTVAENVAFGLRMRGVP-KAEIRARVAELLELVGLE-GLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 428 GQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
|
250
....*....|...
gi 1834229548 508 DAQSIFAAPQHPY 520
Cdd:COG3842 219 TPEEIYERPATRF 231
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
6-260 |
8.24e-55 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 185.40 E-value: 8.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGERCQRVV--EGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLARHpSGTIEYSG-----QN 78
Cdd:COG4107 8 LLSVRGLSKRY--GPGCGTVVacRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPT-SGSVYYRDrdggpRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LLNLKEKTIRHIRGNRIAMIFQEPMTSLNPLHS-----IEKQIneVLGI-HKGLIgkvaTKRTLELLEMVGIPEpeKRLK 152
Cdd:COG4107 81 LFALSEAERRRLRRTDWGMVYQNPRDGLRMDVSaggniAERLM--AAGErHYGDI----RARALEWLERVEIPL--ERID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 ALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:COG4107 153 DLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMK 232
|
250 260
....*....|....*....|....*...
gi 1834229548 233 RGCIVEQASCEQLFRAPQHPYTRELLAA 260
Cdd:COG4107 233 NGRVVESGLTDQVLEDPQHPYTQLLVSS 260
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
275-535 |
1.38e-53 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 182.30 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGLLKKtvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLD--- 350
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 351 -SLTQQQVRplrremqVVFQDPFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQ 429
Cdd:PRK15112 82 ySYRSQRIR-------MIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
250 260
....*....|....*....|....*.
gi 1834229548 510 QSIFAAPQHPYTQQLLEAAFLVPATA 535
Cdd:PRK15112 235 ADVLASPLHELTKRLIAGHFGEALTA 260
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-271 |
1.42e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.51 E-value: 1.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS----TLIRCINL-LERPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGnRIAMIFQEP--MTSLN-------PLhsiekqinEVLGIHKGLIgkvaTKRTLELLEMVGIpepEKRLKALPHE 157
Cdd:COG1135 77 LRAARR-KIGMIFQHFnlLSSRTvaenvalPL--------EIAGVPKAEI----RKRVAELLELVGL---SDKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALD-------------VtvqlkilellkelQARLGMALLLISHDLNLVKRI 224
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsildllkdI-------------NRELGLTIVLITHEMDVVRRI 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1834229548 225 AHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELLAAEPSGTPATNVV 271
Cdd:COG1135 208 CDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELL 254
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-262 |
4.24e-53 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 183.08 E-value: 4.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLaRHPSGTIEYSGQNLLNLKEK 85
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNW-RVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLG--IHKGLIGKV---ATKRTLELLEMVGIPEPEKRLKALPHELSG 160
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPgwTYKGRWWQRfgwRKRRAIELLHRVGIKDHKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQA 240
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260
....*....|....*....|..
gi 1834229548 241 SCEQLFRAPQHPYTRELLAAEP 262
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIP 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
302-527 |
3.02e-52 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 178.73 E-value: 3.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMC 380
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRiHKMG-TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTV 459
Cdd:PRK10419 108 VREIIREPLR-HLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 460 QRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQ---GDAQSIfaapQHPYTQQLLEA 527
Cdd:PRK10419 187 QAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKLTF----SSPAGRVLQNA 253
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
299-517 |
9.35e-52 |
|
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: 175.98 E-value: 9.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDPFgslsp 377
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDGK---DITKKNLRELRRKVGLVFQNPD----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 rmcvSQIVGE--------GLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:COG1122 86 ----DQLFAPtveedvafGPENLGL-PREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-250 |
2.23e-51 |
|
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: 175.46 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLLNLKEK 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS----TLIRCING-LERPTSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRgNRIAMIFQE--PMTSLNPLHSIEKQInEVLGIHKgligKVATKRTLELLEMVGIpepEKRLKALPHELSGGQR 163
Cdd:cd03258 76 ELRKAR-RRIGMIFQHfnLLSSRTVFENVALPL-EIAGVPK----AEIEERVLELLELVGL---EDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCE 243
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 1834229548 244 QLFRAPQ 250
Cdd:cd03258 227 EVFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-259 |
4.87e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.41 E-value: 4.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLlNLKEK 85
Cdd:COG1126 1 MIEIENLHKSF--GD--LEVLKGISLDVEKGEVVVIIGPSGSGKS----TLLRCINL-LEEPDSGTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGnRIAMIFQE----P-MTSL-N----PLHsiekqineVLGIHKgligKVATKRTLELLEMVGIPEpekRLKALP 155
Cdd:COG1126 71 DINKLRR-KVGMVFQQfnlfPhLTVLeNvtlaPIK--------VKKMSK----AEAEERAMELLERVGLAD---KADAYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALD---------VTVQLkilellkelqARLGMALLLISHDLNLVKRIAH 226
Cdd:COG1126 135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevldVMRDL----------AKEGMTMVVVTHEMGFAREVAD 204
|
250 260 270
....*....|....*....|....*....|...
gi 1834229548 227 RVCVMQRGCIVEQASCEQLFRAPQHPYTRELLA 259
Cdd:COG1126 205 RVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-526 |
2.34e-50 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.87 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFpikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQL 349
Cdd:COG1126 1 MIEIENLHKSF-----------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTL----LRCINlleepDSGTITVDGEDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DsLTQQQVRPLRREMQVVFQDpFgSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLdPETRHRYPHEFSGGQ 429
Cdd:COG1126 66 T-DSKKDINKLRRKVGMVFQQ-F-NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL-ADKADAYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALD-RTVQrQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGD 508
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250
....*....|....*...
gi 1834229548 509 AQSIFAAPQHPYTQQLLE 526
Cdd:COG1126 220 PEEFFENPQHERTRAFLS 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-260 |
2.79e-50 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 173.48 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFVVGERCQR-----VVEGVSFDIKRGETLALVGESGSGKSVtahsilrllpypLARHPSGTIE-YSGQN 78
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKST------------LAKMLAGIIEpTSGEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LLN---LKEKTIRHiRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGI-PEpekrlKAL 154
Cdd:COG4167 71 LINghkLEYGDYKY-RCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPE-----HAN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 --PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:COG4167 145 fyPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMH 224
|
250 260
....*....|....*....|....*...
gi 1834229548 233 RGCIVEQASCEQLFRAPQHPYTRELLAA 260
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
273-506 |
3.54e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 171.76 E-value: 3.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGK 347
Cdd:COG1136 2 SPLLELRNLTKSYGTGEG-------EVTALRGVSLSIEAGEFVAIVGPSGSGKSTL----LNILGgldrpTSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 QLDSLTQQQVRPLRRE-MQVVFQDPFgsLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDpETRHRYPHEFS 426
Cdd:COG1136 71 DISSLSERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVSRKERRERAR-ELLERVGLG-DRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 427 GGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLmVVKQGQVVEQ 506
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVI-RLRDGRIVSD 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
299-529 |
5.85e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 174.99 E-value: 5.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDpFG 373
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINllerpTSGRVLVDGQDLTALSEKELRKARRQIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SLSPRMcVSQIVGEGLRIhkMGTEAEQEQAIIAALKE-VGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPT 452
Cdd:PRK11153 93 LLSSRT-VFDNVALPLEL--AGTPKAEIKARVTELLElVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 453 SALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAAF 529
Cdd:PRK11153 169 SALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTL 245
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-258 |
7.65e-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: 171.32 E-value: 7.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 3 QDNLIEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLN 81
Cdd:COG1127 2 SEPMIEVRNLTKSF--GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR------PdSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHIRgNRIAMIFQEP--MTSLN-------PLhsIEkqinevlgiHKGLIGKVATKRTLELLEMVGIPEPEKRLk 152
Cdd:COG1127 72 LSEKELYELR-RRIGMLFQGGalFDSLTvfenvafPL--RE---------HTDLSEAEIRELVLEKLELVGLPGAADKM- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 alPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-----VTVQlkileLLKELQARLGMALLLISHDLNLVKRIAHR 227
Cdd:COG1127 139 --PSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsaVIDE-----LIRELRDELGLTSVVVTHDLDSAFAIADR 211
|
250 260 270
....*....|....*....|....*....|.
gi 1834229548 228 VCVMQRGCIVEQASCEQLfRAPQHPYTRELL 258
Cdd:COG1127 212 VAVLADGKIIAEGTPEEL-LASDDPWVRQFL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
292-507 |
7.96e-50 |
|
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: 170.39 E-value: 7.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTqqqvrPLRREMQV 366
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVP-----PERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDPEtRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03259 77 VFQDY--ALFPHLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
274-524 |
2.24e-49 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 170.88 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKvwfpikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-LRLIGSKGGIRF---EGKQL 349
Cdd:PRK11701 5 PLLSVRGLT-----------KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYrmrDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 D--SLTQQQVRPL-RREMQVVFQDPFGSLspRMCVSQ--IVGEGLrihkMGTEAEQEQAIIAA----LKEVGLDPETRHR 420
Cdd:PRK11701 74 DlyALSEAERRRLlRTEWGFVHQHPRDGL--RMQVSAggNIGERL----MAVGARHYGDIRATagdwLERVEIDAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 421 YPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQ 500
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260
....*....|....*....|....
gi 1834229548 501 GQVVEQGDAQSIFAAPQHPYTQQL 524
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYTQLL 251
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
292-536 |
3.84e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.02 E-value: 3.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSltqqQVRPLRREMQV 366
Cdd:COG1118 8 ISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTL----LRIIAgletpDSGRIVLNGRDLFT----NLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:COG1118 80 VFQHY--ALFPHMTVAENIAFGLRVRPPS-KAEIRARVEELLELVQLE-GLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLE 526
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235
|
250
....*....|
gi 1834229548 527 AAFLVPATAQ 536
Cdd:COG1118 236 CVNVLRGRVI 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
299-503 |
4.26e-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: 166.13 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLRRE-MQVVFQDPf 372
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGgldrpTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 gSLSPRMCVSQIVGEGLRIHKMGTeAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPT 452
Cdd:cd03255 92 -NLLPDLTALENVELPLLLAGVPK-KERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 453 SALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKaLSHQLMVVKQGQV 503
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
273-505 |
4.80e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 167.19 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGK 347
Cdd:COG1116 5 APALELRGVSKRFPTGGG-------GVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIAglekpTSGEVLVDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 QldsltqqqVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGTeAEQEQAIIAALKEVGLDpETRHRYPHEFSG 427
Cdd:COG1116 74 P--------VTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPK-AERRERARELLELVGLA-GFEDAYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 428 GQRQRIAIARALVLKPALILLDEPTSALD----RTVQrqvvELLRSLQSKYNLTYLFISHDL--AVvkALSHQLMVVKQ- 500
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDaltrERLQ----DELLRLWQETGKTVLFVTHDVdeAV--FLADRVVVLSAr 215
|
....*.
gi 1834229548 501 -GQVVE 505
Cdd:COG1116 216 pGRIVE 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-239 |
9.58e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.60 E-value: 9.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLpyplaRHP-SGTIEYSGQNLLNL 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGL-----DRPtSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 KEKTIRHIRGNRIAMIFQEPmtSLNPLHSIEKQINEVLGIhKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQ 162
Cdd:COG1136 76 SERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGL---GDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQ 239
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-234 |
1.47e-47 |
|
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: 164.59 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLNIL-GGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRIAMIFQEPmtSLNPLHSIEKQInEVLGIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRV 166
Cdd:cd03255 76 LAAFRRRHIGFVFQSF--NLLPDLTALENV-ELPLLLAGVPKKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRG 234
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
300-502 |
1.49e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.56 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTqqqVRPLRREMQVVFQDPFgslspr 378
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLS---LKELRRKVGLVFQNPD------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 mcvSQIVGE--------GLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:cd03225 86 ---DQFFGPtveeevafGLENLGL-PEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
273-528 |
8.50e-47 |
|
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: 163.85 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKvwfpikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGK---- 347
Cdd:TIGR02323 1 KPLLQVSGLS-----------KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAPDHGTATYIMRsgae 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 -QLDSLTQQQVRPL-RREMQVVFQDPFGSLspRMCVSQIVGEGLRIHKMGTE--AEQEQAIIAALKEVGLDPETRHRYPH 423
Cdd:TIGR02323 70 lELYQLSEAERRRLmRTEWGFVHQNPRDGL--RMRVSAGANIGERLMAIGARhyGNIRATAQDWLEEVEIDPTRIDDLPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 424 EFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:TIGR02323 148 AFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250 260
....*....|....*....|....*
gi 1834229548 504 VEQGDAQSIFAAPQHPYTQQLLEAA 528
Cdd:TIGR02323 228 VESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-506 |
1.57e-46 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 161.87 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGkqld 350
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAglerpTSGEVLVDG---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 351 sltqQQVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDpETRHRYPHEFSGGQR 430
Cdd:cd03293 66 ----EPVTGPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAE-ELLELVGLS-GFENAYPHQLSGGMR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 431 QRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDL--AVvkALSHQLMVVKQ--GQVVEQ 506
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAV--FLADRVVVLSArpGRIVAE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-256 |
2.52e-46 |
|
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: 161.90 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNLKEKT 86
Cdd:cd03261 1 IELRGLTKSF--GGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PD----SGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQEP--MTSLNPLHSIEKQINEvlgiHKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQ 164
Cdd:cd03261 72 LYRLR-RRMGMLFQSGalFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAEDLY---PAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQ 244
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
250
....*....|..
gi 1834229548 245 LFRApQHPYTRE 256
Cdd:cd03261 224 LRAS-DDPLVRQ 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-534 |
9.71e-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: 160.98 E-value: 9.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVwfpikkGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLT 353
Cdd:COG1120 1 MLEAENLSV------GYGGRPV-----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGeVLLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQvrpLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHK--MGTEAEQEQAIIA-ALKEVGLDpETRHRYPHEFSGGQR 430
Cdd:COG1120 70 RRE---LARRIAYVPQEP--PAPFGLTVRELVALGRYPHLglFGRPSAEDREAVEeALERTGLE-HLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 431 QRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQ 510
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
250 260
....*....|....*....|....
gi 1834229548 511 SIFaapqhpyTQQLLEAAFLVPAT 534
Cdd:COG1120 224 EVL-------TPELLEEVYGVEAR 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
299-505 |
3.65e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 158.29 E-value: 3.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDpFG 373
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTL----LKLLYgeerpTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 sLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:COG2884 90 -LLPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 454 ALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVE 505
Cdd:COG2884 167 NLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
299-528 |
9.69e-45 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 160.84 E-value: 9.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI-----RFEGKQLDSLTQQQVRPL-RREMQVVFQDPF 372
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrfRWNGIDLLKLSPRERRKIiGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 GSLSPrmcvSQIVGEGL---------RIHKMGTEAEQEQAIIAALKEVGL-DPETRHR-YPHEFSGGQRQRIAIARALVL 441
Cdd:COG4170 100 SCLDP----SAKIGDQLieaipswtfKGKWWQRFKWRKKRAIELLHRVGIkDHKDIMNsYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 442 KPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYT 521
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYT 255
|
....*..
gi 1834229548 522 QQLLEAA 528
Cdd:COG4170 256 KALLRSM 262
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-272 |
1.27e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 158.31 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAhsilRLLpYPLARHPSGTIEYSGQNLLNLKEKTIRHIRGNrIAMIFQEP 102
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLA----RLL-VGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:PRK10419 99 ISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRApQHPYTRELLAAEP 262
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF-SSPAGRVLQNAVL 255
|
250
....*....|
gi 1834229548 263 SGTPATNVVG 272
Cdd:PRK10419 256 PAFPVRRRTT 265
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
274-504 |
1.70e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.53 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQ 348
Cdd:COG3638 1 PMLELRNLSKRYP----------GGTPALDDVSLEIERGEFVALIGPSGAGKSTL----LRCLNglvepTSGEILVDGQD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDSLTQQQVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGlRIHKMGT---------EAEQEQAIiAALKEVGLDPETRH 419
Cdd:COG3638 67 VTALRGRALRRLRRRIGMIFQQF--NLVPRLSVLTNVLAG-RLGRTSTwrsllglfpPEDRERAL-EALERVGLADKAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 420 RyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVK 499
Cdd:COG3638 143 R-ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLR 221
|
....*
gi 1834229548 500 QGQVV 504
Cdd:COG3638 222 DGRVV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
288-520 |
2.08e-44 |
|
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: 157.81 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 288 KKGLLKKTvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRPLRRE-MQ 365
Cdd:cd03294 27 KEEILKKT-GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSRKELRELRRKkIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 366 VVFQDpFGsLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDPEtRHRYPHEFSGGQRQRIAIARALVLKPAL 445
Cdd:cd03294 106 MVFQS-FA-LLPHRTVLENVAFGLEVQGVP-RAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPY 520
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
292-517 |
8.02e-44 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 155.09 E-value: 8.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLdsltqQQVRPLRREMQV 366
Cdd:cd03300 6 VSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGKDI-----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03300 77 VFQNY--ALFPHLTVFENIAFGLRLKKLP-KAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-245 |
1.33e-42 |
|
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: 151.56 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:cd03260 1 IELRDLNVYY--GDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgnRIAMIFQEPmtslNPLH-SIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRlKALPHELSGGQRQR 165
Cdd:cd03260 77 LELRR--RVGMVFQKP----NPFPgSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTvqLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPI--STAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-512 |
1.63e-42 |
|
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: 151.56 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVWFpikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG------SKGGIRFEGKQL 349
Cdd:cd03260 1 IELRDLNVYY-----------GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLtQQQVRPLRREMQVVFQ--DPFgslspRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPET-RHRYPHEFS 426
Cdd:cd03260 70 YDL-DVDVLELRRRVGMVFQkpNPF-----PGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVkDRLHALGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 427 GGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYnlTYLFISHDLAVVKALSHQLMVVKQGQVVEQ 506
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
....*.
gi 1834229548 507 GDAQSI 512
Cdd:cd03260 222 GPTEQI 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
300-536 |
1.92e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 152.99 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDP--- 371
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLiqhlnGL----LKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPehq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 -----------FGslsPRMcvsqivgeglrihkMG-TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARAL 439
Cdd:TIGR04521 95 lfeetvykdiaFG---PKN--------------LGlSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 440 VLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPqhp 519
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV--- 234
|
250
....*....|....*...
gi 1834229548 520 ytqQLLEAAFL-VPATAQ 536
Cdd:TIGR04521 235 ---DELEKIGLdVPEITE 249
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
300-525 |
4.42e-42 |
|
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: 150.91 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDPfgSLSPR 378
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGE---DIREQDPVELRRKIGYVIQQI--GLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDPET-RHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:cd03295 90 MTVEENIALVPKLLKWPKEKIRERAD-ELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 458 TVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLL 525
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-250 |
5.61e-42 |
|
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: 150.18 E-value: 5.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLlnlKEKT 86
Cdd:COG1122 1 IELENLSFSYP-GGT--PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL-----KPTSGEVLVDGKDI---TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQEPmtslnplhsiEKQI------NEV-LG-IHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHEL 158
Cdd:COG1122 70 LRELR-RKVGLVFQNP----------DDQLfaptveEDVaFGpENLGLPREEIRERVEEALELVGL---EHLADRPPHEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDvtvqlkilellKELQARL----------GMALLLISHDLNLVKRIAHRV 228
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD-----------PRGRRELlellkrlnkeGKTVIIVTHDLDLVAELADRV 204
|
250 260
....*....|....*....|..
gi 1834229548 229 CVMQRGCIVEQASCEQLFRAPQ 250
Cdd:COG1122 205 IVLDDGRIVADGTPREVFSDYE 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-260 |
7.40e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.03 E-value: 7.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS----TLIRCINL-LERPTSGRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQEpmtsLNPLHSIEKQIN-----EVLGIHKGLIgkvaTKRTLELLEMVGIPEpeKRlKALPHELSGG 161
Cdd:PRK11153 77 LRKAR-RQIGMIFQH----FNLLSSRTVFDNvalplELAGTPKAEI----KARVTELLELVGLSD--KA-DRYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQAS 241
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
250
....*....|....*....
gi 1834229548 242 CEQLFRAPQHPYTRELLAA 260
Cdd:PRK11153 225 VSEVFSHPKHPLTREFIQS 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-504 |
7.92e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.72 E-value: 7.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEF--VvgercqRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILrllpyplA---RHPSGTIEYSGQN 78
Cdd:COG1129 2 EPLLEMRGISKSFggV------KALDGVSLELRPGEVHALLGENGAGKS-TLMKIL-------SgvyQPDSGEILLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LlnlKEKTIRHIRGNRIAMIFQEPmtSLNPLHSIEKQIneVLG---IHKGLIGKVAT-KRTLELLEMVGIPE-PEKRLKa 153
Cdd:COG1129 68 V---RFRSPRDAQAAGIAIIHQEL--NLVPNLSVAENI--FLGrepRRGGLIDWRAMrRRARELLARLGLDIdPDTPVG- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 lphELSGGQRQRVMIAMALANEPELLIADEPTTALDVT-VQlkilellkelqaRL----------GMALLLISHDLNLVK 222
Cdd:COG1129 140 ---DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVE------------RLfriirrlkaqGVAIIYISHRLDEVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 223 RIAHRVCVMQRGCIVEQASCEQLfrapqhpyT----------RELLAAEPSGTPATnvvGPPMLTVEDLKVWfpikkgll 292
Cdd:COG1129 205 EIADRVTVLRDGRLVGTGPVAEL--------TedelvrlmvgRELEDLFPKRAAAP---GEVVLEVEGLSVG-------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 293 kktvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDsltqqqvrpLRremqvvfqdp 371
Cdd:COG1129 266 -------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGeIRLDGKPVR---------IR---------- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 fgslSPRMCVSQ-IV-------GEGL----------------RIHKMG--TEAEQEQAIIAALKEVGLDPETRHRYPHEF 425
Cdd:COG1129 320 ----SPRDAIRAgIAyvpedrkGEGLvldlsirenitlasldRLSRGGllDRRRERALAEEYIKRLRIKTPSPEQPVGNL 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 426 SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
275-530 |
1.17e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 149.62 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKvwfpikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGKQL 349
Cdd:COG4555 1 MIEVENLS-----------KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLagllkPDSGSILIDGEDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 dsltQQQVRPLRREMQVVFQDPFgsLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQ 429
Cdd:COG4555 66 ----RKEPREARRQIGVLPDERG--LYDRLTVRENIRYFAELYGL-FDEELKKRIEELIELLGLE-EFLDRRVGELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
250 260
....*....|....*....|.
gi 1834229548 510 QSIFAApqhpYTQQLLEAAFL 530
Cdd:COG4555 217 DELREE----IGEENLEDAFV 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
299-502 |
1.64e-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: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQqVRPLRREMQVVFQDPfg 373
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAgleepDSGSILIDGEDLTDLEDE-LPPLRRRIGMVFQDF-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SLSPRMCVSQIVGEGLrihkmgteaeqeqaiiaalkevgldpetrhryphefSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:cd03229 86 ALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834229548 454 ALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
292-530 |
2.51e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-G----SKGGIRFEGKQLDSLTQQqvrpLRREMQV 366
Cdd:COG1131 6 LTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRMLlGllrpTSGEVRVLGEDVARDPAE----VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:COG1131 78 VPQEP--ALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIfaapqhpyTQQLLE 526
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL--------KARLLE 224
|
....
gi 1834229548 527 AAFL 530
Cdd:COG1131 225 DVFL 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
303-503 |
4.67e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.88 E-value: 4.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDP--FGslsprm 379
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDpPTSGEIYLDGKPLSAMPPPE---WRRQVAYVPQEPalWG------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cvsQIVGEGL-RIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:COG4619 88 ---GTVRDNLpFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 459 VQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:COG4619 165 NTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
299-514 |
5.34e-41 |
|
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: 148.73 E-value: 5.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGkqLDSLTQQQVRPLRREMQVVFQDP-- 371
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLakllnGL----LLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVFQNPdn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 -FgslsprmcVSQIVGE----GLriHKMGTEAEQEQAIIA-ALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPAL 445
Cdd:TIGR04520 89 qF--------VGATVEDdvafGL--ENLGVPREEMRKRVDeALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-256 |
6.04e-41 |
|
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: 148.56 E-value: 6.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQE--P 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE------PtSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSfaL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNPLHSIEKQInEVLGIHKgligKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03294 114 LPHRTVLENVAFGL-EVQGVPR----AEREERAAEALELVGL---EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRE 256
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
292-518 |
1.14e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.22 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-G----SKGGIRFEGKQLDSLtqqqvRPLRREMQV 366
Cdd:COG3839 9 VSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIaGledpTSGEILIGGRDVTDL-----PPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:COG3839 80 VFQSY--ALYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQH 518
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
25-238 |
2.07e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.58 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYpLARHP-SGTIEYSGQNLLNLKEKTIRHIRgNRIAMIFQE-- 101
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLL-Y-GEERPtSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQDfr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 -------------PMtslnplhsiekqinEVLGIHKGLIGkvatKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMI 168
Cdd:COG2884 90 llpdrtvyenvalPL--------------RVTGKSRKEIR----RRVREVLDLVGL---SDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 169 AMALANEPELLIADEPTTALDvtvqlkilellkELQA-----------RLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLD------------PETSweimelleeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
.
gi 1834229548 238 E 238
Cdd:COG2884 217 R 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
305-525 |
2.38e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.67 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLtqqqvRPLRREMQVVFQDpfGSLSPRM 379
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTL----LNLIAgflppDSGRILWNGQDLTAL-----PPAERPVSMLFQE--NNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVGEGLRiHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTV 459
Cdd:COG3840 87 TVAQNIGLGLR-PGLKLTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 460 QRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLL 525
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
301-520 |
3.32e-40 |
|
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: 154.99 E-value: 3.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---GSLS 376
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDPAS---LRRQIGVVLQDVFlfsGTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcvsqivgEGLRIHKmgTEAEQEQaIIAALKEVGLDPETRHRyPH-----------EFSGGQRQRIAIARALVLKPAL 445
Cdd:COG2274 567 ----------ENITLGD--PDATDEE-IIEAARLAGLHDFIEAL-PMgydtvvgeggsNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLqsKYNLTYLFISHDLAVVKaLSHQLMVVKQGQVVEQGDAQSIFAAPQHPY 520
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
302-517 |
5.37e-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: 144.79 E-value: 5.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTqqqvrPLRREMQVVFQDPfgSLSPRMC 380
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkILLNGKDITNLP-----PEKRDISYVPQNY--ALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRiHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQ 460
Cdd:cd03299 88 VYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 461 RQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
303-505 |
6.01e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 144.42 E-value: 6.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLR-REMQVVFQdpFGSLS 376
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTL----LHLLGgldnpTSGEVLFNGQSLSKLSSNERAKLRnKKLGFIYQ--FHHLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 PRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:TIGR02211 96 PDFTALENVAMPLLIGKK-SVKEAKERAYEMLEKVGLEHRINHR-PSELSGGERQRVAIARALVNQPSLVLADEPTGNLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834229548 457 RTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALShQLMVVKQGQVVE 505
Cdd:TIGR02211 174 NNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEMKDGQLFN 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
302-453 |
1.42e-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: 140.86 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLdslTQQQVRPLRREMQVVFQDPFgsLSPRMC 380
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 381 VSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGL--DPETR-HRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAE-EALEKLGLgdLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
239-510 |
1.67e-39 |
|
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: 151.45 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 239 QASCEQLFRAPQHPytrelLAAEPSGTPATNVVGPPMLTVEDLKVWFPikkgllkktvDYVKAVDGINFSLPQGQTLGIV 318
Cdd:COG4988 305 IAAAEKIFALLDAP-----EPAAPAGTAPLPAAGPPSIELEDVSFSYP----------GGRPALDGLSLTIPPGERVALV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 319 GESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---GSLSprmcvsqivgEGLRihkM 394
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPpYSGSILINGVDLSDLDPAS---WRRQIAWVPQNPYlfaGTIR----------ENLR---L 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 395 GTEAEQEQAIIAALKEVGLDPETRhRYPHEF-----------SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQV 463
Cdd:COG4988 434 GRPDASDEELEAALEAAGLDEFVA-ALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1834229548 464 VELLRSLqSKyNLTYLFISHDLAVVKALSHQLmVVKQGQVVEQGDAQ 510
Cdd:COG4988 513 LQALRRL-AK-GRTVILITHRLALLAQADRIL-VLDDGRIVEQGTHE 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-504 |
1.70e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 150.18 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvTAHSILrllpYPLARHPSGTIEYSGqnllnlKEKTI---RHIRGNRIAMIFQEPMt 104
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKS-TLMKIL----YGLYQPDSGEILIDG------KPVRIrspRDAIALGIGMVHQHFM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 sLNPLHS-IEkqiNEVLGIHKGLIG----KVATKRTLELLEMVGIP-EPEkrlkALPHELSGGQRQRVMIAMALANEPEL 178
Cdd:COG3845 91 -LVPNLTvAE---NIVLGLEPTKGGrldrKAARARIRELSERYGLDvDPD----AKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 179 LIADEPTTALdvTVQLKILELLKELQ-ARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLfrapqhpyTREL 257
Cdd:COG3845 163 LILDEPTAVL--TPQEADELFEILRRlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET--------SEEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 258 LAA-------EPSGTPATNVVGPPMLTVEDLKVwfpikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGL 330
Cdd:COG3845 233 LAElmvgrevLLRVEKAPAEPGEVVLEVENLSV----------RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 331 AI--LRLIgSKGGIRFEGKQLDSLTQQQvrplRREMQVVF--QDPFGS-LSPRMCVSQ--IVGEG----------LRIHK 393
Cdd:COG3845 303 ALagLRPP-ASGSIRLDGEDITGLSPRE----RRRLGVAYipEDRLGRgLVPDMSVAEnlILGRYrrppfsrggfLDRKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 394 MGTEAEQeqaIIAALKEVGLDPETRHRyphEFSGGQRQRIAIARALVLKPALILLDEPTSALD----RTVQRQVVELLRS 469
Cdd:COG3845 378 IRAFAEE---LIEEFDVRTPGPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRDA 451
|
490 500 510
....*....|....*....|....*....|....*
gi 1834229548 470 lqskyNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:COG3845 452 -----GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-245 |
4.30e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.89 E-value: 4.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLKE 84
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE------PtSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KTIRHIRGnRIAMIFQEPmtslnPLhsIEKQ--INEVL-------GIHKGLIGKVATK---RTLELLEMVGIPEpekrlK 152
Cdd:COG3638 73 RALRRLRR-RIGMIFQQF-----NL--VPRLsvLTNVLagrlgrtSTWRSLLGLFPPEdreRALEALERVGLAD-----K 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 AL--PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCV 230
Cdd:COG3638 140 AYqrADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
250
....*....|....*
gi 1834229548 231 MQRGCIVEQASCEQL 245
Cdd:COG3638 220 LRDGRVVFDGPPAEL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
289-512 |
4.39e-39 |
|
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: 142.71 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 289 KGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLTQQQVRPLRREMQVV 367
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTDINKLKGKALRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 368 FQDPfgSLSPRMCVSQIVGEG-------LR-IHKMGTEAEQEQAIiAALKEVGLDPETRHRyPHEFSGGQRQRIAIARAL 439
Cdd:cd03256 84 FQQF--NLIERLSVLENVLSGrlgrrstWRsLFGLFPKEEKQRAL-AALERVGLLDKAYQR-ADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 440 VLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-245 |
8.11e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 141.74 E-value: 8.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLKEK 85
Cdd:COG1131 1 IEVRGLTKRY--GDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR------PtSGEVRVLGEDVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhirgnRIAMIFQEPmtSLNPLHSIEKQINEVLGIHkGLIGKVATKRTLELLEMVGIPEpekRLKALPHELSGGQRQR 165
Cdd:COG1131 71 VRR-----RIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVtVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDP-EARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-240 |
1.12e-38 |
|
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: 140.73 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKekt 86
Cdd:cd03259 1 LELKGLSKTY--GS--VRALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIA-GLERPDSGEILIDGRDVTGVP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 irhIRGNRIAMIFQEPmtSLNPLHSIEKQIneVLGIHKGLIGK-VATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQR 165
Cdd:cd03259 69 ---PERRNIGMVFQDY--ALFPHLTVAENI--AFGLKLRGVPKaEIRARVRELLELVGLEGLLNRY---PHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQA 240
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-261 |
1.18e-38 |
|
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: 141.67 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKEKTIRHirgnRIAMIFQEp 102
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-----EPTSGEIFIDGEDIREQDPVELRR----KIGYVIQQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mTSLNPLHSIEKQINEVLGIHKGLIGKVAtKRTLELLEMVGIPePEKRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03295 84 -IGLFPHMTVEENIALVPKLLKWPKEKIR-ERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELLAAE 261
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
292-503 |
2.05e-38 |
|
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: 139.97 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSlTQQQVRPLRREMQV 366
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTL----LRCINlleepDSGTIIIDGLKLTD-DKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDpFgSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03262 81 VFQQ-F-NLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
300-525 |
2.16e-38 |
|
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: 140.55 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQvrplrREMQVVFQDPfgS 374
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAglerpDSGTILFGGEDATDVPVQE-----RNVGFVFQHY--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 LSPRMCVSQIVGEGLRIHKMGT---EAEQEQAIIAALKEVGLDPETRhRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSErppEAEIRAKVHELLKLVQLDWLAD-RYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 452 TSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLL 525
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-529 |
2.79e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.61 E-value: 2.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLkvwfpikkgllkkTVDY--VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKql 349
Cdd:COG1121 4 MPAIELENL-------------TVSYggRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGK-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 dSLTQQQVR----PLRREMQVVFqdPfgslsprMCVSQIVGEGlRIHKMG----TEAEQEQAIIAALKEVGLDpETRHRY 421
Cdd:COG1121 69 -PPRRARRRigyvPQRAEVDWDF--P-------ITVRDVVLMG-RYGRRGlfrrPSRADREAVDEALERVGLE-DLADRP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 422 PHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQsKYNLTYLFISHDLAVVKALSHQLMVVKQG 501
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
250 260
....*....|....*....|....*...
gi 1834229548 502 qVVEQGDAQSIFaapqhpyTQQLLEAAF 529
Cdd:COG1121 216 -LVAHGPPEEVL-------TPENLSRAY 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
275-512 |
3.60e-38 |
|
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: 140.13 E-value: 3.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKgllkktvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLT 353
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----------QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQVRPLRREMQVVFQDpfGSLSPRMCVSQIVGEGlRIHKMGT---------EAEQEQAIiAALKEVGLDpETRHRYPHE 424
Cdd:TIGR02315 71 GKKLRKLRRRIGMIFQH--YNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERAL-SALERVGLA-DKAYQRADQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 425 FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
....*...
gi 1834229548 505 EQGDAQSI 512
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
305-517 |
4.46e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.15 E-value: 4.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLgLAILRL--IGSKGGIRFEGKQLD---SLTQQQVRPLRREMQVVFQDPfgSLSPRM 379
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSL-LRVLNLleTPDSGQLNIAGHQFDfsqKPSEKAIRLLRQKVGMVFQQY--NLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVGEG-LRIHKMGTEAEQEQAIiAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:COG4161 98 TVMENLIEApCKVLGLSKEQAREKAM-KLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 459 VQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAqSIFAAPQ 517
Cdd:COG4161 176 ITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
300-526 |
7.10e-38 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 143.07 E-value: 7.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRPLRR-EMQVVFQDpFGsLSP 377
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEpTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQ-FA-LFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLdPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKAL-ELLKLVGL-EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 458 TVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLE 526
Cdd:TIGR01186 163 LIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
9.52e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 9.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQ-DNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNL 79
Cdd:COG1116 1 MSAaAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLI-AGLEKPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 lnlkektirHIRGNRIAMIFQEPmtSLNPLHSIEKqiNEVLGI-HKGLIGKVATKRTLELLEMVGIpepEKRLKALPHEL 158
Cdd:COG1116 76 ---------TGPGPDRGVVFQEP--ALLPWLTVLD--NVALGLeLRGVPKAERRERARELLELVGL---AGFEDAYPHQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDV----TVQlkilELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQ----DELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-260 |
9.59e-38 |
|
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: 139.41 E-value: 9.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNLKEK 85
Cdd:COG1120 1 MLEAENLSVGY--GGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-PS----SGEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TirhiRGNRIAMIFQEPMTSLnPLhSIEkqinEVLGI----HKGLIGKVATK---RTLELLEMVGIPEpeKRLKALpHEL 158
Cdd:COG1120 72 E----LARRIAYVPQEPPAPF-GL-TVR----ELVALgrypHLGLFGRPSAEdreAVEEALERTGLEH--LADRPV-DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
250 260
....*....|....*....|..
gi 1834229548 239 QASCEQLFrapqhpyTRELLAA 260
Cdd:COG1120 219 QGPPEEVL-------TPELLEE 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-236 |
1.29e-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: 137.66 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLlNLKEKT 86
Cdd:cd03262 1 IEIKNLHKSF--GD--FHVLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRCINL-LEEPDSGTIIIDGLKL-TDDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQ-----EPMTSLNPLhsIEKQInEVLGIHKgligKVATKRTLELLEMVGIPEpekRLKALPHELSGG 161
Cdd:cd03262 71 INELR-QKVGMVFQqfnlfPHLTVLENI--TLAPI-KVKGMSK----AEAEERALELLEKVGLAD---KADAYPAQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALD---------VTVQLkilellkelqARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDpelvgevldVMKDL----------AEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
....
gi 1834229548 233 RGCI 236
Cdd:cd03262 210 DGRI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
287-536 |
1.42e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.78 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 287 IKKGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGKQL-DSLTQQqvrpl 360
Cdd:PRK11432 12 ITKRFGSNTV-----IDNLNLTIKQGTMVTLLGPSGCGKTT----VLRLVAglekpTEGQIFIDGEDVtHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 361 rREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGTEaEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALV 440
Cdd:PRK11432 78 -RDICMVFQSY--ALFPHMSLGENVGYGLKMLGVPKE-ERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 441 LKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPY 520
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
250
....*....|....*.
gi 1834229548 521 TQQLLEAAFLVPATAQ 536
Cdd:PRK11432 233 MASFMGDANIFPATLS 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
304-526 |
2.71e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.96 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLD---SLTQQQ--VRPLRREMQVVFQDpFg 373
Cdd:PRK11264 21 GIDLEVKPGEVVAIIGPSGSGKTTL----LRCINlleqpEAGTIRVGDITIDtarSLSQQKglIRQLRQHVGFVFQN-F- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPEtRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 454 ALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLE 526
Cdd:PRK11264 174 ALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
299-502 |
4.33e-37 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 134.82 E-value: 4.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---GS 374
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLES---LRKNIAYVPQDPFlfsGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 LsprmcvsqivgeglrihkmgteaeqeqaiiaalKEVGLdpetrhryphefSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:cd03228 92 I---------------------------------RENIL------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1834229548 455 LDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKaLSHQLMVVKQGQ 502
Cdd:cd03228 127 LDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-231 |
4.42e-37 |
|
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: 136.45 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLlnlkekt 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIIA-GLERPTSGEVLVDGEPV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 irHIRGNRIAMIFQEPmtSLNPLHSIEKqiNEVLGI-HKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQR 165
Cdd:cd03293 69 --TGPGPDRGYVFQQD--ALLPWLTVLD--NVALGLeLQGVPKAEARERAEELLELVGL---SGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVM 231
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-234 |
4.46e-37 |
|
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: 136.06 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSGQNLlnl 82
Cdd:cd03225 1 ELKN--LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKS----TLLRLLngllgPT------SGEVLVDGKDL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 KEKTIRHIRGnRIAMIFQEPMTSL-NPlhSIEKQINEVLGiHKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGG 161
Cdd:cd03225 66 TKLSLKELRR-KVGLVFQNPDDQFfGP--TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRS---PFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
301-525 |
6.41e-37 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 136.85 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLdsltqQQVRPLRREMQVVFQDPfgSL 375
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTL----LRIIAgleqpDSGRIRLNGQDA-----TRVHARDRKIGFVFQHY--AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:TIGR00968 84 FKHLTVRDNIAFGLEIRKH-PKAKIKARVEELLELVQLE-GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLL 525
Cdd:TIGR00968 162 DAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-186 |
8.32e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.54 E-value: 8.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLnlkeKTIRHIRGNRIAMIFQEPmtS 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLT----DDERKSLRKEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LNPLHSIEKQINEVLGIhKGLIGKVATKRTLELLEMVGIPEPEKR-LKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 1834229548 185 TT 186
Cdd:pfam00005 149 TA 150
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
297-525 |
9.33e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 138.30 E-value: 9.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDp 371
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTT----LRMINrliepTSGRILIDGE---DIRDLDPVELRRRIGYVIQQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 fGSLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDPET-RHRYPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:COG1125 85 -IGLFPHMTVAENIATVPRLLGW-DKERIRARVDELLELVGLDPEEyRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDL--AVvkALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLL 525
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIdeAL--KLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-253 |
9.49e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.46 E-value: 9.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLpYPLARHPSGTIEYSGQNLLNLK-E 84
Cdd:COG3842 5 ALELENVSKRY--GD--VTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMI-AGFETPDSGRILLDGRDVTGLPpE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KtirhiRGnrIAMIFQEP-----MTSL-N---PLHsiekqinevlgiHKGLIGKVATKRTLELLEMVGIPEPEKRLkalP 155
Cdd:COG3842 76 K-----RN--VGMVFQDYalfphLTVAeNvafGLR------------MRGVPKAEIRARVAELLELVGLEGLADRY---P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLN--LVkrIAHRVCVMQR 233
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA--LADRIAVMND 211
|
250 260
....*....|....*....|
gi 1834229548 234 GCIVEQASCEQLFRAPQHPY 253
Cdd:COG3842 212 GRIEQVGTPEEIYERPATRF 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
305-507 |
1.79e-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: 134.73 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPqGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSlTQQQVR--PLRREMQVVFQDpfGSLSP 377
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTL----LRCIAglekpDGGTIVLNGTVLFD-SRKKINlpPQQRKIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGLRIHKMGTEAEQEQAIIAALkevGLDPETRhRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVDELLDLL---GLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1834229548 458 TVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
300-507 |
2.15e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.61 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---GSl 375
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRILIDGVDIRDLTLES---LRRQIGVVPQDTFlfsGT- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 sprmcvsqiVGEGLRIHKMG-TEAEqeqaIIAALKEVGLDPETRhRYPH-----------EFSGGQRQRIAIARALVLKP 443
Cdd:COG1132 430 ---------IRENIRYGRPDaTDEE----VEEAAKAAQAHEFIE-ALPDgydtvvgergvNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 444 ALILLDEPTSALD----RTVQRQVVELLRslqskyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:COG1132 496 PILILDEATSALDteteALIQEALERLMK------GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
272-517 |
2.84e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 135.55 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 272 GPPMLTVEDLKVWFpikKGLlkktvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEG 346
Cdd:COG0411 1 SDPLLEVRGLTKRF---GGL--------VAVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLITgfyrpTSGRILFDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 347 KQLDSLTQQQV--RPLRRemqvVFQDP--FGSLSPRMCV---------SQIVGEGLRIHKMG-TEAEQEQAIIAALKEVG 412
Cdd:COG0411 66 RDITGLPPHRIarLGIAR----TFQNPrlFPELTVLENVlvaaharlgRGLLAALLRLPRARrEEREARERAEELLERVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 413 LDPEtRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALS 492
Cdd:COG0411 142 LADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
250 260
....*....|....*....|....*
gi 1834229548 493 HQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:COG0411 221 DRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-258 |
3.23e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.97 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLlnlkeKT 86
Cdd:COG1118 3 IEVRNISKRF--GSF--TLLDDVSLEIASGELVALLGPSGSGKT----TLLRII-AGLETPDSGRIVLNGRDL-----FT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRIAMIFQEP-----MTslnplhsiekqineVL-----GIHKGLIGKVATK-RTLELLEMVGIPEPEKRLkalP 155
Cdd:COG1118 69 NLPPRERRVGFVFQHYalfphMT--------------VAeniafGLRVRPPSKAEIRaRVEELLELVQLEGLADRY---P 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGC 235
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
250 260
....*....|....*....|...
gi 1834229548 236 IVEQASCEQLFRAPQHPYTRELL 258
Cdd:COG1118 212 IEQVGTPDEVYDRPATPFVARFL 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
305-517 |
4.09e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 134.76 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLgLAILRL--IGSKGGIRFEGKQLD---SLTQQQVRPLRREMQVVFQDPfgSLSPRM 379
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSL-LRVLNLleMPRSGTLNIAGNHFDfskTPSDKAIRELRRNVGMVFQQY--NLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVGEG-LRIHKMGTEAEQEQAIiAALKEVGLDPETrHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:PRK11124 98 TVQQNLIEApCRVLGLSKDQALARAE-KLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 459 VQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSiFAAPQ 517
Cdd:PRK11124 176 ITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-260 |
4.95e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 135.05 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFVVGERCQrvveGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLArhPS-GTIEYSGQ-- 77
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCR----DVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLA--PDaGEVHYRMRdg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 78 ---NLLNLKEKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVL-GI---HKGLIGKVATkrtlELLEMVGIPEpeKR 150
Cdd:PRK11701 71 qlrDLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLmAVgarHYGDIRATAG----DWLERVEIDA--AR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 151 LKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCV 230
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|
gi 1834229548 231 MQRGCIVEQASCEQLFRAPQHPYTRELLAA 260
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
295-501 |
7.75e-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: 133.04 E-value: 7.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 295 TVDY--VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKqldSLTQQQVR----PLRREMQVV 367
Cdd:cd03235 6 TVSYggHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGK---PLEKERKRigyvPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 368 FqdpfgslspRMCVSQIVGEGLRIHK---MGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPA 444
Cdd:cd03235 83 F---------PISVRDVVLMGLYGHKglfRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 445 LILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQG 501
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-240 |
8.00e-36 |
|
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: 133.33 E-value: 8.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 3 QDNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNL 82
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS----TLLGLLA-GLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 KEKTIRHIRGNRIAMIFQE----P-MTSL-N---PLhsiekqinEVLGihkgliGKVATKRTLELLEMVGIpepEKRLKA 153
Cdd:COG4181 80 DEDARARLRARHVGFVFQSfqllPtLTALeNvmlPL--------ELAG------RRDARARARALLERVGL---GHRLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQR 233
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRA 221
|
....*..
gi 1834229548 234 GCIVEQA 240
Cdd:COG4181 222 GRLVEDT 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
303-526 |
8.09e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 133.68 E-value: 8.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSlTQQQVRPLRREMQVVFQDpFgSLSP 377
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTL----LRCINkleeiTSGDLIVDGLKVND-PKVDERLIRQEAGMVFQQ-F-YLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEG-LRIHKMGTEAEQEQAIiAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK09493 91 HLTALENVMFGpLRVRGASKEEAEKQAR-ELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 457 RTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLE 526
Cdd:PRK09493 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQ 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
9.37e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 9.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLl 80
Cdd:COG1121 1 MMMMPAIELENLTVSY--GGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-PT----SGTVRLFGKPP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 nlkektirHIRGNRIAMIFQE-------PMTSLnplhsiekqinEV--LGI--HKGL---IGKVATKRTLELLEMVGIPE 146
Cdd:COG1121 71 --------RRARRRIGYVPQRaevdwdfPITVR-----------DVvlMGRygRRGLfrrPSRADREAVDEALERVGLED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 147 PEKRlkalP-HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIA 225
Cdd:COG1121 132 LADR----PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYF 206
|
250
....*....|.
gi 1834229548 226 HRVCVMQRGCI 236
Cdd:COG1121 207 DRVLLLNRGLV 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-529 |
1.29e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.62 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFpikkGllKKtvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLR-------LIGS---KGGI 342
Cdd:COG1117 9 EPKIEVRNLNVYY----G--DK-----QALKDINLDIPENKVTALIGPSGCGKSTL----LRclnrmndLIPGarvEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 343 RFEGKQLDSLTQQQVRpLRREMQVVFQ--DPFgslsPrMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHR 420
Cdd:COG1117 74 LLDGEDIYDPDVDVVE-LRRRVGMVFQkpNPF----P-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 421 ---YPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYnlTYLFISHDLAVVKALSHQLMV 497
Cdd:COG1117 148 lkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAF 225
|
250 260 270
....*....|....*....|....*....|..
gi 1834229548 498 VKQGQVVEQGDAQSIFAAPQHPYTQQLLEAAF 529
Cdd:COG1117 226 FYLGELVEFGPTEQIFTNPKDKRTEDYITGRF 257
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-527 |
1.35e-35 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 135.70 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-------LRLIGSKggIRFEG 346
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDG-------WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnWRVTADR--MRFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 347 KQLDSLTQQQVRPL-RREMQVVFQDPFGSLSP-----RMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGL-DP-ETR 418
Cdd:PRK15093 73 IDLLRLSPRERRKLvGHNVSMIFQEPQSCLDPservgRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIkDHkDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 419 HRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260
....*....|....*....|....*....
gi 1834229548 499 KQGQVVEQGDAQSIFAAPQHPYTQQLLEA 527
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRA 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-234 |
1.44e-35 |
|
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: 131.16 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLlNLKEKT 86
Cdd:cd03229 1 LELKNVSKRY--GQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDL-TDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQEPmtSLNPlhsiekqinevlgihkgligkvatkrTLELLEMVGIPepekrlkalpheLSGGQRQRV 166
Cdd:cd03229 71 LPPLR-RRIGMVFQDF--ALFP--------------------------HLTVLENIALG------------LSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
302-507 |
1.58e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.02 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQvrpLRREMQVVFQdpfgslsprmc 380
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeILLDGKDLASLSPKE---LARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 vsqivgeglrihkmgteaeqeqaiiaALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQ 460
Cdd:cd03214 81 --------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834229548 461 RQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
305-534 |
1.74e-35 |
|
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: 136.00 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQL-DSLTQQQVRPLRREMQVVFQDPfgSLSPR 378
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTL----LRAIAglerpDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQEA--RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHKMGTEAEQEQAIIAALkevGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 459 VQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAAFLVPAT 534
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEAT 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
299-517 |
2.58e-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: 132.18 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRplRREMQVVFQDP-- 371
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISgflrpTSGSVLFDGEDITGLPPHEIA--RLGIGRTFQIPrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 FGSLSPR--MCVSQIVGEGLRIH---KMGTEAEQEQAIIAALKEVGLDPEtRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03219 87 FPELTVLenVMVAAQARTGSGLLlarARREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
294-507 |
2.91e-35 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 131.22 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 294 KTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDsltqqQVRPLRREMQVVF 368
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGGRDVT-----DLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILL 448
Cdd:cd03301 79 QNY--ALYPHMTVYDNIAFGLKLRKVP-KDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 449 DEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
302-527 |
3.08e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 132.52 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIgsKGGIRFEGKQLdSLTQQQVRP--LR-REMQVVFQDPFGSLSPr 378
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL--PAGVRQTAGRV-LLDGKPVAPcaLRgRKIATIMQNPRSAFNP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 mcvsqivgeglrIHKMGTEAEQ----------EQAIIAALKEVGLDPETR--HRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:PRK10418 95 ------------LHTMHTHAREtclalgkpadDATLTAALEAVGLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLE 526
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
.
gi 1834229548 527 A 527
Cdd:PRK10418 243 A 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
255-526 |
4.09e-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: 138.75 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 255 RELLAAEPSGT-PATNVVGP--PMLTVEDLkvwfpikkgllkkTVDY----VKAVDGINFSLPQGQTLGIVGESGSGKST 327
Cdd:COG4987 310 NELLDAPPAVTePAEPAPAPggPSLELEDV-------------SFRYpgagRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 328 LGLAILRLIGSKGG-IRFEGKQLDSLTQQQvrpLRREMQVVFQDP--FgslsprmcvSQIVGEGLRIhkmGTEAEQEQAI 404
Cdd:COG4987 377 LLALLLRFLDPQSGsITLGGVDLRDLDEDD---LRRRIAVVPQRPhlF---------DTTLRENLRL---ARPDATDEEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 405 IAALKEVGLDPETRhRYPH-----------EFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRS-LQS 472
Cdd:COG4987 442 WAALERVGLGDWLA-ALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAG 520
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 473 KynlTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAapQHPYTQQLLE 526
Cdd:COG4987 521 R---TVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-250 |
4.94e-35 |
|
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: 132.58 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSGQNLLNLKEKTIRHIRgNRIAM 97
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKS----TLIQHLngllkPT------SGTVTIDGRDITAKKKKKLKDLR-KKVGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 98 IFQEPmtslnplhsiEKQINEVLgIHK---------GLIGKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQRVMI 168
Cdd:TIGR04521 87 VFQFP----------EHQLFEET-VYKdiafgpknlGLSEEEAEERVKEALELVGLDE--EYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 169 AMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRA 248
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
..
gi 1834229548 249 PQ 250
Cdd:TIGR04521 234 VD 235
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
317-520 |
1.44e-34 |
|
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: 132.62 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 317 IVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLdsltqQQVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRI 391
Cdd:TIGR01187 1 LLGPSGCGKTTL----LRLLAgfeqpDSGSIMLDGEDV-----TNVPPHLRHINMVFQSY--ALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 392 HKMGTEaEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQ 471
Cdd:TIGR01187 70 RKVPRA-EIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834229548 472 SKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPY 520
Cdd:TIGR01187 148 EQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
302-535 |
1.55e-34 |
|
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: 133.58 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI---GSKGGIRFEGKQLDSLTqqqvrPLRREMQVVFQDPfgSLSPR 378
Cdd:TIGR03258 21 LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVkaaGLTGRIAIADRDLTHAP-----PHKRGLALLFQNY--ALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:TIGR03258 94 LKVEDNVAFGLRAQKM-PKADIAERVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDAN 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 459 VQRQVVELLRSLQSKY-NLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAAFLVPATA 535
Cdd:TIGR03258 172 IRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPAIA 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-260 |
1.59e-34 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 131.07 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGE---RCQRV--VEGVSFDIKRGETLALVGESGSGKSVtahsilrllpypLARHPSGTIEYSGQN 78
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfRRQTVeaVKPLSFTLREGQTLAIIGENGSGKST------------LAKMLAGMIEPTSGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LLnLKEKTIR----HIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGI-PEpekRLKA 153
Cdd:PRK15112 70 LL-IDDHPLHfgdySYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPD---HASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQR 233
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
250 260
....*....|....*....|....*..
gi 1834229548 234 GCIVEQASCEQLFRAPQHPYTRELLAA 260
Cdd:PRK15112 226 GEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-238 |
2.05e-34 |
|
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: 129.39 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHsILRLLPYPlarhPSGTIEYSGQNLLNLKEK 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLH-LLGGLDNP----TSGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQ--EPMTSLNPLHSIEKQInevlgihkgLIGKV----ATKRTLELLEMVGIpepEKRLKALPHELS 159
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhHLLPDFTALENVAMPL---------LIGKKsvkeAKERAYEMLEKVGL---EHRINHRPSELS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAhRVCVMQRGCIVE 238
Cdd:TIGR02211 144 GGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLD-RVLEMKDGQLFN 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
292-516 |
2.21e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.53 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGKQLDsltqqQVRPLRREMQV 366
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAgfetpDSGRIMLDGQDIT-----HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:PRK09452 91 VFQSY--ALFPHMTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-239 |
3.24e-34 |
|
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: 127.17 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNLKEKTI 87
Cdd:cd03214 1 EVENLSVGY--GGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK-PS----SGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 88 RhirgNRIAMIFQEpMTSLNPLHSIEKQINEvlgihkgligkvatkrtlellemvgipepekrlkalpheLSGGQRQRVM 167
Cdd:cd03214 72 A----RKIAYVPQA-LELLGLAHLADRPFNE---------------------------------------LSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 168 IAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ 239
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-245 |
3.34e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 129.22 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERcqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLKEK 85
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE------PtSGSVLIDGTDINKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGnRIAMIFQ-----EPMTSL-NPLHSIEKQINEVLGIhKGLIGKVATKRTLELLEMVGIPE-PEKRLKalphEL 158
Cdd:cd03256 72 ALRQLRR-QIGMIFQqfnliERLSVLeNVLSGRLGRRSTWRSL-FGLFPKEEKQRALAALERVGLLDkAYQRAD----QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
....*..
gi 1834229548 239 QASCEQL 245
Cdd:cd03256 226 DGPPAEL 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
304-525 |
6.31e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 129.15 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLT----------QQQVRPLRREMQVVF 368
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTF----LRCINlletpDSGEIRVGGEEIRLKPdrdgelvpadRRQLQRIRTRLGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDpFgSLSPRMCVSQIVGEG-LRIHKMGTEAEQEQAIiAALKEVGLdPETRHRYPHEFSGGQRQRIAIARALVLKPALIL 447
Cdd:COG4598 102 QS-F-NLWSHMTVLENVIEApVHVLGRPKAEAIERAE-ALLAKVGL-ADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 448 LDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLL 525
Cdd:COG4598 178 FDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
301-527 |
9.36e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 9.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLdslTQQQVRPLRREMQVVFQDPfgslsprm 379
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVL---SEETVWDVRRQVGMVFQNP-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cVSQIVGE--------GLRIHKMGTEAEQEQaIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:PRK13635 91 -DNQFVGAtvqddvafGLENIGVPREEMVER-VDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 452 TSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAAPQH--------PYTQQ 523
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKSGHMlqeigldvPFSVK 246
|
....
gi 1834229548 524 LLEA 527
Cdd:PRK13635 247 LKEL 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-528 |
1.01e-33 |
|
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: 133.80 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyplARHPSGTieYSGQNLLNLKEKTIRHIRGNR---IAMIFQ 100
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKS----TLMKILS---GVYPHGT--WDGEIYWSGSPLKASNIRDTEragIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 EPMtsLNPLHSIEKQI---NEVlgIHKGLIGKVA--TKRTLELLEMVGIPE-PEKRLKAlphELSGGQRQRVMIAMALAN 174
Cdd:TIGR02633 86 ELT--LVPELSVAENIflgNEI--TLPGGRMAYNamYLRAKNLLRELQLDAdNVTRPVG---DYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 175 EPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIV--EQASCEQLFRAPQHP 252
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVatKDMSTMSEDDIITMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 253 YTRELLAAEPSgTPATnvVGPPMLTVEDLKVWFPIKKgllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaI 332
Cdd:TIGR02633 238 VGREITSLYPH-EPHE--IGDVILEARNLTCWDVINP--------HRKRVDDVSFSLRRGEILGVAGLVGAGRTEL---V 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 333 LRLIGS-----KGGIRFEGKQLDSLTQQQVrpLRREMQVVFQD-PFGSLSPRMCVSQ-IVGEGL-RIHKMGT--EAEQEQ 402
Cdd:TIGR02633 304 QALFGAypgkfEGNVFINGKPVDIRNPAQA--IRAGIAMVPEDrKRHGIVPILGVGKnITLSVLkSFCFKMRidAAAELQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 403 AIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFIS 482
Cdd:TIGR02633 382 IIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVS 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1834229548 483 HDLAVVKALSHQLMVVKQGQVveQGDAQSifaapqHPYTQ-QLLEAA 528
Cdd:TIGR02633 461 SELAEVLGLSDRVLVIGEGKL--KGDFVN------HALTQeQVLAAA 499
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-528 |
1.57e-33 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 133.52 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSVtahsilrLLPYPLARHPSGTieYSGQNLLNLKEKTIRHIRGNR---IAMIFQ 100
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKST-------LMKVLSGVYPHGT--YEGEIIFEGEELQASNIRDTEragIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 EPMtsLNPLHSIEKQI---NEVLgiHKGLIGKVA-TKRTLELLEMVGIP-EPEKRLKalphELSGGQRQRVMIAMALANE 175
Cdd:PRK13549 90 ELA--LVKELSVLENIflgNEIT--PGGIMDYDAmYLRAQKLLAQLKLDiNPATPVG----NLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 176 PELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLfrapqhpyT- 254
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM--------Te 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 255 ---------RELLAAEPSgtpATNVVGPPMLTVEDLKVWFPIKKGllkktvdyVKAVDGINFSLPQGQTLGIVGESGSGK 325
Cdd:PRK13549 233 ddiitmmvgRELTALYPR---EPHTIGEVILEVRNLTAWDPVNPH--------IKRVDDVSFSLRRGEILGIAGLVGAGR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 326 STLGLAILrliG-----SKGGIRFEGKQLDSLTQQQVrpLRREMQVVFQD--PFGsLSPRMCVSQ-IVGEGL-RIHKMGT 396
Cdd:PRK13549 302 TELVQCLF---GaypgrWEGEIFIDGKPVKIRNPQQA--IAQGIAMVPEDrkRDG-IVPVMGVGKnITLAALdRFTGGSR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 397 --EAEQEQAIIAALKEVgldpetRHRYPHEF------SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLR 468
Cdd:PRK13549 376 idDAAELKTILESIQRL------KVKTASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 469 SLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVveQGDaqsifaAPQHPYTQ-QLLEAA 528
Cdd:PRK13549 450 QL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL--KGD------LINHNLTQeQVMEAA 501
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
274-511 |
2.81e-33 |
|
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: 126.39 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPIKKGLLKktvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQ 348
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELT-------ILKGISLEVEAGESVAIVGASGSGKSTL----LGLLAgldrpTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDSLTQQQVRPLRRE-MQVVFQDpFgSLSPRMCVSQIVG---EgLRIHKmgtEAEQEQAiiAALKEVGLDPETRHrYPHE 424
Cdd:COG4181 76 LFALDEDARARLRARhVGFVFQS-F-QLLPTLTALENVMlplE-LAGRR---DARARAR--ALLERVGLGHRLDH-YPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 425 FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVkALSHQLMVVKQGQVV 504
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLV 225
|
....*..
gi 1834229548 505 EQGDAQS 511
Cdd:COG4181 226 EDTAATA 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-236 |
3.26e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKT 86
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLSAMPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHirgnRIAMIFQEPmtslnPL--HSIEKQINEVLGIHKGligKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQ 164
Cdd:COG4619 72 WRR----QVAYVPQEP-----ALwgGTVRDNLPFPFQLRER---KFDRERALELLERLGLPP--DILDKPVERLSGGERQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCI 236
Cdd:COG4619 138 RLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
274-529 |
5.96e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 126.43 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPIKKgllkktvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL------IGSKGGIRFEGK 347
Cdd:PRK14239 4 PILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 QLDSLTQQQVRpLRREMQVVFQDPfgslSP-RMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYpHE-- 424
Cdd:PRK14239 73 NIYSPRTDTVD-LRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-HDsa 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 425 --FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYnlTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:PRK14239 147 lgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGD 224
|
250 260
....*....|....*....|....*..
gi 1834229548 503 VVEQGDAQSIFAAPQHPYTQQLLEAAF 529
Cdd:PRK14239 225 LIEYNDTKQMFMNPKHKETEDYISGKF 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-258 |
9.34e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 125.63 E-value: 9.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlRLLPYPLA-RHPSGTIEYSGQNLLNLK 83
Cdd:PRK11264 2 SAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAgTIRVGDITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRgNRIAMIFQEpmTSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKrlkALPHELSGGQR 163
Cdd:PRK11264 77 KGLIRQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKET---SYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVT-VQLKILELLKELQARLGMalLLISHDLNLVKRIAHRVCVMQRGCIVEQASC 242
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPElVGEVLNTIRQLAQEKRTM--VIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
250
....*....|....*.
gi 1834229548 243 EQLFRAPQHPYTRELL 258
Cdd:PRK11264 229 KALFADPQQPRTRQFL 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
292-503 |
9.55e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 122.89 E-value: 9.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSltqqQVRPLRREMQV 366
Cdd:cd03230 6 LSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIILgllkpDSGEIKVLGKDIKK----EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVgeglrihkmgteaeqeqaiiaalkevgldpetrhryphEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03230 78 LPEEP--SLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
292-502 |
9.69e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 122.74 E-value: 9.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKqldSLTQQQVRPLRREMQVVFQd 370
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGeILIDGK---DIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 371 pfgslsprmcvsqivgeglrihkmgteaeqeqaiiaalkevgldpetrhrypheFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
274-529 |
1.00e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.65 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVwfpiKKGllKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGKQ 348
Cdd:PRK13548 1 AMLEARNLSV----RLG--GRTL-----LDDVSLTLRPGEVVAILGPNGAGKSTL----LRALsgelsPDSGEVRLNGRP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDSLTQQQvRPLRREM-----QVVFqdPFGslsprmcVSQIVGEGLRIHKmGTEAEQEQAIIAALKEVGLDpETRHRYPH 423
Cdd:PRK13548 66 LADWSPAE-LARRRAVlpqhsSLSF--PFT-------VEEVVAMGRAPHG-LSRAEDDALVAAALAQVDLA-HLAGRDYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 424 EFSGGQRQRIAIARALV------LKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMV 497
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
250 260 270
....*....|....*....|....*....|..
gi 1834229548 498 VKQGQVVEQGdaqsifaAPQHPYTQQLLEAAF 529
Cdd:PRK13548 214 LHQGRLVADG-------TPAEVLTPETLRRVY 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-246 |
1.48e-32 |
|
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: 125.62 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvTahsilrllpypLARH------P-SGTIEYSGQNL 79
Cdd:TIGR04520 1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKS-T-----------LAKLlnglllPtSGKVTVDGLDT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 LNlkEKTIRHIRgNRIAMIFQepmtslNPlhsiEKQI------NEV------LGIHKGLIGKvatkRTLELLEMVGIpep 147
Cdd:TIGR04520 67 LD--EENLWEIR-KKVGMVFQ------NP----DNQFvgatveDDVafglenLGVPREEMRK----RVDEALKLVGM--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 148 EKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLN-LVKriAH 226
Cdd:TIGR04520 127 EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--AD 204
|
250 260
....*....|....*....|
gi 1834229548 227 RVCVMQRGCIVEQASCEQLF 246
Cdd:TIGR04520 205 RVIVMNKGKIVAEGTPREIF 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
305-520 |
1.64e-32 |
|
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: 127.54 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQL-DSLTQQQVRPLRREMQVVFQDpfGSLSPRMCVS 382
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRTLfDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 QIVGEGLRihkmGTEAEQEQAIIAALKEV-GLDPETRhRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQR 461
Cdd:TIGR02142 94 GNLRYGMK----RARPSERRISFERVIELlGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 462 QVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPY 520
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
301-513 |
2.25e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.25 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLG-LAILRLIGSKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDP----FGSL 375
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAkLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRKHIGIVFQNPdnqfVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 sprmcVSQIVGEGLRIHKMGTEAEQEQaIIAALKEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:PRK13648 101 -----VKYDVAFGLENHAVPYDEMHRR-VSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAvvKAL-SHQLMVVKQGQVVEQGDAQSIF 513
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
283-507 |
2.81e-32 |
|
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: 123.49 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 283 VWFPIKKGllkktvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrpLR 361
Cdd:cd03254 8 VNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDISRKS---LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 362 REMQVVFQDPFgsLSPRMCVSQIvgeglrihKMGTEAEQEQAIIAALKEVGLDPETRHR---YPHE-------FSGGQRQ 431
Cdd:cd03254 77 SMIGVVLQDTF--LFSGTIMENI--------RLGRPNATDEEVIEAAKEAGAHDFIMKLpngYDTVlgenggnLSQGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 432 RIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
300-507 |
2.91e-32 |
|
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: 123.88 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLI-----GSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDpfgs 374
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLfrfydVSSGSILIDGQDIREVTLDS---LRRAIGVVPQD---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 lsprmCV--SQIVGEGLRihkMGTEAEQEQAIIAALKEVGLDPETRhRYPHEF-----------SGGQRQRIAIARALVL 441
Cdd:cd03253 84 -----TVlfNDTIGYNIR---YGRPDATDEEVIEAAKAAQIHDKIM-RFPDGYdtivgerglklSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 442 KPALILLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
299-503 |
3.97e-32 |
|
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: 122.90 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDpfGSLSP 377
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGLRIHKMGTEAEQEQaIIAALKEVGLdpETRHR-YPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKR-VPAALELVGL--SHKHRaLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834229548 457 RTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:cd03292 169 PDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
305-495 |
6.97e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 122.62 E-value: 6.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLR-REMQVVFQdpFGSLSPR 378
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTL----LHLLGgldtpTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQ--FHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRAL-EMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1834229548 459 VQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQL 495
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-505 |
7.92e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.64 E-value: 7.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 9 VRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplarhpSGTIE-YSGqnllnlkekTI 87
Cdd:COG0488 1 LENLSKSF--GGR--PLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKIL--------AGELEpDSG---------EV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 88 RHIRGNRIAMIFQEP------------MTSLNPLHSIEKQINEV---LGIHKGLIGKVATK--------------RTLEL 138
Cdd:COG0488 56 SIPKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELeakLAEPDEDLERLAELqeefealggweaeaRAEEI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 139 LEMVGIPEPEkrLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDV-TVqlkilellkelQ------ARLGMAL 211
Cdd:COG0488 136 LSGLGFPEED--LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSI-----------EwleeflKNYPGTV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 212 LLISHD---LNlvkRIAHRVCVMQRGCI-------------------VEQASCEQL-------------FRAPQHPYTR- 255
Cdd:COG0488 203 LVVSHDryfLD---RVATRILELDRGKLtlypgnysayleqraerleQEAAAYAKQqkkiakeeefirrFRAKARKAKQa 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 256 -----------ELLAAEPSGT-----PATNVVGPPMLTVEDLKVWFPikkgllKKTVdyvkaVDGINFSLPQGQTLGIVG 319
Cdd:COG0488 280 qsrikalekleREEPPRRDKTveirfPPPERLGKKVLELEGLSKSYG------DKTL-----LDDLSLRIDRGDRIGLIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 320 ESGSGKSTLglaiLRLIGSK----GGIRFEGKQLD--SLTQQQvrplrremqvvfqdpfGSLSPRMCVSQIVGEGLrihk 393
Cdd:COG0488 349 PNGAGKSTL----LKLLAGElepdSGTVKLGETVKigYFDQHQ----------------EELDPDKTVLDELRDGA---- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 394 mgtEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDrtvqrqvVELLRSLQ-- 471
Cdd:COG0488 405 ---PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-------IETLEALEea 474
|
570 580 590
....*....|....*....|....*....|....*
gi 1834229548 472 -SKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVE 505
Cdd:COG0488 475 lDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-237 |
8.92e-32 |
|
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: 122.79 E-value: 8.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKEK 85
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV-----EPSSGSILLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRgNRIAMIFQEpMTSLNPLHSIEKQINEVLGIHK------GLIGKVATKRTLELLEMVGIPE-PEKRLKalphEL 158
Cdd:TIGR02315 73 KLRKLR-RRIGMIFQH-YNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADkAYQRAD----QL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-260 |
1.09e-31 |
|
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: 122.63 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSVTAHSIL-RLLPyplarhPSGTIEY---SGQ--NLLNLKEKTIRHIRGNRIAMIFQEP 102
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAgRLAP------DHGTATYimrSGAelELYQLSEAERRRLMRTEWGFVHQNP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNPLHSIEKQINEVL----GIHKGLIGKVATKrtleLLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALANEPEL 178
Cdd:TIGR02323 96 RDGLRMRVSAGANIGERLmaigARHYGNIRATAQD----WLEEVEIDP--TRIDDLPRAFSGGMQQRLQIARNLVTRPRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 179 LIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELL 258
Cdd:TIGR02323 170 VFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLV 249
|
..
gi 1834229548 259 AA 260
Cdd:TIGR02323 250 SS 251
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-256 |
1.41e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYPLARHpSGTIEYSG 76
Cdd:COG1117 7 TLEPKIEVRNLNVYY--GDKQ--ALKDINLDIPENKVTALIGPSGCGKS----TLLRCLnrmndLIPGARV-EGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 77 QNLLNLKEKTIRHIRgnRIAMIFQEPmtslNPL-HSIEKqiNEVLG--IHKgligkVATKRTL-----ELLEMVGIPEPE 148
Cdd:COG1117 78 EDIYDPDVDVVELRR--RVGMVFQKP----NPFpKSIYD--NVAYGlrLHG-----IKSKSELdeiveESLRKAALWDEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 149 K-RLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-----------------VTVqlkilellkelqarlgma 210
Cdd:COG1117 145 KdRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakieelilelkkdYTI------------------ 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1834229548 211 lLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRE 256
Cdd:COG1117 207 -VIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-234 |
1.60e-31 |
|
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: 119.80 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLL-PYplarhpSGTIEYSGQNLLNLKEK 85
Cdd:cd03228 1 IEFKN--VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPT------SGEILIDGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhirgNRIAMIFQEPMtslnpLH--SIEKQInevlgihkgligkvatkrtlellemvgipepekrlkalpheLSGGQR 163
Cdd:cd03228 73 SLR----KNIAYVPQDPF-----LFsgTIRENI-----------------------------------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRG 234
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETE--ALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
300-504 |
1.80e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSltqqqvRPLRREMQVVFQDP---FGSL 375
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLNGKPIKA------KERRKSIGYVMQDVdyqLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SprmcvsqiVGEGLRIHKMGTEAEQEQaIIAALKEVGL-DPETRHryPHEFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:cd03226 88 S--------VREELLLGLKELDAGNEQ-AETVLKDLDLyALKERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1834229548 455 LDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
304-529 |
1.94e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.38 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGK----------QLDSLTQQQVRPLRREMQVVF 368
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTF----LRCINflekpSEGSIVVNGQtinlvrdkdgQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDpfGSLSPRMCVSQIVGEGlRIHKMG-TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALIL 447
Cdd:PRK10619 99 QH--FNLWSHMTVLENVMEA-PIQVLGlSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 448 LDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEA 527
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
..
gi 1834229548 528 AF 529
Cdd:PRK10619 255 SL 256
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
300-529 |
2.48e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.82 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQLDSLT-QQQVRPLRREMQVVFQDPFG 373
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlnGL----LQPTSGTVTIGERVITAGKkNKKLKPLRKKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SLsprmcVSQIVGEGLRIHKMG---TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK13634 97 QL-----FEETVEKDICFGPMNfgvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQH--------PYT- 521
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEleaigldlPETv 251
|
250
....*....|
gi 1834229548 522 --QQLLEAAF 529
Cdd:PRK13634 252 kfKRALEEKF 261
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-234 |
4.50e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.95 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNlkekti 87
Cdd:cd03235 1 EVEDLTVSY--GGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-PT----SGSIRVFGKPLEK------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 88 rhiRGNRIAMIFQepmtslnpLHSIEKQ----INEVLGI----HKGLIGKVATK---RTLELLEMVGIPEPEKRLKAlph 156
Cdd:cd03235 66 ---ERKRIGYVPQ--------RRSIDRDfpisVRDVVLMglygHKGLFRRLSKAdkaKVDEALERVGLSELADRQIG--- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
28-234 |
6.88e-31 |
|
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: 119.28 E-value: 6.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKTIRHIRgNRIAMIFQEpmTSLN 107
Cdd:TIGR02673 20 DVSLHIRKGEFLFLTGPSGAGKT----TLLKLL-YGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQD--FRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 108 PLHSIEKQIN---EVLGIHKGLIGKvatkRTLELLEMVGIPEpekRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:TIGR02673 92 PDRTVYENVAlplEVRGKKEREIQR----RVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1834229548 185 TTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:TIGR02673 165 TGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-515 |
1.03e-30 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 119.64 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPFgsl 375
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLAS---LRRQIGLVSQDVF--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 sprmCVSQIVGEGLRIhkmGTEAEQEQAIIAALKEVGLdpetrhrypHEF-------------------SGGQRQRIAIA 436
Cdd:cd03251 87 ----LFNDTVAENIAY---GRPGATREEVEEAARAANA---------HEFimelpegydtvigergvklSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 437 RALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
302-528 |
1.41e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.56 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQL---DSLTQQQVRPL--RREMQVVFQ--DPFgs 374
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRlfgRNIYSPDVDPIevRREVGMVFQypNPF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 lsPRMCVSQIVGEGLRIHKM-GTEAEQEQAIIAALKEVGLDPETRHR---YPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK14267 98 --PHLTIYDNVAIGVKLNGLvKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKYnlTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAA 528
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
28-234 |
1.56e-30 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 118.28 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKTIRHIRgNRIAMIFQEpmTSLN 107
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKS----TLLKLI-YKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 108 PLHSIEKQINEVLGIhKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTA 187
Cdd:cd03292 91 PDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834229548 188 LDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
301-507 |
1.90e-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: 118.36 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDPF---GSLs 376
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGV---DISKIGLHDLRSRISIIPQDPVlfsGTI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 pRmcvsqivgEGLRIHKMGTEAEqeqaIIAALKEVGLD-----PETRHRYPHE-----FSGGQRQRIAIARALVLKPALI 446
Cdd:cd03244 95 -R--------SNLDPFGEYSDEE----LWQALERVGLKefvesLPGGLDTVVEeggenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-236 |
2.35e-30 |
|
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: 116.34 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLL-PYplarhpSGTIEYSGQNLLNLKEK 85
Cdd:cd03230 1 IEVRNLSKRY--GKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPD------SGEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhirgnRIAMIFQEPMtslnplhsiekqinevlgIHKGLIGKvatkrtlELLEmvgipepekrlkalpheLSGGQRQR 165
Cdd:cd03230 71 VKR-----RIGYLPEEPS------------------LYENLTVR-------ENLK-----------------LSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCI 236
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
300-525 |
2.57e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQldsLTQQQV--RPLRREMQVVFQDPF 372
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLiqhlnGL----LKPTSGKIIIDGVD---ITDKKVklSDIRKKVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 GSLSPRMcVSQIVGEGLRihKMG-TEAEQEQAIIAALKEVGLDPET-RHRYPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK13637 94 YQLFEET-IEKDIAFGPI--NLGlSEEEIENRVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIF-----------AAPQHP 519
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFkevetlesiglAVPQVT 250
|
....*.
gi 1834229548 520 YTQQLL 525
Cdd:PRK13637 251 YLVRKL 256
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-506 |
3.20e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 118.81 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFPikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGkq 348
Cdd:COG4525 2 SMLTVRHVSVRYP-------GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTL----LNLIAgflapSSGEITLDG-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 ldsltqQQVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGG 428
Cdd:COG4525 69 ------VPVTGPGADRGVVFQKD--ALLPWLNVLDNVAFGLRLRGVP-KAERRARAEELLALVGLA-DFARRRIWQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 429 QRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDL--AVVKALSHQLMVVKQGQVVEQ 506
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALFLATRLVVMSPGPGRIVER 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
23-250 |
4.89e-30 |
|
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: 117.34 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEktirHIRGnrIAMIFQEp 102
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIA-GFETPTSGEILLDGKDITNLPP----HKRP--VNTVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mTSLNPLHSIEKQINEVLGIhKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03300 81 -YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRK---PSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
302-536 |
5.10e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.68 E-value: 5.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGkqlDSLTQQQVRPLRREMQVVFQDPfgsls 376
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKST----TVRLIDglleaESGQIIIDG---DLLTEENVWDIRHKIGMVFQNP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcVSQIVG-------------EGLRIHKMGTEAEQeqaiiaALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKP 443
Cdd:PRK13650 91 ----DNQFVGatveddvafglenKGIPHEEMKERVNE------ALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 444 ALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAApqhpyTQQ 523
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR-----GND 233
|
250
....*....|...
gi 1834229548 524 LLEAAFLVPATAQ 536
Cdd:PRK13650 234 LLQLGLDIPFTTS 246
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-529 |
5.62e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.91 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPikkgllKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGKQL 349
Cdd:COG4559 1 MLEAENLSVRLG------GRTL-----LDDVSLTLRPGELTAIIGPNGAGKSTL----LKLLtgeltPSSGEVRLNGRPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQQvrpLRREMQVVFQD-----PFGslsprmcVSQIVGEGLRIHkmGTEAEQEQAII-AALKEVGLDPeTRHRYPH 423
Cdd:COG4559 66 AAWSPWE---LARRRAVLPQHsslafPFT-------VEEVVALGRAPH--GSSAAQDRQIVrEALALVGLAH-LAGRSYQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 424 EFSGGQRQRIAIARALV-------LKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLM 496
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRIL 211
|
250 260 270
....*....|....*....|....*....|...
gi 1834229548 497 VVKQGQVVEQGDAQSIFaapqhpyTQQLLEAAF 529
Cdd:COG4559 212 LLHQGRLVAQGTPEEVL-------TDELLERVY 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
299-502 |
5.76e-30 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 117.15 E-value: 5.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRF--EGKQLD--SLTQQQVRPLRR-EMQVVF 368
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTL----LKCIygnylPDSGSILVrhDGGWVDlaQASPREILALRRrTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QdpFGSLSPRMCVSQIVGEGLRihKMGTEAEQEQAIIAA-LKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALIL 447
Cdd:COG4778 100 Q--FLRVIPRVSALDVVAEPLL--ERGVDREEARARARElLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 448 LDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-234 |
6.00e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.22 E-value: 6.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHsILRLLPYPlarhPSGTIEYSGQNLLNLKEK 85
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTP----TSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQ--EPMTSLNPLHSIEKQInevlgihkgLIGKV----ATKRTLELLEMVGIpepEKRLKALPHELS 159
Cdd:PRK11629 80 AKAELRNQKLGFIYQfhHLLPDFTALENVAMPL---------LIGKKkpaeINSRALEMLAAVGL---EHRANHRPSELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIaHRVCVMQRG 234
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
308-507 |
1.28e-29 |
|
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: 115.67 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 308 SLPQGQTLGIVGESGSGKSTLglaiLRLIGSkggirFEGKQLDSLTQQQV-----RPLRREMQVVFQDpfGSLSPRMCVS 382
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTL----LNLIAG-----FETPQSGRVLINGVdvtaaPPADRPVSMLFQE--NNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 QIVGEGlRIHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQ 462
Cdd:cd03298 89 QNVGLG-LSPGLKLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 463 VVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
301-513 |
1.39e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLG---LAILRliGSKGGIRFEGKQLDSLTqqqVRPLRREMQVVFQDPfgslsp 377
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISkilTGLLK--PQSGEIKIDGITISKEN---LKEIRKKIGIIFQNP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 rmcVSQIVGE--------GLRiHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:PRK13632 93 ---DNQFIGAtveddiafGLE-NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDL-AVVKAlsHQLMVVKQGQVVEQGDAQSIF 513
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAILA--DKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
263-523 |
2.39e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 116.73 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 263 SGTPATNVVGPPMLTVEdlkvwfpIKKGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGI 342
Cdd:PRK14271 10 SGAADVDAAAPAMAAVN-------LTLGFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 343 RFEGKQL----DSLTQQQVRPLRREMQVVFQDPfgslSP-RMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPET 417
Cdd:PRK14271 78 RYSGDVLlggrSIFNYRDVLEFRRRVGMLFQRP----NPfPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 418 RHRY---PHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKynLTYLFISHDLAVVKALSHQ 494
Cdd:PRK14271 154 KDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDR 231
|
250 260
....*....|....*....|....*....
gi 1834229548 495 LMVVKQGQVVEQGDAQSIFAAPQHPYTQQ 523
Cdd:PRK14271 232 AALFFDGRLVEEGPTEQLFSSPKHAETAR 260
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-245 |
2.97e-29 |
|
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: 122.25 E-value: 2.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSGQNLLN 81
Cdd:COG2274 474 IELEN--VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS----TLLKLLlglyePT------SGRILIDGIDLRQ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRhirgNRIAMIFQEPM----------TSLNPLHSIEkQINEVLgihkgligkvatkrtlellEMVGIpepEKRL 151
Cdd:COG2274 542 IDPASLR----RQIGVVLQDVFlfsgtireniTLGDPDATDE-EIIEAA-------------------RLAGL---HDFI 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 152 KALPH-----------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNL 220
Cdd:COG2274 595 EALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE--AIILENLRRLLKGRTVIIIAHRLST 672
|
250 260
....*....|....*....|....*
gi 1834229548 221 VkRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:COG2274 673 I-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
300-514 |
3.19e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQ-QQVRPLRREMQVVFQDPFGSLSP 377
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKTKdKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGeGLRIHKMGTEAEQEQAIiAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:PRK13646 101 DTVEREIIF-GPKNFKMNLDEVKNYAH-RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 458 TVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
274-468 |
3.25e-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: 114.50 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFpikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQ 348
Cdd:COG4133 1 MMLEAENLSCRR-----------GERLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILAgllppSAGEVLWNGEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDsltqQQVRPLRREMQVVFQDP--FGSLSPRmcvsqivgEGLRIH-KMGTEAEQEQAIIAALKEVGLDPEtRHRYPHEF 425
Cdd:COG4133 66 IR----DAREDYRRRLAYLGHADglKPELTVR--------ENLRFWaALYGLRADREAIDEALEAVGLAGL-ADLPVRQL 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1834229548 426 SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLR 468
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-247 |
3.46e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.65 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLavEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLln 81
Cdd:PRK13635 1 MKEEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL-----LPEAGTITVGGMVL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 lKEKTIRHIRgNRIAMIFQEPMtslnplhsiekqiNEVLGIhkgligkvatkrTLE-----LLEMVGIPEPE--KRLK-A 153
Cdd:PRK13635 72 -SEETVWDVR-RQVGMVFQNPD-------------NQFVGA------------TVQddvafGLENIGVPREEmvERVDqA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 L------------PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:PRK13635 125 LrqvgmedflnrePHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA 204
|
250 260
....*....|....*....|....*.
gi 1834229548 222 KRiAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:PRK13635 205 AQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
299-514 |
4.19e-29 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 114.94 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLtqqQVRPLRREMQVVFQDP---FGS 374
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeILLDGVDIRDL---NLRWLRSQIGLVSQEPvlfDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 lsprmcvsqiVGEGLRIHKmgTEAEQEQaIIAALKEVGLdpetrhrypHEF-------------------SGGQRQRIAI 435
Cdd:cd03249 93 ----------IAENIRYGK--PDATDEE-VEEAAKKANI---------HDFimslpdgydtlvgergsqlSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 436 ARALVLKPALILLDEPTSALDRTVQRQVVELLRslQSKYNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
287-525 |
4.89e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 118.98 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 287 IKKGLLKKTV----DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRPLR 361
Cdd:PRK10070 25 IEQGLSKEQIlektGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 362 RE-MQVVFQDpfGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALV 440
Cdd:PRK10070 105 RKkIAMVFQS--FALMPHMTVLDNTAFGMELAGINAEERREKAL-DALRQVGLE-NYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 441 LKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPY 520
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
....*
gi 1834229548 521 TQQLL 525
Cdd:PRK10070 261 VRTFF 265
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-523 |
5.17e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.52 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQL---DSLTQQQVR--PLRREMQVVFQDP 371
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEffnQNIYERRVNlnRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 fgSLSPrMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETR---HRYPHEFSGGQRQRIAIARALVLKPALILL 448
Cdd:PRK14258 98 --NLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKhkiHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 449 DEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQ-----GQVVEQGDAQSIFAAPQHPYTQQ 523
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTRE 254
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
301-513 |
5.95e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-LRLIGSKGGIRFEGkqLDSLTQQQVRPLRREMQVVFQDPFGSLsprm 379
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQI---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cVSQIVGEGLRI--HKMGTEAEQ-EQAIIAALKEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK13633 99 -VATIVEEDVAFgpENLGIPPEEiRERVDESLKKVGMYEYRRHA-PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 457 RTVQRQVVELLRSLQSKYNLTYLFISHDL-AVVKAlsHQLMVVKQGQVVEQGDAQSIF 513
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-234 |
7.13e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.95 E-value: 7.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKTI 87
Cdd:cd00267 1 EIENLSFRY--GGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 88 RhirgNRIAMIFQepmtslnplhsiekqinevlgihkgligkvatkrtlellemvgipepekrlkalpheLSGGQRQRVM 167
Cdd:cd00267 72 R----RRIGYVPQ---------------------------------------------------------LSGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 168 IAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-250 |
7.51e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 7.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPypLARHP-SGTIEYSGQNL---LNLKEKTIRHIRGNrIAMI 98
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKS----SLLRVLN--LLETPdSGQLNIAGHQFdfsQKPSEKAIRLLRQK-VGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 99 FQE----P-MTSLNPLhsIEKQINeVLGIHKgligKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALA 173
Cdd:COG4161 88 FQQynlwPhLTVMENL--IEAPCK-VLGLSK----EQAREKAMKLLARLRL---TDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 174 NEPELLIADEPTTALD--VTVQLKILELLKelqARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEqLFRAPQ 250
Cdd:COG4161 158 MEPQVLLFDEPTAALDpeITAQVVEIIREL---SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQ 232
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
303-516 |
9.24e-29 |
|
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: 120.83 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLR-LIG----SKGGIRFEGKQLDSLTQQQVRplrREMQVVFQDpfGSLSP 377
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTL----LRlLLGfetpESGSVFYDGQDLAGLDVQAVR---RQLGVVLQN--GRLMS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGeglrihkmGTEAEQEQAIiAALKEVGLDPETR------HRYPHE----FSGGQRQRIAIARALVLKPALIL 447
Cdd:TIGR03797 541 GSIFENIAG--------GAPLTLDEAW-EAARMAGLAEDIRampmgmHTVISEgggtLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 448 LDEPTSALDRTVQRQVVELLRSLqskyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
297-514 |
1.39e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGL---AILRliGSKGGIRFEGKQLDsLTQQQVRPLRREMQVVFQDPFG 373
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQnlnGILK--PSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SLSpRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:PRK13636 94 QLF-SASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 454 ALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
302-510 |
1.46e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.58 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAIL----RLIGSKGGIRFEGKQLDSLTqqqvrPLRREMQVVFQDPFgsLSP 377
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgtlsPAFSASGEVLLNGRRLTALP-----AEQRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGL--RIHKmgteAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:COG4136 90 HLSVGENLAFALppTIGR----AQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKAlshqlmvvkQGQVVEQGDAQ 510
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQ 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
29-250 |
1.61e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.57 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNL---LNLKEKTIRHIRGNrIAMIFQE---- 101
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMP----RSGTLNIAGNHFdfsKTPSDKAIRELRRN-VGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 P-MTSLNPLhsIEKQINeVLGIHKgligKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK11124 95 PhLTVQQNL--IEAPCR-VLGLSK----DQALARAEKLLERLRLKPYADRF---PLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 181 ADEPTTALD--VTVQLKILELLKelqARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ--ASCeqlFRAPQ 250
Cdd:PRK11124 165 FDEPTAALDpeITAQIVSIIREL---AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQgdASC---FTQPQ 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-523 |
2.63e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.08 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQL---DSLTQQQVRPLRREMQVVF 368
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYldgQDIFKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDPfgSLSPRMCVSQIVGEGLRIHKM-GTEAEQEQAIIAALKEVGLDPETRHRY---PHEFSGGQRQRIAIARALVLKPA 444
Cdd:PRK14247 89 QIP--NPIPNLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 445 LILLDEPTSALDRTVQRQVVELLrsLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQ 523
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-245 |
3.46e-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: 112.08 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLnlkeKTIRHIRgNRIAMIFQEP 102
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK------PtSGRATVAGHDVV----REPREVR-RRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mtslnplhSIEKQIN--EVLGIHK---GLIGKVATKRTLELLEMVGIPEPEKRLKAlphELSGGQRQRVMIAMALANEPE 177
Cdd:cd03265 83 --------SVDDELTgwENLYIHArlyGVPGAERRERIDELLDFVGLLEAADRLVK---TYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 178 LLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-503 |
6.00e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 117.07 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPSGTIEYSGQNLLNLKeK 85
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP-----PDSGTLEIGGNPCARLT-P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGnrIAMIFQEPMtsLNPLHSIEKQIneVLGIHKGligKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQR 165
Cdd:PRK15439 81 AKAHQLG--IYLVPQEPL--LFPNLSVKENI--LFGLPKR---QASMQKMKQLLAALGC---QLDLDSSAGSLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArLGMALLLISHDLNLVKRIAHRVCVMQRGCIV-----EQA 240
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIAlsgktADL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 241 SCEQLFRApQHPYTREL-------LAAEPSGTPATNVVGPPMLTVEDLKvwfpiKKGLLKktvdyvkavdgINFSLPQGQ 313
Cdd:PRK15439 228 STDDIIQA-ITPAAREKslsasqkLWLELPGNRRQQAAGAPVLTVEDLT-----GEGFRN-----------ISLEVRAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 314 TLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSL-TQQQVR------PLRREMQVVFQDpfGSLSPRMCvsqiv 385
Cdd:PRK15439 291 ILGLAGVVGAGRTELAETLYGLRPARGGrIMLNGKEINALsTAQRLArglvylPEDRQSSGLYLD--APLAWNVC----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 386 geGLRIHKMG--TEAEQEQAII----AAL--KEVGLDPETRhryphEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:PRK15439 364 --ALTHNRRGfwIKPARENAVLeryrRALniKFNHAEQAAR-----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1834229548 458 TVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:PRK15439 437 SARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
299-507 |
6.17e-28 |
|
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: 111.14 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEG---KQLDsltqqqVRPLRREMQVVFQDP--- 371
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGtdiRQLD------PADLRRNIGYVPQDVtlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 FGSLSPRMCvsqivgeglrihkMGTEAEQEQAIIAALKEVGLDPETRhRYPHEF-----------SGGQRQRIAIARALV 440
Cdd:cd03245 91 YGTLRDNIT-------------LGAPLADDERILRAAELAGVTDFVN-KHPNGLdlqigergrglSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 441 LKPALILLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQG 507
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-260 |
6.56e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 112.20 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILR---LLPYPlarhPSGTIEYSGQnLLNLK 83
Cdd:COG4598 9 LEVRDLHKSF--GD--LEVLKGVSLTARKGDVISIIGSSGSGKS----TFLRcinLLETP----DSGEIRVGGE-EIRLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 -----------EKTIRHIRGnRIAMIFQE-----PMTSLN-----PLHsiekqineVLGIHKgligKVATKRTLELLEMV 142
Cdd:COG4598 76 pdrdgelvpadRRQLQRIRT-RLGMVFQSfnlwsHMTVLEnvieaPVH--------VLGRPK----AEAIERAEALLAKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 143 GIPEpekRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-------VTVQLKIlellkelqARLGMALLLIS 215
Cdd:COG4598 143 GLAD---KRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelvgevLKVMRDL--------AEEGRTMLVVT 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1834229548 216 HDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELLAA 260
Cdd:COG4598 212 HEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
299-535 |
7.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 7.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS-KGGIRFEGKQLdslTQQQVRPLRREMQVVFQDPFGSLSP 377
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGELL---TAENVWNLRRKIGMVFQNPDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 rMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHryPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:PRK13642 97 -ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTRE--PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 458 TVQRQVVELLRSLQSKYNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAApqhpyTQQLLEAAFLVPATA 535
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFAT-----SEDMVEIGLDVPFSS 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-245 |
7.96e-28 |
|
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: 111.49 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLpYPLARHPSGTIEYSGQNLLNLKEK 85
Cdd:COG4555 1 MIEVENLSKKY--GKV--PALKDVSFTAKDGEITGLLGPNGAGKTTL----LRML-AGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIrgnriAMIFQEpmtslNPLH---SIEKQINEVLGIHkGLIGKVATKRTLELLEMVGIPEPEKRLKalpHELSGGQ 162
Cdd:COG4555 72 ARRQI-----GVLPDE-----RGLYdrlTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRV---GELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASC 242
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
...
gi 1834229548 243 EQL 245
Cdd:COG4555 217 DEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-234 |
8.17e-28 |
|
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: 110.85 E-value: 8.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKrGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEpmTSLNP 108
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKS----TLLRCIA-GLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 LHSIEKQINEVLgihKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:cd03297 89 HLNVRENLAFGL---KRKRNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834229548 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
297-507 |
1.16e-27 |
|
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: 116.74 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTqqqVRPLRREMQVVFQDPfgsl 375
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEpDSGQILLDGHDLADYT---LASLRRQVALVSQDV---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 sprMCVSQIVGEGLRIHKMGT--EAEQEQAIIAA-LKEV------GLDPETRHRyPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:TIGR02203 416 ---VLFNDTIANNIAYGRTEQadRAEIERALAAAyAQDFvdklplGLDTPIGEN-GVLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
292-516 |
2.27e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 113.25 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQqqvrplrREMQV 366
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAglehqTSGHIRFHGTDVSRLHA-------RDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 --VFQDPfgSLSPRMCVSQIVGEGLRI---HKMGTEAEQEQAIIAALKEVGLdPETRHRYPHEFSGGQRQRIAIARALVL 441
Cdd:PRK10851 77 gfVFQHY--ALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 442 KPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
292-522 |
2.37e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLdsltqQQVRPLRREMQV 366
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGVDL-----SHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:PRK11607 96 MFQSY--ALFPHMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 447 LLDEPTSALDRTV----QRQVVELLRslqsKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFaapQHPYTQ 522
Cdd:PRK11607 172 LLDEPMGALDKKLrdrmQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR 244
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
24-228 |
2.60e-27 |
|
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: 109.24 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEpm 103
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKF----DSGQVYLNGQETPPLNSKKASKFRREKLGYLFQN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 TSLNPLHSIEKQINEVLgIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:TIGR03608 85 FALIENETVEENLDLGL-KYKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 184 PTTALDvTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRV 228
Cdd:TIGR03608 161 PTGSLD-PKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
278-536 |
2.68e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 278 VEDLKVWFPikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaILRLIG----SKGGIRFEGKQLDSLT 353
Cdd:PRK13647 7 VEDLHFRYK----------DGTKALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLNGiylpQRGRVKVMGREVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQVRplrREMQVVFQDPFGSLSPrMCVSQIVGEGLRihKMG-TEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQR 432
Cdd:PRK13647 74 EKWVR---SKVGLVFQDPDDQVFS-STVWDDVAFGPV--NMGlDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 433 IAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDaQSI 512
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSL 224
|
250 260
....*....|....*....|....*
gi 1834229548 513 FAAPqhpytqQLLEAAFL-VPATAQ 536
Cdd:PRK13647 225 LTDE------DIVEQAGLrLPLVAQ 243
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
292-506 |
2.98e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 112.63 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVD-YVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDsltqqQVRPLRREMQ 365
Cdd:PRK11650 9 VRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVAgleriTSGEIWIGGRVVN-----ELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 366 VVFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPAL 445
Cdd:PRK11650 80 MVFQNY--ALYPHMSVRENMAYGLKIRGMP-KAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 446 ILLDEPTSALDRTVQRQV-VElLRSLQSKYNLTYLFISHDLavVKA--LSHQLMVVKQGqVVEQ 506
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMrLE-IQRLHRRLKTTSLYVTHDQ--VEAmtLADRVVVMNGG-VAEQ 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
299-516 |
3.07e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQLdslTQQQVRPLRREMQVVFQDPFG 373
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLfrhfnGI----LKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SL-SPrmCVSQIVGEGLRihKMGTEAEQ-EQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:PRK13652 90 QIfSP--TVEQDIAFGPI--NLGLDEETvAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 452 TSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
306-508 |
3.14e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 109.18 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 306 NFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTqqqvrPLRREMQVVFQDpfGSLSPRMC 380
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTL----LNLIAgfiepASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRiHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQ 460
Cdd:TIGR01277 87 VRQNIGLGLH-PGLKLNAEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1834229548 461 RQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGD 508
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
301-512 |
4.47e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 109.06 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQVrpLRREMQVVFQDP--FGSLSp 377
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGRDITGLPPHER--ARAGIGYVPEGRriFPELT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 rmcvsqiVGEGLRihkMGTEAEQEQAIIAALKEV-GLDP---ETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:cd03224 92 -------VEENLL---LGAYARRRAKRKARLERVyELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 454 ALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-237 |
4.55e-27 |
|
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: 109.45 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLKEk 85
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR------PtSGSVLFDGEDITGLPP- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 tirHIRGNR-IAMIFQEP-----MTSLN----PLHSIEKQINEVLGIHKGLigKVATKRTLELLEMVGIPEpekRLKALP 155
Cdd:cd03219 70 ---HEIARLgIGRTFQIPrlfpeLTVLEnvmvAAQARTGSGLLLARARREE--REARERAEELLERVGLAD---LADRPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGC 235
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE-ETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
..
gi 1834229548 236 IV 237
Cdd:cd03219 221 VI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
301-517 |
5.24e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.27 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG--------SKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDP- 371
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKST----ISKLINglllpddnPNSKITVDGI---TLTAKTVWDIREKVGIVFQNPd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 ---FGSlsprmCVSQIVGEGLRihKMGTEAEQEQAIIA-ALKEVGL----DPEtrhryPHEFSGGQRQRIAIARALVLKP 443
Cdd:PRK13640 95 nqfVGA-----TVGDDVAFGLE--NRAVPRPEMIKIVRdVLADVGMldyiDSE-----PANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 444 ALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-245 |
5.66e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 108.68 E-value: 5.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplARhpSGTIEYSGQNLLNLK-EKTIRhiRGnrIAMIFQEPM 103
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PR--SGSIRFDGRDITGLPpHERAR--AG--IGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 tsLNPLHSIEKqiNEVLGIHKGLIGKVatKRTLE-LLEMVgiPEPEKRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03224 86 --IFPELTVEE--NLLLGAYARRRAKR--KARLErVYELF--PRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 183 EPTTALD-VTVQLKILELLKElqARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:cd03224 158 EPSEGLApKIVEEIFEAIREL--RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-245 |
5.80e-27 |
|
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: 114.47 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLL-PYplarhpSGTIEYSGQNLLNLKEK 85
Cdd:COG4988 337 IELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPY------SGSILINGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhirgNRIAMIFQEPM---TSL-------NPLHSiEKQINEVLgihkgligkvatkRTLELLEMVgipepekrlKALP 155
Cdd:COG4988 408 SWR----RQIAWVPQNPYlfaGTIrenlrlgRPDAS-DEELEAAL-------------EAAGLDEFV---------AALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HE-----------LSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRi 224
Cdd:COG4988 461 DGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD--AETEAEILQALRRLAKGRTVILITHRLALLAQ- 537
|
250 260
....*....|....*....|.
gi 1834229548 225 AHRVCVMQRGCIVEQASCEQL 245
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEEL 558
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-259 |
6.12e-27 |
|
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: 114.48 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKT 86
Cdd:COG4987 334 LELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRhirgNRIAMIFQEP----MTSLNPLhsiekqinevlgihkgLIGKV-ATKRTL-ELLEMVGIpepEKRLKALPH---- 156
Cdd:COG4987 407 LR----RRIAVVPQRPhlfdTTLRENL----------------RLARPdATDEELwAALERVGL---GDWLAALPDgldt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 -------ELSGGQRQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQARlgmALLLISHDLNLVKRiAHRV 228
Cdd:COG4987 464 wlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEALAGR---TVLLITHRLAGLER-MDRI 539
|
250 260 270
....*....|....*....|....*....|.
gi 1834229548 229 CVMQRGCIVEQASCEQLfrAPQHPYTRELLA 259
Cdd:COG4987 540 LVLEDGRIVEQGTHEEL--LAQNGRYRQLYQ 568
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-255 |
7.68e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.85 E-value: 7.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEK 85
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLA-GFEQPTAGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TirhirgNRIAMIFQEpmTSLNPLHSIEKQIneVLGIHKGLIGKVA-TKRTLELLEMVGIPEPEKRLkalPHELSGGQRQ 164
Cdd:PRK11607 90 Q------RPINMMFQS--YALFPHMTVEQNI--AFGLKQDKLPKAEiASRVNEMLGLVHMQEFAKRK---PHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQ 244
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
250
....*....|.
gi 1834229548 245 LFrapQHPYTR 255
Cdd:PRK11607 237 IY---EHPTTR 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-247 |
7.99e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 7.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKEKtIRHIRgNRIAMIFQEPMTSLNP 108
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL-----KPTSGKIIIDGVDITDKKVK-LSDIR-KKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 lHSIEKQI-----NevLGIHKGLIgkvaTKRTLELLEMVGIPEPEKRLKAlPHELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:PRK13637 99 -ETIEKDIafgpiN--LGLSEEEI----ENRVKRAMNIVGLDYEDYKDKS-PFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 184 PTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
294-517 |
8.90e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.92 E-value: 8.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 294 KTVDYV---------KAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQLDSLT-QQQVR 358
Cdd:PRK13641 6 ENVDYIyspgtpmekKGLDNISFELEEGSFVALVGHTGSGKSTLmqhfnAL----LKPSSGTITIAGYHITPETgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 359 PLRREMQVVFQDPFGSLSPRMCVSQIvgeglrihKMG------TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQR 432
Cdd:PRK13641 82 KLRKKVSLVFQFPEAQLFENTVLKDV--------EFGpknfgfSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 433 IAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQsKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
....*
gi 1834229548 513 FAAPQ 517
Cdd:PRK13641 233 FSDKE 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-261 |
1.55e-26 |
|
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: 107.81 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLK-EKtirhirgNRIAMIFQEp 102
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK------PdSGKILLNGKDITNLPpEK-------RDISYVPQN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mTSLNPLHSIEKQIneVLGIHKGLIGKVAT-KRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:cd03299 80 -YALFPHMTVYKNI--AYGLKKRKVDKKEIeRKVLEIAEMLGI---DHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELLAAE 261
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFN 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-254 |
2.37e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFVVGErcqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLP-YPLARhPSGTIEYSGQNLLNLK 83
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElYPEAR-VSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHirgnRIAMIFQEPmtslNPLHSIEKQINEVLGIHKGLIGKVATK---RTLELLEMVGIPEPEK-RLKALPHELS 159
Cdd:PRK14247 77 VIELRR----RVQMVFQIP----NPIPNLSIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVKdRLDAPAGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ 239
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLD--PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
250
....*....|....*
gi 1834229548 240 ASCEQLFRAPQHPYT 254
Cdd:PRK14247 227 GPTREVFTNPRHELT 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
305-523 |
2.43e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.83 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQL---DSLTQQQVRPLRREMQVVFQDPfgSLSPRMC 380
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQP--NPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRY---PHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:PRK14246 107 IYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 458 TVQRQVVELLRSLqsKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQ 523
Cdd:PRK14246 187 VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-253 |
2.63e-26 |
|
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: 107.43 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIeysgqnLLNLKEKT 86
Cdd:cd03296 3 IEVRNVSKRF--GDF--VALDDVSLDIPSGELVALLGPSGSGKT----TLLRLIA-GLERPDSGTI------LFGGEDAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRIAMIFQEpmTSLNPLHSIEKQINEVLGIHKGLIGKVAT---KRTLELLEMVGIPEPEKRLkalPHELSGGQR 163
Cdd:cd03296 68 DVPVQERNVGFVFQH--YALFRHMTVFDNVAFGLRVKPRSERPPEAeirAKVHELLKLVQLDWLADRY---PAQLSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCE 243
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
250
....*....|
gi 1834229548 244 QLFRAPQHPY 253
Cdd:cd03296 223 EVYDHPASPF 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-258 |
3.46e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEKtIRHIRgNRIAMIFQE--- 101
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCIN-KLEEITSGDLIVDGLKVNDPKVD-ERLIR-QEAGMVFQQfyl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 -P-MTSLNplhsiekqiNEVLG-IH-KGLIGKVATKRTLELLEMVGIPEpekRLKALPHELSGGQRQRVMIAMALANEPE 177
Cdd:PRK09493 89 fPhLTALE---------NVMFGpLRvRGASKEEAEKQARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 178 LLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTREL 257
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
.
gi 1834229548 258 L 258
Cdd:PRK09493 236 L 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-517 |
3.50e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.86 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGL---AILRliGSKGGIRFEGKQLDs 351
Cdd:PRK13639 1 ILETRDLKYSYP----------DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLhfnGILK--PTSGEVLIKGEPIK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 352 LTQQQVRPLRREMQVVFQDPFGSL-SPRmcVSQIVGEGLRihKMG-TEAEQEQAIIAALKEVGLDPETRhRYPHEFSGGQ 429
Cdd:PRK13639 68 YDKKSLLEVRKTVGIVFQNPDDQLfAPT--VEEDVAFGPL--NLGlSKEEVEKRVKEALKAVGMEGFEN-KPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*...
gi 1834229548 510 QSIFAAPQ 517
Cdd:PRK13639 222 KEVFSDIE 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-239 |
3.55e-26 |
|
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: 106.21 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhpsgtiEYSGQNLLNLKEKTIRHirGNRIAMIFQEpm 103
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-----------PDSGEVLFDGKPLDIAA--RNRIGYLPEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 TSLNPLHSIEKQINeVLGIHKGLIGKVATKRTLELLEMVGIPE-PEKRLKalphELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03269 79 RGLYPKMKVIDQLV-YLAQLKGLKKEEARRRIDEWLERLELSEyANKRVE----ELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 183 EPTTALDVtVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ 239
Cdd:cd03269 154 EPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-505 |
3.59e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNLLNLKEKTIRHirgNRIAMIFQEpM 103
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEP----TKGTITINNINYNKLDHKLAAQ---LGIGIIYQE-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 TSLNPLhsiekQINEVLGIHKGLIGKV----------ATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALA 173
Cdd:PRK09700 90 SVIDEL-----TVLENLYIGRHLTKKVcgvniidwreMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 174 NEPELLIADEPTTALdvTVQLKILELLKELQARL-GMALLLISHDLNLVKRIAHRVCVMQRGC-----IVEQASCEQLFR 247
Cdd:PRK09700 162 LDAKVIIMDEPTSSL--TNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDIVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 248 ApqhPYTRELLAAEPSGTPAT-NVVGPPMLTVEDLkvwfpikkgllkkTVDYVKAVDGINFSLPQGQTLGIVGESGSGKS 326
Cdd:PRK09700 240 L---MVGRELQNRFNAMKENVsNLAHETVFEVRNV-------------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 327 TLGLAILRLIGSKGG-IRFEGKQ------LDSLTQ--QQVRPLRREMQvvFQDPFgSLSPRMCVSQIVGEGLRIHKMGTE 397
Cdd:PRK09700 304 ELMNCLFGVDKRAGGeIRLNGKDisprspLDAVKKgmAYITESRRDNG--FFPNF-SIAQNMAISRSLKDGGYKGAMGLF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 398 AEQEQAIIA--ALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLqSKYN 475
Cdd:PRK09700 381 HEVDEQRTAenQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDG 459
|
490 500 510
....*....|....*....|....*....|
gi 1834229548 476 LTYLFISHDLAVVKALSHQLMVVKQGQVVE 505
Cdd:PRK09700 460 KVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
299-515 |
3.71e-26 |
|
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: 112.49 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDP---FGS 374
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDpQSGRILLDGVDLRQLDPAE---LRARMALVPQDPvlfAAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 lsprmcvsqiVGEGLRIHKMgtEAEQEQAIIAALKEVGLD-----PETRHRYPHE----FSGGQRQRIAIARALVLKPAL 445
Cdd:TIGR02204 430 ----------VMENIRYGRP--DATDEEVEAAARAAHAHEfisalPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:TIGR02204 498 LLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-456 |
4.33e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 111.42 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvTAHSILRllpyplARHPSGTieYSGQNLLNLKEKTIRHIRGNR---IAMIFQEpmTS 105
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKS-TLMKVLS------GVYPHGS--YEGEILFDGEVCRFKDIRDSEalgIVIIHQE--LA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LNPLHSIEKQI---NEVLgiHKGLIGKVAT-KRTLELLEMVGIPE-PEKRLKalphELSGGQRQRVMIAMALANEPELLI 180
Cdd:NF040905 89 LIPYLSIAENIflgNERA--KRGVIDWNETnRRARELLAKVGLDEsPDTLVT----DIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 181 ADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF----RAPQHPYTRE 256
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADEvtedRIIRGMVGRD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 257 LLAAEPSGTPAtnvVGPPMLTVEDLKVWFPIKKGLlkktvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL-RL 335
Cdd:NF040905 242 LEDRYPERTPK---IGEVVFEVKNWTVYHPLHPER--------KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 336 IGSK--GGIRFEGKQLDSLTQQQ--------VRPLRREMQVVFQDP---------FGSLSPRMCVSQI----VGEGLRiH 392
Cdd:NF040905 311 YGRNisGTVFKDGKEVDVSTVSDaidaglayVTEDRKGYGLNLIDDikrnitlanLGKVSRRGVIDENeeikVAEEYR-K 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 393 KMGTEAEQEQAIIAALkevgldpetrhryphefSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:NF040905 390 KMNIKTPSVFQKVGNL-----------------SGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
301-536 |
5.07e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.98 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL-RLIGSKGG-IRFEGKQLDSLTQQQvrpLRREMQVVFQDPfgslspr 378
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTL-INLLqRVFDPQSGrILIDGTDIRTVTRAS---LRRNIAVVFQDA------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHKMG-TEAEQEQAIIAAL-------KEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPDaTDEEMRAAAERAQahdfierKPDGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAAPQHPYtqQLLEAAFL 530
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGRFA--ALLRAQGM 572
|
....*.
gi 1834229548 531 VPATAQ 536
Cdd:PRK13657 573 LQEDER 578
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-507 |
5.20e-26 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 105.91 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKGllkktvdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGkqL 349
Cdd:cd03266 1 MITADALTKRFRDVKK-------TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAgllepDAGFATVDG--F 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DslTQQQVRPLRREMQVVFqDPFGsLSPRMCVSQIVGEGLRIHKMgteaeQEQAIIAALKEVG--LD-PETRHRYPHEFS 426
Cdd:cd03266 68 D--VVKEPAEARRRLGFVS-DSTG-LYDRLTARENLEYFAGLYGL-----KGDELTARLEELAdrLGmEELLDRRVGGFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 427 GGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQ 506
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
.
gi 1834229548 507 G 507
Cdd:cd03266 218 G 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-258 |
6.48e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 30 SFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSGQNLLNLKEktirhirGNR-IAMIFQEpm 103
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIagflpPD------SGRILWNGQDLTALPP-------AERpVSMLFQE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 TSLNPLHSIEKQINevLGIHKGL-IGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:COG3840 80 NNLFPHLTVAQNIG--LGLRPGLkLTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELL 258
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
303-526 |
6.78e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.77 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDpfGSLSP 377
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTL----LRLIGgqiapDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETrHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 458 TVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQhPYTQQLLE 526
Cdd:PRK11831 177 ITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFLD 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
302-501 |
7.19e-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: 105.63 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDsltqqqvRPLRREMqVVFQDPfgSLS 376
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTL----LNLISglaqpTSGGVILEGKQIT-------EPGPDRM-VVFQNY--SLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 PRMCVSQIVGEGL-RIHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:TIGR01184 67 PWLTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQG 501
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-245 |
9.47e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 9.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLP--YPLArhpSGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEP 102
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLrfYDPT---SGRILIDGVDIRDLTLESLR----RQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 M---TSL-------NPLHSiEKQINEVLgihkgligkvatkRTLELLEMVgipepekrlKALPH-----------ELSGG 161
Cdd:COG1132 424 FlfsGTIrenirygRPDAT-DEEVEEAA-------------KAAQAHEFI---------EALPDgydtvvgergvNLSGG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL-----GMALLLISHDLNLVKRiAHRVCVMQRGCI 236
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETE-------ALIQEALerlmkGRTTIVIAHRLSTIRN-ADRILVLDDGRI 552
|
....*....
gi 1834229548 237 VEQASCEQL 245
Cdd:COG1132 553 VEQGTHEEL 561
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-228 |
1.02e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 105.25 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRllpyPLARHPSGTIEYSGQNLL 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS-TLLAILA----GLDDGSSGEVSLVGQPLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKEKTIRHIRGNRIAMIFQEPM--TSLNPLHSIEkqineVLGIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHEL 158
Cdd:PRK10584 76 QMDEEARAKLRAKHVGFVFQSFMliPTLNALENVE-----LPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRV 228
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
297-515 |
1.10e-25 |
|
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: 111.50 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEG---KQLDSLTqqqvrpLRREMQVVFQDP- 371
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQpTEGSVLLDGvdiRQIDPAD------LRRNIGYVPQDPr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 --FGSLSPRMCvsqivgeglrihkMGTEAEQEQAIIAALKEVGLDPETRhRYPHEF-----------SGGQRQRIAIARA 438
Cdd:TIGR03375 550 lfYGTLRDNIA-------------LGAPYADDEEILRAAELAGVTEFVR-RHPDGLdmqigergrslSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 439 LVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKynLTYLFISHDLAVVKaLSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
302-532 |
1.11e-25 |
|
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: 105.55 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG------SKGGIRFEGKQLDSLTqqqVRPLRREMQVVFQDPFGSL 375
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTL----LSLITgdlpptYGNDVRLFGERRGGED---VWELRKRIGLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SPRMCVSQIVGEGL----RIHKMGTEAEQEQAIiAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:COG1119 92 PRDETVLDVVLSGFfdsiGLYREPTDEQRERAR-ELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 452 TSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLA-VVKALSHQLMvVKQGQVVEQGDAQSIFaapqhpyTQQLLEAAFL 530
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLL-LKDGRVVAAGPKEEVL-------TSENLSEAFG 241
|
..
gi 1834229548 531 VP 532
Cdd:COG1119 242 LP 243
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
292-507 |
1.19e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 104.61 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQldslTQQQVRPLRReMQVVFQD 370
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeITFDGKS----YQKNIEALRR-IGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 371 P--FGSLSPRmcvsqivgEGLRIH---KMGTEAEQEQAiiaaLKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPAL 445
Cdd:cd03268 81 PgfYPNLTAR--------ENLRLLarlLGIRKKRIDEV----LDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQsKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
302-507 |
1.28e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 111.37 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGKQLdsltqQQVRP--LRREMQVVFQDPFgslspr 378
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQHGQVLVDGVDL-----AIADPawLRRQMGVVLQENV------ 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 mCVSQIVGEGLRIHKMGTEAEQeqaIIAALKEVGLDP---ETRHRYPHE-------FSGGQRQRIAIARALVLKPALILL 448
Cdd:TIGR01846 542 -LFSRSIRDNIALCNPGAPFEH---VIHAAKLAGAHDfisELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 449 DEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
275-505 |
1.34e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.55 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIKKgllkktvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQL 349
Cdd:PRK11248 1 MLQISHLYADYGGKP-----------ALEDINLTLESGELLVVLGPSGCGKTTL----LNLIAgfvpyQHGSITLDGKPV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQqqvrplrrEMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQ 429
Cdd:PRK11248 66 EGPGA--------ERGVVFQNE--GLLPWRNVQDNVAFGLQLAGVE-KMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDL--AVVKALSHQLMVVKQGQVVE 505
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIeeAVFMATELVLLSPGPGRVVE 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-246 |
1.76e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVvGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLlnlK 83
Cdd:PRK13650 2 SNIIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL-----EAESGQIIIDGDLL---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRgNRIAMIFQEPMtslNPLHSIEKQINEVLGI-HKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQ 162
Cdd:PRK13650 73 EENVWDIR-HKIGMVFQNPD---NQFVGATVEDDVAFGLeNKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKrIAHRVCVMQRGCIVEQASC 242
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
|
....
gi 1834229548 243 EQLF 246
Cdd:PRK13650 225 RELF 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-259 |
1.76e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.44 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLLN 81
Cdd:PRK10619 1 MSENKLNVIDLHKRY--GE--HEVLKGVSLQANAGDVISIIGSSGSGKS----TFLRCINF-LEKPSEGSIVVNGQTINL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKE----------KTIRHIRgNRIAMIFQE--PMTSLNPLHSIEKQINEVLGIHKgligKVATKRTLELLEMVGIPEPEK 149
Cdd:PRK10619 72 VRDkdgqlkvadkNQLRLLR-TRLTMVFQHfnLWSHMTVLENVMEAPIQVLGLSK----QEARERAVKYLAKVGIDERAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 150 rlKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVqLKILELLKELQARLGMALLLISHDLNLVKRIAHRVC 229
Cdd:PRK10619 147 --GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
250 260 270
....*....|....*....|....*....|
gi 1834229548 230 VMQRGCIVEQASCEQLFRAPQHPYTRELLA 259
Cdd:PRK10619 224 FLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
287-514 |
1.88e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.32 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 287 IKKGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL--GLAILrLIGSKGGIRF-------------EGKQLDS 351
Cdd:PRK13651 8 IVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFieHLNAL-LLPDTGTIEWifkdeknkkktkeKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 352 LTQQ--------QVRPLRREMQVVFQDP--------------FGSLSprmcvsqivgeglrihkMGTEAEQEQAIIAA-L 408
Cdd:PRK13651 87 LVIQktrfkkikKIKEIRRRVGVVFQFAeyqlfeqtiekdiiFGPVS-----------------MGVSKEEAKKRAAKyI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 409 KEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVV 488
Cdd:PRK13651 150 ELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNV 228
|
250 260
....*....|....*....|....*.
gi 1834229548 489 KALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-526 |
2.34e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.91 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQdpfgs 374
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdpQQGEILLNGQPIADYSEAA---LRQAISVVSQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 lsprmcvsqivgeglRIH----------KMGTEAEQEQAIIAALKEVGLDPETRHRYP---------HEFSGGQRQRIAI 435
Cdd:PRK11160 422 ---------------RVHlfsatlrdnlLLAAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 436 ARALvLKPA-LILLDEPTSALDRTVQRQVVELLRSL-QSKynlTYLFISHDLavvKALSH--QLMVVKQGQVVEQGDAQS 511
Cdd:PRK11160 487 ARAL-LHDApLLLLDEPTEGLDAETERQILELLAEHaQNK---TVLMITHRL---TGLEQfdRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*
gi 1834229548 512 IFAapQHPYTQQLLE 526
Cdd:PRK11160 560 LLA--QQGRYYQLKQ 572
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-512 |
2.43e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFPikkGllkktvdyVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGK 347
Cdd:COG1129 2 EPLLEMRGISKSFG---G--------VKALDGVSLELRPGEVHALLGENGAGKSTL----MKILSgvyqpDSGEILLDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 348 QLDSLTQQQVRplRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHKMGT--EAEQEQAIIAALKEVGL--DPETRHRyph 423
Cdd:COG1129 67 PVRFRSPRDAQ--AAGIAIIHQEL--NLVPNLSVAENIFLGREPRRGGLidWRAMRRRARELLARLGLdiDPDTPVG--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 424 EFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
....*....
gi 1834229548 504 VEQGDAQSI 512
Cdd:COG1129 219 VGTGPVAEL 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
266-513 |
2.64e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 266 PATNVVGPPMLTVEDLKVWFPikkgllKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKG 340
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFD------EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnGL----IKSKYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 341 GIRFE----------GKQLDSLTQQQVR---PLRREMQVVFQDPFGSLSPRMCVSQIV-GE-GLRIHKmgTEAEQEQAII 405
Cdd:PRK13631 82 TIQVGdiyigdkknnHELITNPYSKKIKnfkELRRRVSMVFQFPEYQLFKDTIEKDIMfGPvALGVKK--SEAKKLAKFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 406 aaLKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQsKYNLTYLFISHDL 485
Cdd:PRK13631 160 --LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTM 236
|
250 260
....*....|....*....|....*...
gi 1834229548 486 AVVKALSHQLMVVKQGQVVEQGDAQSIF 513
Cdd:PRK13631 237 EHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
300-497 |
2.65e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 109.30 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQvrpLRREMQVVFQDPFgslspr 378
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGsIAVNGVPLADADADS---WRDQIAWVPQHPF------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 mCVSQIVGEGLRIHKMG-TEAEQEQAIIAA-----LKEVGLDPETR-HRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:TIGR02857 407 -LFAGTIAENIRLARPDaSDAEIREALERAgldefVAALPQGLDTPiGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834229548 452 TSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKALSHQLMV 497
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
303-503 |
3.04e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 104.76 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGSkggirfegkqLDSLTQQQVR----PL---RREMQVVFQDpfGSL 375
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTL----LRLLAG----------LETPSAGELLagtaPLaeaREDTRLMFQD--ARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SPRMCVSQIVGEGLRIHkMGTEAEQeqaiiaALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQ-WRDAALQ------ALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-258 |
3.23e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.71 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLkektirHIRGNRIAMIFQ--- 100
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIA-GLEHQTSGHIRFHGTDVSRL------HARDRKVGFVFQhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 --EPMTSLNplhSIEKQINeVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPEL 178
Cdd:PRK10851 85 lfRHMTVFD---NIAFGLT-VLPRRERPNAAAIKAKVTQLLEMVQLAHLADRY---PAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 179 LIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELL 258
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
303-507 |
3.33e-25 |
|
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: 109.52 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDP--Fgslsprm 379
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDvTSGRILIDGQDIRDVTQAS---LRAAIGIVPQDTvlF------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cvSQIVGEGLRIHKMG-TEAEQEQAI--------IAALKE-----VGldpetrhryphE----FSGGQRQRIAIARALVL 441
Cdd:COG5265 445 --NDTIAYNIAYGRPDaSEEEVEAAAraaqihdfIESLPDgydtrVG-----------ErglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 442 KPALILLDEPTSALDRTVQRQVVELLRSLqSKyNLTYLFISHDLA-VVKAlsHQLMVVKQGQVVEQG 507
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREV-AR-GRTTLVIAHRLStIVDA--DEILVLEAGRIVERG 574
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
297-507 |
3.56e-25 |
|
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: 103.35 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGSKGGIRFEGKqldSLTQQQVRpLRREMQVVFQDP--F 372
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLtgELRPTSGTAYINGY---SIRTDRKA-ARQSLGYCPQFDalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 GSLSPRmcvsqivgEGLRIHKM--GTEAEQEQAIIAA-LKEVGLDPEtRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:cd03263 88 DELTVR--------EHLRFYARlkGLPKSEIKEEVELlLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
301-515 |
4.69e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 103.72 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDpfGSLSPRM 379
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAW---LRRQVGVVLQE--NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVgeglrihkMGTEAEQEQAIIAALKEVGldpetrhryPHEF-------------------SGGQRQRIAIARALV 440
Cdd:cd03252 92 IRDNIA--------LADPGMSMERVIEAAKLAG---------AHDFiselpegydtivgeqgaglSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 441 LKPALILLDEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
300-510 |
4.92e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.03 E-value: 4.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-----GSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDP--- 371
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTL----LKLIcgierPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 -----FGSLSPRMCVSQIVGEGLRihkmgteaeqeQAIIAALKEVGLDPETRHrYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:PRK10908 92 mdrtvYDNVAIPLIIAGASGDDIR-----------RRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQ 510
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
292-507 |
5.57e-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: 102.66 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTlGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGkqLDSLTQQQvrPLRREMQV 366
Cdd:cd03264 6 LTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTL----MRILAtltppSSGTIRIDG--QDVLKQPQ--KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgSLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03264 77 LPQEF--GVYPNFTVREFLDYIAWLKGI-PSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 447 LLDEPTSALDrTVQRQVV-ELLRSLQSkyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03264 153 IVDEPTAGLD-PEERIRFrNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
275-499 |
7.73e-25 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 102.85 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPI-KKGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILR--LIGS-KGGIRFEGKQLD 350
Cdd:TIGR02324 1 LLEVEDLSKTFTLhQQGGVRLPV-----LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYAnyLPDSgRILVRHEGAWVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 351 --SLTQQQVRPLRR-EMQVVFQdpFGSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDPETRHRYPHEFSG 427
Cdd:TIGR02324 76 laQASPREVLEVRRkTIGYVSQ--FLRVIPRVSALEVVAEPLLERGVPREAARARAR-ELLARLNIPERLWHLPPATFSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 428 GQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVK 499
Cdd:TIGR02324 153 GEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVMDVT 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-245 |
1.30e-24 |
|
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: 102.23 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQR-VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLlpY-PLarhpSGTIEYSGQNLLNLke 84
Cdd:cd03249 1 IEFKN--VSFRYPSRPDVpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF--YdPT----SGEILLDGVDIRDL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 kTIRHIRgNRIAMIFQEPMTSLNplhSIEKQInevlgihkgLIGKvaTKRTLELLEMV-GIPEPEKRLKALPH------- 156
Cdd:cd03249 71 -NLRWLR-SQIGLVSQEPVLFDG---TIAENI---------RYGK--PDATDEEVEEAaKKANIHDFIMSLPDgydtlvg 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 ----ELSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQ 232
Cdd:cd03249 135 ergsQLSGGQKQRIAIARALLRNPKILLLDEATSALD--AESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQ 211
|
250
....*....|...
gi 1834229548 233 RGCIVEQASCEQL 245
Cdd:cd03249 212 NGQVVEQGTHDEL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-271 |
1.57e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.77 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLpYPLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:COG3839 4 LELENVSKSY--GG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMI-AGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 irhiRGnrIAMIFQEP-----MTSL-N---PLhsiekqinEVLGIHKGLIgkvaTKRTLELLEMVGIpepEKRLKALPHE 157
Cdd:COG3839 75 ----RN--IAMVFQSYalyphMTVYeNiafPL--------KLRKVPKAEI----DRRVREAAELLGL---EDLLDRKPKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
250 260 270
....*....|....*....|....*....|....
gi 1834229548 238 EQASCEQLFRAPQHPYTRELLaaepsGTPATNVV 271
Cdd:COG3839 214 QVGTPEELYDRPANLFVAGFI-----GSPPMNLL 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-261 |
1.67e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.65 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLlnlKEKTIRHI------RGnriam 97
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL-----APDSGEVLWDGEPL---DPEDRRRIgylpeeRG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 98 ifqepmtsLNPLHSIEKQInEVLGIHKGLIGKVATKRTLELLEMVGIPE-PEKRLKalphELSGGQRQRVMIAMALANEP 176
Cdd:COG4152 82 --------LYPKMKVGEQL-VYLARLKGLSKAEAKRRADEWLERLGLGDrANKKVE----ELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 177 ELLIADEPTTALD-VTVQlkILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLfRApQHPYTR 255
Cdd:COG4152 149 ELLILDEPFSGLDpVNVE--LLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI-RR-QFGRNT 224
|
....*.
gi 1834229548 256 ELLAAE 261
Cdd:COG4152 225 LRLEAD 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-507 |
2.32e-24 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 101.29 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL--GLAILrLIGSKGGIRFEGkqLDSLtqQQVRPLRREMQVVFQ 369
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTL-LKPTSGRATVAG--HDVV--REPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 370 DPfgSLSPRMCVSQIVGEGLRIHKMGTeAEQEQAIIAALKEVGLdPETRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:cd03265 81 DL--SVDDELTGWENLYIHARLYGVPG-AERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-234 |
2.97e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 100.97 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFV---VGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQ----N 78
Cdd:COG4778 4 LLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCI-YGNYLPDSGSILVRHDggwvD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LLNLKEKTIRHIRGNRIAMIFQEpmtslnpLHSIEKQ-----INEVLgIHKGLIGKVATKRTLELLEMVGIPEpekRLKA 153
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQF-------LRVIPRVsaldvVAEPL-LERGVDREEARARARELLARLNLPE---RLWD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 L-PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:COG4778 148 LpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVT 226
|
..
gi 1834229548 233 RG 234
Cdd:COG4778 227 PF 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-237 |
3.84e-24 |
|
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: 100.02 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDLAVEFvvgERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplarhpSGTI-EYSGQNLLNlKEKT 86
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKT----TLAKIL--------AGLIkESSGSILLN-GKPI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRIAMIFQEPMTSLnplhsIEKQINEVLGIHKGLIGKVATKrTLELLEMVGIPEPEKRLkalPHELSGGQRQRV 166
Cdd:cd03226 65 KAKERRKSIGYVMQDVDYQL-----FTDSVREELLLGLKELDAGNEQ-AETVLKDLDLYALKERH---PLSLSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-247 |
4.58e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGER-CQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPlarhPSGTIEYS-GQNLLN 81
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE-P----TSGEVNVRvGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHiRGNR---IAMIFQEpmTSLNPLHSIEKQINEVLGIHkgLIGKVATKRTLELLEMVGIPEPEKR--LKALPH 156
Cdd:TIGR03269 352 MTKPGPDG-RGRAkryIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEEKAEeiLDKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCI 236
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|.
gi 1834229548 237 VEQASCEQLFR 247
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
299-504 |
5.91e-24 |
|
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: 98.27 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGSKGGIRFEGKQLDSLTQQQVRplRREMQVVFQdpfgsls 376
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTL-MKILsgLYKPDSGEILVDGKEVSFASPRDAR--RAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcvsqivgeglrihkmgteaeqeqaiiaalkevgldpetrhrypheFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1834229548 457 RTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:cd03216 115 PAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-239 |
8.77e-24 |
|
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: 99.25 E-value: 8.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLPyPLARHPSGTIEYSGQNLLNLKEKTirhiRGnrIAMIFQEpmT 104
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIA-GLEEPTSGRIYIGGRDVTDLPPKD----RD--IAMVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLNPLHSIEKQINEVLGIHKGLIGKVAtKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEID-ERVREVAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 185 TTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGcIVEQ 239
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG-QIQQ 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
256-483 |
1.06e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 256 ELLAAEPSGTPATNVVGPPMLTVEDLKVWFPikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRL 335
Cdd:COG4178 343 EAADALPEAASRIETSEDGALALEDLTLRTP----------DGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 336 I------GSkGGIRfegkqldsltqqqvRPLRREMQVVFQDPF---GSL-----SPRmcvsqivgeglrihkmGTEAEQE 401
Cdd:COG4178 409 IaglwpyGS-GRIA--------------RPAGARVLFLPQRPYlplGTLreallYPA----------------TAEAFSD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 402 QAIIAALKEVGLDP-----ETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRslQSKYNL 476
Cdd:COG4178 458 AELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGT 535
|
....*..
gi 1834229548 477 TYLFISH 483
Cdd:COG4178 536 TVISVGH 542
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
273-517 |
1.12e-23 |
|
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: 99.67 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWfpikkgllkktvdY--VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQL 349
Cdd:COG0410 1 MPMLEVENLHAG-------------YggIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDGEDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSL-TQQQVR------PLRREMqvvfqdpFGSLSprmcvsqiVGEGLRihkMGTEAEQEQAIIAA-LKEV-GLDP---ET 417
Cdd:COG0410 68 TGLpPHRIARlgigyvPEGRRI-------FPSLT--------VEENLL---LGAYARRDRAEVRAdLERVyELFPrlkER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 418 RHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMV 497
Cdd:COG0410 130 RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYV 208
|
250 260
....*....|....*....|
gi 1834229548 498 VKQGQVVEQGDAQSIFAAPQ 517
Cdd:COG0410 209 LERGRIVLEGTAAELLADPE 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
306-512 |
1.13e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 306 NFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKqldslTQQQVRPLRREMQVVFQDpfGSLSPRMC 380
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL----LNLIAgfltpASGSLTLNGQ-----DHTTTPPSRRPVSMLFQE--NNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVG----EGLRIhkmgtEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK10771 88 VAQNIGlglnPGLKL-----NAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 457 RTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
304-507 |
1.15e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.19 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKqldSLTQQQVRPLRREMQVVFQDPfgsLSPRMCVS 382
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGqVLLDGV---PLVQYDHHYLHRQVALVGQEP---VLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 QIVGEGLrihkmgTEAEQEQaIIAALKEVGLDP---ETRHRYPHE-------FSGGQRQRIAIARALVLKPALILLDEPT 452
Cdd:TIGR00958 573 ENIAYGL------TDTPDEE-IMAAAKAANAHDfimEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 453 SALDRTVQRqvveLLRSLQSKYNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-258 |
1.80e-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: 101.42 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 41 LVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEktirHIRGnrIAMIFQEpmTSLNPLHSIEKQINEVL 120
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLA-GFEQPDSGSIMLDGEDVTNVPP----HLRH--INMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 121 GIhKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELL 200
Cdd:TIGR01187 68 KM-RKVPRAEIKPRVLEALRLVQLEEFADRK---PHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 201 KELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRELL 258
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-504 |
3.07e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.00 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPikkgllKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQL 349
Cdd:COG1101 1 MLELKNLSKTFN------PGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTL----LNAIAgslppDSGSILIDGKDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQqvrplRREMQV--VFQDPFGSLSPRMCVsqivgE-------------GLRIhkmGTEAEQEQAIIAALKEVGLD 414
Cdd:COG1101 71 TKLPEY-----KRAKYIgrVFQDPMMGTAPSMTI-----EenlalayrrgkrrGLRR---GLTKKRRELFRELLATLGLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 415 PETRHRYPHEF-SGGQRQRIAIARALVLKPALILLDEPTSALD-RTVQrQVVELLRSLQSKYNLTYLFISHDLAvvKALS 492
Cdd:COG1101 138 LENRLDTKVGLlSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKTAA-LVLELTEKIVEENNLTTLMVTHNME--QALD 214
|
250
....*....|....
gi 1834229548 493 H--QLMVVKQGQVV 504
Cdd:COG1101 215 YgnRLIMMHEGRII 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
297-516 |
3.72e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.29 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 297 DYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGiRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLs 376
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKG-KVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcVSQIVGEGLrihKMGTE------AEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK13644 91 ----VGRTVEEDL---AFGPEnlclppIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-249 |
3.94e-23 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 103.50 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL---PYPLarhpSGTIEYSGQNLLNLK 83
Cdd:TIGR03797 452 IEVDR--VTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKS----TLLRLLlgfETPE----SGSVFYDGQDLAGLD 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRhirgNRIAMIFQ--EPMTSlnplhSIEKQInevlgihkgLIGKVAT-KRTLELLEMVGIpepEKRLKALP---H- 156
Cdd:TIGR03797 522 VQAVR----RQLGVVLQngRLMSG-----SIFENI---------AGGAPLTlDEAWEAARMAGL---AEDIRAMPmgmHt 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 -------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLkelqARLGMALLLISHDLNLVKRiAHRVC 229
Cdd:TIGR03797 581 visegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIY 655
|
250 260
....*....|....*....|
gi 1834229548 230 VMQRGCIVEQASCEQLFRAP 249
Cdd:TIGR03797 656 VLDAGRVVQQGTYDELMARE 675
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
256-485 |
4.07e-23 |
|
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: 102.82 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 256 ELLAAEPSG-TPATNVVGPPMLTVEDLKVWFPikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILR 334
Cdd:TIGR02868 314 AGPVAEGSApAAGAVGLGKPTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 335 LIGSKGG-IRFEGKQLDSLTQQQVRplrREMQVVFQDP--FGSlsprmcvsqIVGEGLRIhkmGTEAEQEQAIIAALKEV 411
Cdd:TIGR02868 384 LLDPLQGeVTLDGVPVSSLDQDEVR---RRVSVCAQDAhlFDT---------TVRENLRL---ARPDATDEELWAALERV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 412 GLDPETRhRYPH-----------EFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYnlTYLF 480
Cdd:TIGR02868 449 GLADWLR-ALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVL 525
|
....*
gi 1834229548 481 ISHDL 485
Cdd:TIGR02868 526 ITHHL 530
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-255 |
4.19e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplarHPS-GTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEpmT 104
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI------EPTrGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--F 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLNPLHSIEKqiNEVLGIH-KGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:PRK10070 116 ALMPHMTVLD--NTAFGMElAGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 184 PTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTR 255
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-247 |
5.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.70 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLN-LKEKTIRHIRgNRIAMIFQEPMTSLN 107
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALL-----KPTTGTVTVDDITITHkTKDKYIRPVR-KRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 108 PlHSIEKQI-----NEVLGIHKgligkvATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:PRK13646 100 E-DTVEREIifgpkNFKMNLDE------VKNYAHRLLMDLGFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
275-514 |
6.04e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.54 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLkvWF-----PIKKGLlkkTVDYVKAVdginfslpqgqTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQ 348
Cdd:PRK13638 1 MLATSDL--WFryqdePVLKGL---NLDFSLSP-----------VTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDsLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQIvgeGLRIHKMGT-EAEQEQAIIAALKEVGLDpETRHRYPHEFSG 427
Cdd:PRK13638 65 LD-YSKRGLLALRQQVATVFQDPEQQIFYTDIDSDI---AFSLRNLGVpEAEITRRVDEALTLVDAQ-HFRHQPIQCLSH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 428 GQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTyLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:PRK13638 140 GQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
....*..
gi 1834229548 508 DAQSIFA 514
Cdd:PRK13638 219 APGEVFA 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-246 |
8.84e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGERCQR--VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhPSGTIEYSgQNLLN 81
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLI------PSEGKVYV-DGLDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHIRgNRIAMIFQepmtslNPLHSIEKQI--------NEVLGIHKGLIgkvaTKRTLELLEMVGIPEPEKRLka 153
Cdd:PRK13633 75 SDEENLWDIR-NKAGMVFQ------NPDNQIVATIveedvafgPENLGIPPEEI----RERVDESLKKVGMYEYRRHA-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 lPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQR 233
Cdd:PRK13633 142 -PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS 219
|
250
....*....|...
gi 1834229548 234 GCIVEQASCEQLF 246
Cdd:PRK13633 220 GKVVMEGTPKEIF 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
255-515 |
1.03e-22 |
|
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: 101.75 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 255 RELLAAEPSGTPATNVVGP-PMLTVEDLKVWFPIKKGLLkktvdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGlail 333
Cdd:COG4618 309 NELLAAVPAEPERMPLPRPkGRLSVENLTVVPPGSKRPI---------LRGVSFSLEPGEVLGVIGPSGSGKSTLA---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 334 RLI-G----SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDP--F-GSlsprmcvsqiVGEGlrIHKMGtEAEQEqAII 405
Cdd:COG4618 376 RLLvGvwppTAGSVRLDGADLSQWDREE---LGRHIGYLPQDVelFdGT----------IAEN--IARFG-DADPE-KVV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 406 AALKEVGLdpetrhrypHEF-------------------SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVEL 466
Cdd:COG4618 439 AAAKLAGV---------HEMilrlpdgydtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1834229548 467 LRSLQSKyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:COG4618 510 IRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-237 |
1.18e-22 |
|
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: 94.42 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvTAHSILrllpyplarhpSGTIEY-SGQnllnlkektIRhIRGnriamifqEP 102
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKS-TLMKIL-----------SGLYKPdSGE---------IL-VDG--------KE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNPLHSIEkqinevLGIhkgligkvatkrtlellEMVgipepekrlkalpHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03216 64 VSFASPRDARR------AGI-----------------AMV-------------YQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
1.22e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.75 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAveFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPLarhpSGTIEYSGqnlLN 81
Cdd:PRK13632 3 NKSVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKS-TISKILTGLLKPQ----SGEIKIDG---IT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHIRGNrIAMIFQEPMtslnplhsiekqiNEVLGI-----------HKGLIGKVATKRTLELLEMVGIpepEKR 150
Cdd:PRK13632 73 ISKENLKEIRKK-IGIIFQNPD-------------NQFIGAtveddiafgleNKKVPPKKMKDIIDDLAKKVGM---EDY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 151 LKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKrIAHRVCV 230
Cdd:PRK13632 136 LDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIV 214
|
250
....*....|....*.
gi 1834229548 231 MQRGCIVEQASCEQLF 246
Cdd:PRK13632 215 FSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-250 |
1.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKS-VTAHSILRLLPyplarhPSGTIEYSGQNL-LNLKEKTIRHIRgNRIAMIFQEPMTSL 106
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKStLMQHFNALLKP------SSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 107 NPlHSIEKQInEVLGIHKGLIGKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTT 186
Cdd:PRK13641 99 FE-NTVLKDV-EFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 187 ALDVTVQLKILELLKELQaRLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-281 |
1.41e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.78 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLN-LKEKTIRHIRgNRIAMIFQEPMTSLN 107
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKS----TLLQHLN-GLLQPTSGTVTIGERVITAgKKNKKLKPLR-KKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 108 PlHSIEKQIneVLG-IHKGLIGKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTT 186
Cdd:PRK13634 100 E-ETVEKDI--CFGpMNFGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 187 ALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPqhpytrELLAAEPSGTP 266
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP------DELEAIGLDLP 248
|
250 260
....*....|....*....|....*..
gi 1834229548 267 ATN------------VVGPPMLTVEDL 281
Cdd:PRK13634 249 ETVkfkraleekfgiSFPKPCLTLEEL 275
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
302-518 |
1.42e-22 |
|
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: 101.94 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGlailRLIG-----SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---G 373
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpWSGEILFDGIPREEIPREV---LANSVAMVDQDIFlfeG 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SlsprmcvsqiVGEGLrihKMGTEAEQEQAIIAALKEVGLDPETRHR---YPHE-------FSGGQRQRIAIARALVLKP 443
Cdd:TIGR03796 568 T----------VRDNL---TLWDPTIPDADLVRACKDAAIHDVITSRpggYDAElaegganLSGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 444 ALILLDEPTSALDRTVQRQVVELLRslqsKYNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQGDAQSIFAAPQH 518
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVGGA 704
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
301-528 |
1.43e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 101.33 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDPFgslsprm 379
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDI---PLTKLQLDSWRSRLAVVSQTPF------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVGEGLRIHKMG-TEAEQEQAiiAALKEV---------GLDPETRHRYPHeFSGGQRQRIAIARALVLKPALILLD 449
Cdd:PRK10789 400 LFSDTVANNIALGRPDaTQQEIEHV--ARLASVhddilrlpqGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 450 EPTSALDRTVQRQVVELLRslQSKYNLTYLFISHDL-AVVKAlsHQLMVVKQGQVVEQGDAQSIFAAP---QHPYTQQLL 525
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLsALTEA--SEILVMQHGHIAQRGNHDQLAQQSgwyRDMYRYQQL 552
|
...
gi 1834229548 526 EAA 528
Cdd:PRK10789 553 EAA 555
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-245 |
1.51e-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: 96.20 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVefVVGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplARhpSGTIEYSGQNLLNLK 83
Cdd:COG0410 1 MPMLEVENLHA--GYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP---PR--SGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 -EKTIRhiRGnrIAM------IFqepmtslnPLHSIEKqiNEVLGIHKGLiGKVATKRTLE-LLEMVgiPEPEKRLKALP 155
Cdd:COG0410 72 pHRIAR--LG--IGYvpegrrIF--------PSLTVEE--NLLLGAYARR-DRAEVRADLErVYELF--PRLKERRRQRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 HELSGGQRQRVMIAMALANEPELLIADEPTTAL---------DVTVQLkilellkelqARLGMALLLISHDLNLVKRIAH 226
Cdd:COG0410 135 GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLapliveeifEIIRRL----------NREGVTILLVEQNARFALEIAD 204
|
250
....*....|....*....
gi 1834229548 227 RVCVMQRGCIVEQASCEQL 245
Cdd:COG0410 205 RAYVLERGRIVLEGTAAEL 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-237 |
1.80e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQ-RVVEGVSFDIKRGETLALVGESGSGKSV-TAHSILRLLPyplarhPSGTIEYSGQNLLNLKE 84
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLNALLLP------DTGTIEWIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 ---------------------KTIRHIRgNRIAMIFQEPMTSLNPlHSIEKQIneVLG-IHKGLIGKVATKRTLELLEMV 142
Cdd:PRK13651 77 tkekekvleklviqktrfkkiKKIKEIR-RRVGVVFQFAEYQLFE-QTIEKDI--IFGpVSMGVSKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 143 GIPEpeKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQArlGMALLLISHDLNLV 221
Cdd:PRK13651 153 GLDE--SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQ--GKTIILVTHDLDNV 228
|
250
....*....|....*.
gi 1834229548 222 KRIAHRVCVMQRGCIV 237
Cdd:PRK13651 229 LEWTKRTIFFKDGKII 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-265 |
1.85e-22 |
|
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: 98.65 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEpmTSLNP 108
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKT----TLIRLIA-GLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 LHSIEKqiNEVLGIHKGLiGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:TIGR02142 89 HLSVRG--NLRYGMKRAR-PSERRISFERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYtrelLAAEPSGT 265
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW----LAREDQGS 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
307-528 |
2.08e-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: 95.69 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 307 FSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQldsltqqqVRPLRREMQVVFQDPFGSLSPRMCVSQIV 385
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpAKGTVKVAGAS--------PGKGWRHIGYVPQRHEFAWDFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 386 GEGlRIHKMG----TEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQR 461
Cdd:TIGR03771 73 MSG-RTGHIGwlrrPCVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 462 QVVELLRSLQSKYNlTYLFISHDLAVVKALSHQLMVVkQGQVVEQGdaqsifaapqHPytQQLLEAA 528
Cdd:TIGR03771 151 LLTELFIELAGAGT-AILMTTHDLAQAMATCDRVVLL-NGRVIADG----------TP--QQLQDPA 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-516 |
2.11e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.69 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPfgslsprMCVSQI 384
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPES---WRKHLSWVGQNP-------QLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 385 VGEGLRihkMGTEAEQEQAIIAALKEVGLD---PETRHRYPHE-------FSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:PRK11174 439 LRDNVL---LGNPDASDEQLQQALENAWVSeflPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 455 LDRTVQRQVVELLRslQSKYNLTYLFISHDLAVVKALShQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PRK11174 516 LDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQWD-QIWVMQDGQIVQQGDYAELSQAG 574
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-249 |
3.07e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.95 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVefVVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSGQNLL 80
Cdd:COG4559 1 MLEAENLSV--RLGGR--TLLDDVSLTLRPGELTAIIGPNGAGKS----TLLKLLtgeltPS------SGEVRLNGRPLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKEKTIRHIRgnriAMIFQEpmTSLN-PLHsiekqINEV--LG-IHKGLIGKVATKRTLELLEMVGIPEPEKRLKalpH 156
Cdd:COG4559 67 AWSPWELARRR----AVLPQH--SSLAfPFT-----VEEVvaLGrAPHGSSAAQDRQIVREALALVGLAHLAGRSY---Q 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 ELSGGQRQRVMIAMALA-------NEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVC 229
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRIL 211
|
250 260
....*....|....*....|
gi 1834229548 230 VMQRGCIVEQASCEQLFRAP 249
Cdd:COG4559 212 LLHQGRLVAQGTPEEVLTDE 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-256 |
3.85e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNLLNLKEK 85
Cdd:PRK14239 5 ILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhIRgNRIAMIFQEPmtslNPL-HSIEKqiNEVLGIH-KGLIGKVATKRTLEL-LEMVGI-PEPEKRLKALPHELSGG 161
Cdd:PRK14239 81 TVD-LR-KEIGMVFQQP----NPFpMSIYE--NVVYGLRlKGIKDKQVLDEAVEKsLKGASIwDEVKDRLHDSALGLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMalLLISHDLNLVKRIAHRVCVMQRGCIVEQAS 241
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
250
....*....|....*
gi 1834229548 242 CEQLFRAPQHPYTRE 256
Cdd:PRK14239 231 TKQMFMNPKHKETED 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
292-507 |
3.99e-22 |
|
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: 94.65 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQV------RPLRREM 364
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGeVLFDGKPLDIAARNRIgylpeeRGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 365 QVVFQ-DPFGSLsprmcvsqivgEGLRIHkmgtEAEQEqaIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKP 443
Cdd:cd03269 86 KVIDQlVYLAQL-----------KGLKKE----EARRR--IDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 444 ALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-190 |
5.64e-22 |
|
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: 94.08 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEK 85
Cdd:COG4133 2 MLEAENLSCRR--GER--LLFSGLSFTLAAGEALALTGPNGSGKT----TLLRIL-AGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIrgnriAMIFQEPM--TSLNPLhsiekqinEVLGIHKGLIGKVATKRTL-ELLEMVGIpepEKRLKALPHELSGGQ 162
Cdd:COG4133 73 YRRRL-----AYLGHADGlkPELTVR--------ENLRFWAALYGLRADREAIdEALEAVGL---AGLADLPVRQLSAGQ 136
|
170 180
....*....|....*....|....*...
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDA 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
304-484 |
5.75e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLgLAILRLI--GSKGGIRFEGKQLDSLTQQQVRPLR-REMQVVFQDPFgsLSPRMC 380
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTL-LAILAGLddGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFM--LIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRIHKMGTEAEQEQAIiAALKEVGLDPETRHrYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQ 460
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAK-ALLEQLGLGKRLDH-LPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180
....*....|....*....|....
gi 1834229548 461 RQVVELLRSLQSKYNLTYLFISHD 484
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHD 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
253-515 |
6.24e-22 |
|
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: 99.34 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 253 YTR--ELLAAEPSGTPATNVVGPP-MLTVEDLKVWFPIKKgllkKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLG 329
Cdd:TIGR01842 291 YKRlnELLANYPSRDPAMPLPEPEgHLSVENVTIVPPGGK----KPT-----LRGISFSLQAGEALAIIGPSGSGKSTLA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 330 LAILRLIG-SKGGIRFEGKQLDSLTQQQVRP----LRREMQVVfqdpfgslsprmcvSQIVGEGlrIHKMGTEAEQEQaI 404
Cdd:TIGR01842 362 RLIVGIWPpTSGSVRLDGADLKQWDRETFGKhigyLPQDVELF--------------PGTVAEN--IARFGENADPEK-I 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 405 IAALKEVGLDpETRHRYPHEF-----------SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSK 473
Cdd:TIGR01842 425 IEAAKLAGVH-ELILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR 503
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1834229548 474 yNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:TIGR01842 504 -GITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
6.86e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 6.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 3 QDNLIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSV---TAHSILRLLPYPLARHpSGTIEYSGQNL 79
Cdd:PRK13636 2 EDYILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTlfqNLNGILKPSSGRILFD-GKPIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 LNLKEKtirhirgnrIAMIFQEPMtslNPLHSIEKQINEVLG-IHKGLIGKVATKRTLELLEMVGIpepeKRLKALP-HE 157
Cdd:PRK13636 78 MKLRES---------VGMVFQDPD---NQLFSASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
....*....
gi 1834229548 238 EQASCEQLF 246
Cdd:PRK13636 222 LQGNPKEVF 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
294-512 |
7.08e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.85 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 294 KTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI---GS-KGGIRFEGKQLdslTQQQVRPLRRE-MQVVF 368
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVyphGTyEGEIIFEGEEL---QASNIRDTERAgIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDPfgSLSPRMCVSQIV------GEGLRIH--KMGTEAEQeqaiiaALKEVGLD--PETRHRyphEFSGGQRQRIAIARA 438
Cdd:PRK13549 89 QEL--ALVKELSVLENIflgneiTPGGIMDydAMYLRAQK------LLAQLKLDinPATPVG---NLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 439 LVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-189 |
7.43e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.41 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNLLNLKEK 85
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKP----TSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQE--PMTSLNPLHSIEkqineVLGIHKGLIGKVATKRTLELLEMVGIPEpekRLKALPHELSGGQR 163
Cdd:PRK10535 79 ALAQLRREHFGFIFQRyhLLSHLTAAQNVE-----VPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQ 150
|
170 180
....*....|....*....|....*.
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALD 189
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALD 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
7.83e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFvvgERCQRVVEGVSFDIKRGETLALVGESGSGKSVtahsilrllpypLARHPSGTIE-YSGQNLLNLK 83
Cdd:PRK13652 2 HLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKST------------LFRHFNGILKpTSGSVLIRGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRGNR--IAMIFQEPMTSL-NPlhSIEKQIneVLG-IHKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELS 159
Cdd:PRK13652 67 PITKENIREVRkfVGLVFQNPDDQIfSP--TVEQDI--AFGpINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ 239
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
250
....*....|
gi 1834229548 240 ASCEQLFRAP 249
Cdd:PRK13652 220 GTVEEIFLQP 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
305-523 |
7.92e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 7.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLP-QGQTlGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQL-DSLTQQQVRPLRREMQVVFQDpfGSLSPRMCV 381
Cdd:PRK11144 17 VNLTLPaQGIT-AIFGRSGAGKTSLINAISGLTRpQKGRIVLNGRVLfDAEKGICLPPEKRRIGYVFQD--ARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 382 SQIVGEGLRiHKMgteAEQEQAIIAALkevGLDPETRhRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQR 461
Cdd:PRK11144 94 RGNLRYGMA-KSM---VAQFDKIVALL---GIEPLLD-RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 462 QVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ-HPYTQQ 523
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPWLPK 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-248 |
1.06e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEfvVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSGQNLL 80
Cdd:PRK13548 2 MLEARNLSVR--LGGR--TLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALsgelsPD------SGEVRLNGRPLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKektiRHIRGNRIAMIFQEpmTSLN-PLhsiekQINEV--LGIHKGLIGKVATKRTL-ELLEMVGIPEPEKRLKalpH 156
Cdd:PRK13548 68 DWS----PAELARRRAVLPQH--SSLSfPF-----TVEEVvaMGRAPHGLSRAEDDALVaAALAQVDLAHLAGRDY---P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 ELSGGQRQRVMIAMALA------NEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCV 230
Cdd:PRK13548 134 QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
250
....*....|....*...
gi 1834229548 231 MQRGCIVEQASCEQLFRA 248
Cdd:PRK13548 214 LHQGRLVADGTPAEVLTP 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
301-529 |
1.10e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.85 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQL---DSLTQQQVRP--LRREMQVVFQ--DPFg 373
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTfhgKNLYAPDVDPveVRRRIGMVFQkpNPF- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 slsPRMCVSQIvGEGLRIHkmGTEAEQEQAIIAALKEVGLDPETRHRYPHE---FSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK14243 104 ---PKSIYDNI-AYGARIN--GYKGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKYnlTYLFISHDLAVVKALSHQLMVV---------KQGQVVEQGDAQSIFAAPQHPYT 521
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQAT 255
|
....*...
gi 1834229548 522 QQLLEAAF 529
Cdd:PRK14243 256 RDYVSGRF 263
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-260 |
1.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.78 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 13 AVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNLLNLKEktIRHIRg 92
Cdd:PRK14271 24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRD--VLEFR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 93 NRIAMIFQEPmtslNPL-HSIEKQINEVLGIHKGLIGK----VATKRTLEllemVGIPEPEK-RLKALPHELSGGQRQRV 166
Cdd:PRK14271 101 RRVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKefrgVAQARLTE----VGLWDAVKdRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLgmALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF 246
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
250
....*....|....
gi 1834229548 247 RAPQHPYTRELLAA 260
Cdd:PRK14271 251 SSPKHAETARYVAG 264
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
300-507 |
1.93e-21 |
|
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: 98.27 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---GS- 374
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeILLNGFSLKDIDRHT---LRQFINYLPQEPYifsGSi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 -----LSPRMCVSQ-IVGEGLRIHKMGTEAEQEQaiiaalkeVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILL 448
Cdd:TIGR01193 565 lenllLGAKENVSQdEIWAACEIAEIKDDIENMP--------LGYQTELSEE-GSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 449 DEPTSALDRTVQRQVVELLRSLQSKynlTYLFISHDLAVVKaLSHQLMVVKQGQVVEQG 507
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-245 |
2.07e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 93.06 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLL-FRFYDVSSGSILIDGQDIREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRhirgNRIAMIFQEpmTSL------------NPLHSIEKQIN--EVLGIH---KGLIGKVATkrtlelleMVGipepEK 149
Cdd:cd03253 73 LR----RAIGVVPQD--TVLfndtigynirygRPDATDEEVIEaaKAAQIHdkiMRFPDGYDT--------IVG----ER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 150 RLKalpheLSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL-----GMALLLISHDLNLVKRi 224
Cdd:cd03253 135 GLK-----LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE-------REIQAALrdvskGRTTIVIAHRLSTIVN- 201
|
250 260
....*....|....*....|.
gi 1834229548 225 AHRVCVMQRGCIVEQASCEQL 245
Cdd:cd03253 202 ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-240 |
2.41e-21 |
|
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: 92.28 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKEKT 86
Cdd:cd03268 1 LKTNDLTKTY--GKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI-----KPDSGEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 irhirgNRIAMIFQEPmtSLNPLHSIEKQinevLGIHKGLIGkVATKRTLELLEMVGIPEPEKRLKALpheLSGGQRQRV 166
Cdd:cd03268 72 ------RRIGALIEAP--GFYPNLTAREN----LRLLARLLG-IRKKRIDEVLDVVGLKDSAKKKVKG---FSLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 167 MIAMALANEPELLIADEPTTALDvTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQA 240
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLD-PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
275-533 |
2.59e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.54 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVwfpikkGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLT 353
Cdd:PRK11231 2 TLRTENLTV------GYGTKRI-----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtVFLGDKPISMLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQvrpLRREMQVVFQDPfgsLSPR-MCVSQIVGEGLRIHK--MGTEAEQEQAIIA-ALKEVGLDpETRHRYPHEFSGGQ 429
Cdd:PRK11231 71 SRQ---LARRLALLPQHH---LTPEgITVRELVAYGRSPWLslWGRLSAEDNARVNqAMEQTRIN-HLADRRLTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGda 509
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-- 220
|
250 260
....*....|....*....|....
gi 1834229548 510 qsifaAPQHPYTQQLLEAAFLVPA 533
Cdd:PRK11231 221 -----TPEEVMTPGLLRTVFDVEA 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-515 |
3.97e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFPI--------KKGLL---KKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG---- 337
Cdd:COG1134 2 SSMIEVENVSKSYRLyhepsrslKELLLrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAgile 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 338 -SKGGIRFEGKqldsltqqqVRPLrREMQVVFQdpfGSLSPRmcvsqivgE----GLRIHKMgTEAEQEQAI--IAALKE 410
Cdd:COG1134 78 pTSGRVEVNGR---------VSAL-LELGAGFH---PELTGR--------EniylNGRLLGL-SRKEIDEKFdeIVEFAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 411 VG--LDPETRHrypheFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVV 488
Cdd:COG1134 136 LGdfIDQPVKT-----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|....*..
gi 1834229548 489 KALSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:COG1134 210 RRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
300-507 |
4.00e-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: 91.70 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEGKQLDSLtqqQVRPLRREMQVVFQDPfgslspr 378
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTI---PLEDLRSSLTIIPQDP------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHKMGTEAEqeqaIIAALK--EVGLDpetrhrypheFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSDEE----IYGALRvsEGGLN----------LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 457 RTVQRQVVELLRSLQSkyNLTYLFISHDLAVVkALSHQLMVVKQGQVVEQG 507
Cdd:cd03369 158 YATDALIQKTIREEFT--NSTILTIAHRLRTI-IDYDKILVMDAGEVKEYD 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-245 |
4.31e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 30 SFDIKRGETLALVGESGSGKSvtahSILRLLPYPLARHpsgtieySGQNLLNLKEKTIRHIRGNRIAMIFQEpmTSLNPL 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGFLTPA-------SGSLTLNGQDHTTTPPSRRPVSMLFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 110 HSIEKQINevLGIHKGLIGKVATKRTLE-LLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:PRK10771 86 LTVAQNIG--LGLNPGLKLNAAQREKLHaIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-246 |
4.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIE----YSGQNLLNL---------KEKTIRHIR 91
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI-----KSKYGTIQvgdiYIGDKKNNHelitnpyskKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 92 gNRIAMIFQEPMTSLNPlHSIEKQIN---EVLGIHKgligKVATKRTLELLEMVGIPEPekRLKALPHELSGGQRQRVMI 168
Cdd:PRK13631 116 -RRVSMVFQFPEYQLFK-DTIEKDIMfgpVALGVKK----SEAKKLAKFYLNKMGLDDS--YLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 169 AMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF 246
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-249 |
4.86e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLl 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRF--GS--NTVIDNLNLTIKQGTMVTLLGPSGCGKT----TVLRLVA-GLEKPTEGQIFIDGEDV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 nlkekTIRHIRGNRIAMIFQEpmTSLNPLHSIEKQIN---EVLGIHKGLIgkvaTKRTLELLEMVGIPEPEKRLKalpHE 157
Cdd:PRK11432 71 -----THRSIQQRDICMVFQS--YALFPHMSLGENVGyglKMLGVPKEER----KQRVKEALELVDLAGFEDRYV---DQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
250
....*....|..
gi 1834229548 238 EQASCEQLFRAP 249
Cdd:PRK11432 217 QIGSPQELYRQP 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
302-512 |
6.68e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.07 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQvrpLRREMQVVFQDPfgSLSPRMC 380
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGeVLVDGLDVATTPSRE---LAKRLAILRQEN--HINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRIHKMG--TeAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:COG4604 92 VRELVAFGRFPYSKGrlT-AEDREIIDEAIAYLDLED-LADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 459 VQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:COG4604 170 HSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-250 |
6.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.94 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLARH--PSGTIEYSGqnlLN 81
Cdd:PRK13640 3 DNIVEFKH--VSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKS----TISKLINGLLLPDdnPNSKITVDG---IT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHIRgNRIAMIFQEPMtslnplhsiekqiNEVLGIHKGliGKVATKrtlelLEMVGIPEPEKR----------- 150
Cdd:PRK13640 74 LTAKTVWDIR-EKVGIVFQNPD-------------NQFVGATVG--DDVAFG-----LENRAVPRPEMIkivrdvladvg 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 151 ----LKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKrIAH 226
Cdd:PRK13640 133 mldyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MAD 211
|
250 260
....*....|....*....|....
gi 1834229548 227 RVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:PRK13640 212 QVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
301-507 |
8.26e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 95.86 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTqqqVRPLRREMQVV------FQDPFG 373
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYT---LASLRNQVALVsqnvhlFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 -----SLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLdpetrhryphEFSGGQRQRIAIARALVLKPALILL 448
Cdd:PRK11176 435 nniayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGV----------LLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 449 DEPTSALDRTVQRQVVELLRSLQSkyNLTYLFISHDLAVVKAlSHQLMVVKQGQVVEQG 507
Cdd:PRK11176 505 DEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
300-513 |
9.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQ-QVRPLRREMQVVFQDPFGSLSP 377
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQkEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIvgeGLRIHKMGTEAEQEQAIIA-ALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK13643 100 ETVLKDV---AFGPQNFGIPKEKAEKIAAeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 457 RTVQRQVVELLRSLQsKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIF 513
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
304-503 |
1.05e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 90.99 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKqldSLTQQQVRPLRREMQVVFQDPfgSLSPRmCVS 382
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqVLLDGK---PISQYEHKYLHSKVSLVGQEP--VLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 QIVGEGLRIHKMGTEAEQEQAIIA----ALKEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKAHAhsfiSELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 459 VQRQVVELLRslQSKYNLTYLFISHDLAVVKAlSHQLMVVKQGQV 503
Cdd:cd03248 185 SEQQVQQALY--DWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
289-507 |
1.47e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 90.85 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 289 KGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGkqLDSLTQQqvRPLRREMQV 366
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-LKILSglLQPTSGEVRVAG--LVPWKRR--KKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VF---QDPFGSLSPRmcvsqivgEGLRIHKM-----GTEAEQEQAIIAALKEVG--LDPETRhryphEFSGGQRQRIAIA 436
Cdd:cd03267 99 VFgqkTQLWWDLPVI--------DSFYLLAAiydlpPARFKKRLDELSELLDLEelLDTPVR-----QLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 437 RALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
294-512 |
1.48e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 94.89 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 294 KTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI---GS-KGGIRFEGKQLDSltqQQVRPLRREMQVVFQ 369
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVyphGTwDGEIYWSGSPLKA---SNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 370 DPFgSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAA---LKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:TIGR02633 85 QEL-TLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAknlLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-512 |
1.56e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKvwfpikkgllkKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLT 353
Cdd:COG4152 1 MLELKGLT-----------KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGeVLWDGEPLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQV------RPLRREM----QVVFqdpFGSLsprmcvsqivgEGLrihkmgTEAEQEQAIIAALKEVGLdPETRHRYPH 423
Cdd:COG4152 70 RRRIgylpeeRGLYPKMkvgeQLVY---LARL-----------KGL------SKAEAKRRADEWLERLGL-GDRANKKVE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 424 EFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
....*....
gi 1834229548 504 VEQGDAQSI 512
Cdd:COG4152 208 VLSGSVDEI 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-249 |
1.58e-20 |
|
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: 93.24 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNlKEKTIR---HIRgnRIAMIFQEPmtS 105
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKT----TLLRAIA-GLERPDSGRIRLGGEVLQD-SARGIFlppHRR--RIGYVFQEA--R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LNPLHSIEKqiNEVLGIHKglIGKVATKRTL-ELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEP 184
Cdd:COG4148 88 LFPHLSVRG--NLLYGRKR--APRAERRISFdEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 185 TTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAP 249
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-246 |
1.86e-20 |
|
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: 90.36 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPSGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEP-- 102
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-----PQKGQILIDGIDIRDISRKSLR----SMIGVVLQDTfl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 ----------MTSLNPLHSIEKQINEVLGIHKgLIgkvatkRTLE--LLEMVGipepEKrlkalPHELSGGQRQRVMIAM 170
Cdd:cd03254 89 fsgtimenirLGRPNATDEEVIEAAKEAGAHD-FI------MKLPngYDTVLG----EN-----GGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 171 ALANEPELLIADEPTTALDV----TVQLKILELlkelqaRLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQASCEQLF 246
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTetekLIQEALEKL------MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-234 |
2.19e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.93 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKTIRHIRgNRIAMIFQEP 102
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKS----TLLKLI-CGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNplHSIEKQINEVLgIHKGLIGKVATKRTLELLEMVGIPEpekRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:PRK10908 89 HLLMD--RTVYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 183 EPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
301-512 |
2.32e-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: 89.89 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSL-TQQQVRplrREMQVVFQ--DPFGSLS 376
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGsIRLDGEDITKLpPHERAR---AGIAYVPQgrEIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcvsqiVGEGLRIhKMGTEAEQEQAIIA-------ALKEVgldpetRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:TIGR03410 92 --------VEENLLT-GLAALPRRSRKIPDeiyelfpVLKEM------LGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-245 |
2.49e-20 |
|
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: 89.98 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLP--YPLArhpSGTIEYSGQNLLNLKE 84
Cdd:cd03251 1 VEFKN--VTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPrfYDVD---SGRILIDGHDVRDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KTIRhirgNRIAMIFQEPMtslnpLHS--IEKQIN-EVLGIHKGLIGKVAtkRTLELLEMV-GIPE------PEKRLKal 154
Cdd:cd03251 72 ASLR----RQIGLVSQDVF-----LFNdtVAENIAyGRPGATREEVEEAA--RAANAHEFImELPEgydtviGERGVK-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 pheLSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVKRiAHRVCVMQRG 234
Cdd:cd03251 139 ---LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDG 212
|
250
....*....|.
gi 1834229548 235 CIVEQASCEQL 245
Cdd:cd03251 213 KIVERGTHEEL 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
276-509 |
2.65e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVwfpikkgllkkTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILrliGS------KGGIRFEGKQL 349
Cdd:COG0396 1 LEIKNLHV-----------SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM---GHpkyevtSGSILLDGEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 350 DSLTQQQvRPlRREMQVVFQDP----------FgsLspRMCVSQIVGEGLRIHKMGTEAEQeqaiiaALKEVGLDPETRH 419
Cdd:COG0396 67 LELSPDE-RA-RAGIFLAFQYPveipgvsvsnF--L--RTALNARRGEELSAREFLKLLKE------KMKELGLDEDFLD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 420 RYPHE-FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHD---LAVVKAlsHQL 495
Cdd:COG0396 135 RYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYqriLDYIKP--DFV 211
|
250
....*....|....
gi 1834229548 496 MVVKQGQVVEQGDA 509
Cdd:COG0396 212 HVLVDGRIVKSGGK 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
302-503 |
3.08e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 88.04 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDP--FGslspr 378
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNE---LGDHVGYLPQDDelFS----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 mcvsqivgeglrihkmGTEAEqeqaIIaalkevgldpetrhrypheFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:cd03246 90 ----------------GSIAE----NI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 459 VQRQVVELLRSLQSKyNLTYLFISHDLAVVKALShQLMVVKQGQV 503
Cdd:cd03246 131 GERALNQAIAALKAA-GATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-260 |
3.43e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNLLNlKEKTIRHIRgNRIAMIFQEP 102
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYE-RRVNLNRLR-RQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mtSLNPLhSIEKQIN---EVLGIHKGLIGKVATKRTLELLEMvgIPEPEKRLKALPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PRK14258 98 --NLFPM-SVYDNVAygvKIVGWRPKLEIDDIVESALKDADL--WDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 180 IADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQR-----GCIVEQASCEQLFRAPQHPYT 254
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRT 252
|
....*.
gi 1834229548 255 RELLAA 260
Cdd:PRK14258 253 REYVLS 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-250 |
3.45e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.52 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVT---AHSILRllpyplarhPSG--------TIEY 74
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILK---------PTSgevlikgePIKY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 75 SGQNLLNLKEKtirhirgnrIAMIFQEPMTSL-NPlhSIEKQIneVLG-IHKGLIGKVATKRTLELLEMVGIPEPEKRLk 152
Cdd:PRK13639 69 DKKSLLEVRKT---------VGIVFQNPDDQLfAP--TVEEDV--AFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKP- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 alPHELSGGQRQRVMIAMALANEPELLIADEPTTALDvTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:PRK13639 135 --PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD-PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMS 211
|
250
....*....|....*...
gi 1834229548 233 RGCIVEQASCEQLFRAPQ 250
Cdd:PRK13639 212 DGKIIKEGTPKEVFSDIE 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-239 |
4.75e-20 |
|
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: 88.70 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 33 IKRGETLALVGESGSGKSvtahSILRLLP-YPLARhpsgtieySGQNLLNLKEKTIRHIRGNRIAMIFQEpmTSLNPLHS 111
Cdd:cd03298 21 FAQGEITAIVGPSGSGKS----TLLNLIAgFETPQ--------SGRVLINGVDVTAAPPADRPVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 112 IEKQINevLGIHKGL-IGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:cd03298 87 VEQNVG--LGLSPGLkLTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834229548 191 TVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ 239
Cdd:cd03298 162 ALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-234 |
6.05e-20 |
|
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: 88.33 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERCQRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNLLnlkeKT 86
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKT-TTLKMLTGELRP----TSGTAYINGYSIR----TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNrIAMIFQEPM--TSLNPLhsiekqinEVLGIH---KGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGG 161
Cdd:cd03263 70 RKAARQS-LGYCPQFDAlfDELTVR--------EHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDV--------TVQLKilellkelqaRLGMALLLISHDLNLVKRIAHRVCVMQR 233
Cdd:cd03263 138 MKRKLSLAIALIGGPSVLLLDEPTSGLDPasrraiwdLILEV----------RKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
.
gi 1834229548 234 G 234
Cdd:cd03263 208 G 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-508 |
6.94e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVWFPIK----------KGLLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSK 339
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTikmltGI----LVPTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 340 GGIRFEGKqldsltqqqvRPLRREMQ------VVF-------QDpfgsLSPRmcvsqivgEGLRIHK--MGTEAEQEQAI 404
Cdd:COG4586 77 GEVRVLGY----------VPFKRRKEfarrigVVFgqrsqlwWD----LPAI--------DSFRLLKaiYRIPDAEYKKR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 405 IAALKEV-GLDP--ETRHRyphEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFI 481
Cdd:COG4586 135 LDELVELlDLGEllDTPVR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLT 211
|
250 260
....*....|....*....|....*..
gi 1834229548 482 SHDLAVVKALSHQLMVVKQGQVVEQGD 508
Cdd:COG4586 212 SHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
293-514 |
7.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.68 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 293 KKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEG--KQLDSLTQ-QQVRPLRREMQVVFQ 369
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKiKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 370 DPFGSLSpRMCVSQIVGEGlRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:PRK13645 98 FPEYQLF-QETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-256 |
8.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.95 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLP-YPLARHPSGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEPm 103
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 tslNPLH--SIEKQINEVLGIHkGLIGKVATKRTLE-LLEMVGI-PEPEKRLKALPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PRK14246 100 ---NPFPhlSIYDNIAYPLKSH-GIKEKREIKKIVEeCLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 180 IADEPTTALDVTvqLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQHPYTRE 256
Cdd:PRK14246 176 LMDEPTSMIDIV--NSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-237 |
8.39e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 88.54 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 21 RCQRVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLPYPLarHP-SGTIEYSGqnLLNLKEKtIRHIRgnRIAMIF 99
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTT----LKILSGLL--QPtSGEVRVAG--LVPWKRR-KKFLR--RIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 100 QE---------PMTSLNPLHSIEKqinevlgihkglIGKVATKRTL-ELLEMVGIpepEKRLKALPHELSGGQRQRVMIA 169
Cdd:cd03267 101 GQktqlwwdlpVIDSFYLLAAIYD------------LPPARFKKRLdELSELLDL---EELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 170 MALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
274-529 |
8.69e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFpikkgllkktvDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSL 352
Cdd:PRK09536 2 PMIDVSDLSVEF-----------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 353 TqqqVRPLRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIH--KMGTEAEQEQAII-AALKEVGLDpETRHRYPHEFSGGQ 429
Cdd:PRK09536 71 S---ARAASRRVASVPQDT--SLSFEFDVRQVVEMGRTPHrsRFDTWTETDRAAVeRAMERTGVA-QFADRPVTSLSGGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
250 260
....*....|....*....|
gi 1834229548 510 QSIFAAPQhpytqqlLEAAF 529
Cdd:PRK09536 224 ADVLTADT-------LRAAF 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
274-507 |
9.05e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.89 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVWFpikKGLLkktvdyvkAVDGINFSLPQGQTLGIVGESGSGKSTlglaILRLIG-----SKGGIRFEGKQ 348
Cdd:PRK11300 4 PLLSVSGLMMRF---GGLL--------AVNNVNLEVREQEIVSLIGPNGAGKTT----VFNCLTgfykpTGGTILLRGQH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDSL------------TQQQVRpLRREMQVVfqdpfgslsPRMCVSQ--IVGEGLRIHKMGT----EAEQEQAIIAA--L 408
Cdd:PRK11300 69 IEGLpghqiarmgvvrTFQHVR-LFREMTVI---------ENLLVAQhqQLKTGLFSGLLKTpafrRAESEALDRAAtwL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 409 KEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVV 488
Cdd:PRK11300 139 ERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
250
....*....|....*....
gi 1834229548 489 KALSHQLMVVKQGQVVEQG 507
Cdd:PRK11300 218 MGISDRIYVVNQGTPLANG 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
300-507 |
1.00e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 86.60 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGKQLDSLTQQqvrpLRREMQVVFQDPF---GS 374
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTgdLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPYlfdTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 375 LsprmcvsqivgeglrihkmgteaeqeqaiiaaLKEVGLdpetrhryphEFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:cd03247 91 L--------------------------------RNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 455 LDRTVQRQVVELLrsLQSKYNLTYLFISHDLAVVKALShQLMVVKQGQVVEQG 507
Cdd:cd03247 129 LDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHMD-KILFLENGKIIMQG 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-245 |
1.14e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNLLNLKEKTIRHirgnRIAMIFQEPMTs 105
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDP----QSGRILIDGTDIRTVTRASLRR----NIAVVFQDAGL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LNplHSIEKQInevlgihkgLIGKV-ATKRtlELLEMVG-------IPEPEKRLKALPHE----LSGGQRQRVMIAMALA 173
Cdd:PRK13657 421 FN--RSIEDNI---------RVGRPdATDE--EMRAAAEraqahdfIERKPDGYDTVVGErgrqLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 174 NEPELLIADEPTTALDVTVqlkilellkelQARLGMAL---------LLISHDLNLVkRIAHRVCVMQRGCIVEQASCEQ 244
Cdd:PRK13657 488 KDPPILILDEATSALDVET-----------EAKVKAALdelmkgrttFIIAHRLSTV-RNADRILVFDNGRVVESGSFDE 555
|
.
gi 1834229548 245 L 245
Cdd:PRK13657 556 L 556
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-258 |
1.20e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.36 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFVVGErcqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNLLNLKE 84
Cdd:PRK14267 3 FAIETVNLRVYYGSNH----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KTIRHIRgnRIAMIFQEPmtslNPLHSIEKQINEVLGIHkgLIGKVATKRTLE------LLEMVGIPEPEKRLKALPHEL 158
Cdd:PRK14267 79 DPIEVRR--EVGMVFQYP----NPFPHLTIYDNVAIGVK--LNGLVKSKKELDervewaLKKAALWDEVKDRLNDYPSNL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTvqLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPV--GTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
250 260
....*....|....*....|
gi 1834229548 239 QASCEQLFRAPQHPYTRELL 258
Cdd:PRK14267 229 VGPTRKVFENPEHELTEKYV 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-248 |
1.43e-19 |
|
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: 87.93 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLAR-----HPSGTIE---YSGQNLLNLKEKTI--RHIRGNr 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdgHDLALADpawLRRQVGVVLQENVLfnRSIRDN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 95 IAMIFQEPmtslnPLHSIEkQINEVLGIHKGLigkvatkrtLELLE----MVGipepEKRLKalpheLSGGQRQRVMIAM 170
Cdd:cd03252 96 IALADPGM-----SMERVI-EAAKLAGAHDFI---------SELPEgydtIVG----EQGAG-----LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 171 ALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQASCEQLFRA 248
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-234 |
1.56e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLpYPLARHPSGTIEYSGQNLlnlkEKT 86
Cdd:PRK13537 8 IDFRN--VEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTT----LRML-LGLTHPDAGSISLCGEPV----PSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQepMTSLNPLHSIEKQInEVLGIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRV 166
Cdd:PRK13537 75 ARHAR-QRVGVVPQ--FDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
300-484 |
1.93e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGS-----KGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDP--F 372
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTL----LKIVASlisptSGTLLFEGEDISTLKPEI---YRQQVSYCAQTPtlF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 GslsprmcvsQIVGEGLRI-HKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:PRK10247 94 G---------DTVYDNLIFpWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|...
gi 1834229548 452 TSALDRTVQRQVVELLRSLQSKYNLTYLFISHD 484
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-507 |
2.06e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.20 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVWFPIKKG---LLKKT--------VDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SK 339
Cdd:cd03220 1 IELENVSKSYPTYKGgssSLKKLgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLAgiyppDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 340 GGIRFEGKqldsltqqqVRPLrREMQVVFQdpfGSLSPRMCVsQIVGeglRIHKM-GTEAEQEQAIIAALKEVGLDPETR 418
Cdd:cd03220 77 GTVTVRGR---------VSSL-LGLGGGFN---PELTGRENI-YLNG---RLLGLsRKEIDEKIDEIIEFSELGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 419 HRyphEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALSHQLMVV 498
Cdd:cd03220 140 VK---TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVL 215
|
....*....
gi 1834229548 499 KQGQVVEQG 507
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-237 |
2.10e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 87.04 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLpYPLARHPSGTIEYSGQNLLNLKEK 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRML-AGLLEPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhirgnRIAMIFQEpmTSLNPLHSIEKQINEVLGIHkGLIGKVATKRTLELLEMVGIPE-PEKRLKalphELSGGQRQ 164
Cdd:cd03266 76 ARR-----RLGFVSDS--TGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEElLDRRVG----GFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVqLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIV 237
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMA-TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
2.43e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 85.56 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLavefvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpYPLARHPSGTIEYSGQNLlnlK 83
Cdd:cd03215 2 EPVLEVRGL--------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL-----FGLRPPASGEITLDGKPV---T 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRGNRIAMIFQEPM-TSLNPLHSIEKQInevlgihkgligkvatkrtlellemvgipepekrlkALPHELSGGQ 162
Cdd:cd03215 66 RRSPRDAIRAGIAYVPEDRKrEGLVLDLSVAENI------------------------------------ALSSLLSGGN 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDV-TVQlkILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVgAKA--EIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-246 |
3.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplarhpsgtIEYSGQNLL-------NLKE-KTIRHIRgNRI 95
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-----------ISETGQTIVgdyaipaNLKKiKEVKRLR-KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 96 AMIFQEPMTSLNPlHSIEKQIneVLG-IHKGLIGKVATKRTLELLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALAN 174
Cdd:PRK13645 93 GLVFQFPEYQLFQ-ETIEKDI--AFGpVNLGENKQEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 175 EPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF 246
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
290-526 |
4.97e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 290 GLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQVRplrREMQVVF 368
Cdd:PRK10253 16 GYGKYTV-----AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVA---RRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDpfGSLSPRMCVSQIVGEGLRIHK-MGTE--AEQEQAIIAALKEVGLDPETRHRYpHEFSGGQRQRIAIARALVLKPAL 445
Cdd:PRK10253 88 QN--ATTPGDITVQELVARGRYPHQpLFTRwrKEDEEAVTKAMQATGITHLADQSV-DTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGdaqsifaAPQHPYTQQLL 525
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELI 237
|
.
gi 1834229548 526 E 526
Cdd:PRK10253 238 E 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
299-509 |
5.13e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQLDSLTQQQVRPLRREMqvVFQDPfg 373
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLmkilyGL----YQPDSGEILIDGKPVRIRSPRDAIALGIGM--VHQHF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SLSPRMCVSQ--IVG-EGLRIHKMGTEAEQEQaIIAALKEVGL--DPetrHRYPHEFSGGQRQRIAIARALVLKPALILL 448
Cdd:COG3845 90 MLVPNLTVAEniVLGlEPTKGGRLDRKAARAR-IRELSERYGLdvDP---DAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 449 DEPTSALdrTVQ--RQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDA 509
Cdd:COG3845 166 DEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-266 |
5.59e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNLKEKTIrhirGNRIAMIFQEP 102
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT-PQ----SGTVFLGDKPISMLSSRQL----ARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNPlhSIEKQINEVLGIHKGLIGKVATK---RTLELLEMVGIPE-PEKRLKalphELSGGQRQRVMIAMALANEPEL 178
Cdd:PRK11231 86 LTPEGI--TVRELVAYGRSPWLSLWGRLSAEdnaRVNQAMEQTRINHlADRRLT----DLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 179 LIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFrapqhpyTRELL 258
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-------TPGLL 231
|
250
....*....|....*....
gi 1834229548 259 A----------AEP-SGTP 266
Cdd:PRK11231 232 RtvfdveaeihPEPvSGTP 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-246 |
5.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVvGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLlnlK 83
Cdd:PRK13642 2 NKILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF-----EEFEGKVKIDGELL---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRgNRIAMIFQEPMtslNPLHSIEKQINEVLGI-HKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQ 162
Cdd:PRK13642 73 AENVWNLR-RKIGMVFQNPD---NQFVGATVEDDVAFGMeNQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQASC 242
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
....
gi 1834229548 243 EQLF 246
Cdd:PRK13642 225 SELF 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-258 |
6.69e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAveFVVGERCqrVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLaRHPSGTIEYSGQNLL 80
Cdd:PRK11831 2 QSVANLVDMRGVS--FTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQI-APDHGEILFDGENIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKEKTIRHIRgNRIAMIFQEP--MTSLNPLHSIEKQINEvlgiHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHEL 158
Cdd:PRK11831 73 AMSRSRLYTVR-KRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGL---RGAAKLMPSEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
250 260
....*....|....*....|
gi 1834229548 239 QASCEQLfRAPQHPYTRELL 258
Cdd:PRK11831 225 HGSAQAL-QANPDPRVRQFL 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
276-507 |
8.22e-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: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVWFPIKKGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGS--KGGIRFEGKQLDS 351
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQL-----LKNVSGKAKPGELTAIMGPSGAGKSTL-LNALagRRTGLgvSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 352 LTqqqvrpLRREMQVVFQDP--FGSLSPRmcvsqivgEGLRIHkmgteaeqeqaiiAALKevGLdpetrhryphefSGGQ 429
Cdd:cd03213 78 RS------FRKIIGYVPQDDilHPTLTVR--------ETLMFA-------------AKLR--GL------------SGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 430 RQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDL-AVVKALSHQLMVVKQGQVVEQG 507
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
301-496 |
1.05e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTL--GLA-ILRLIGskGGIRFEGKQLDSLTQQQVR-----PLRremqvvfqdpf 372
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLlkVLAgVLRPTS--GTVRRAGGARVAYVPQRSEvpdslPLT----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 gslsprmcVSQIVGEGLRIHKMGT---EAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:NF040873 74 --------VRDLVAMGRWARRGLWrrlTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLM 496
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-236 |
1.16e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLArhpsGTIEYSGQNLLNLKEKT 86
Cdd:PRK09536 4 IDVSDLSVEF--GD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PTA----GTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IrhirGNRIAMIFQEpmTSLNPLHSIEKQINEVLGIHKGLIGKV--ATKRTLE-LLEMVGIPEPEKRLKAlphELSGGQR 163
Cdd:PRK09536 75 A----SRRVASVPQD--TSLSFEFDVRQVVEMGRTPHRSRFDTWteTDRAAVErAMERTGVAQFADRPVT---SLSGGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLkelqARL---GMALLLISHDLNLVKRIAHRVCVMQRGCI 236
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV----RRLvddGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-228 |
1.31e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhPSgtieySGqnllnlkekTIRHIRGNRIAMIFQE- 101
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------PT-----SG---------TVRRAGGARVAYVPQRs 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 ------PMTslnplhsiekqINEVLGI----HKGLIGKV---ATKRTLELLEMVGIPEPEKRlkALpHELSGGQRQRVMI 168
Cdd:NF040873 65 evpdslPLT-----------VRDLVAMgrwaRRGLWRRLtrdDRAAVDDALERVGLADLAGR--QL-GELSGGQRQRALL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 169 AMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRV 228
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-247 |
1.59e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.95 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNL-KEKTIRHIRgNRIAMIFQEP 102
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLN-GLHVPTQGSVRVDDTLITSTsKNKDIKQIR-KKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNPlhsiEKQINEV------LGIHKgligKVATKRTLELLEMVGIPEP--EKRlkalPHELSGGQRQRVMIAMALAN 174
Cdd:PRK13649 95 ESQLFE----ETVLKDVafgpqnFGVSQ----EEAEALAREKLALVGISESlfEKN----PFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 175 EPELLIADEPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-248 |
1.90e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEfvvgercqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpYPLARHPSGTIEYSGqnllnlKEK 85
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL-----FGADPADSGEIRLDG------KPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIR---GNRIAMIfqeP----MTSLNPLHSIEKqiNEVLGI-----HKGLI-GKVATKRTLELLEMVGI--PEPEKR 150
Cdd:COG1129 317 RIRSPRdaiRAGIAYV---PedrkGEGLVLDLSIRE--NITLASldrlsRGGLLdRRRERALAEEYIKRLRIktPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 151 LKalphELSGGQRQRVMIAMALANEPELLIADEPTTALDV--------TVQlkilellkeLQARLGMALLLISHDLNLVK 222
Cdd:COG1129 392 VG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaeiyrLIR---------ELAAEGKAVIVISSELPELL 458
|
250 260 270
....*....|....*....|....*....|.
gi 1834229548 223 RIAHRVCVMQRGCIV-----EQASCEQLFRA 248
Cdd:COG1129 459 GLSDRILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-245 |
2.04e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDlaVEFVVGERC-QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLlpYplarHP-SGTIEYSGQNLLNLK 83
Cdd:TIGR00958 478 LIEFQD--VSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--Y----QPtGGQVLLDGVPLVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRhirgNRIAMIFQEPMtslnpLHSIEKQINEVLGIHKGLIGKV-ATKRTLELLEMVGIPEPEKRLKALPH--ELSG 160
Cdd:TIGR00958 550 HHYLH----RQVALVGQEPV-----LFSGSVRENIAYGLTDTPDEEImAAAKAANAHDFIMEFPNGYDTEVGEKgsQLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQA 240
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
....*
gi 1834229548 241 SCEQL 245
Cdd:TIGR00958 696 THKQL 700
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
305-517 |
2.56e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.62 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDsltqqQVRPLRREMQVVFQDPfgSLSPRM 379
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTL----LRMIAglediTSGDLFIGEKRMN-----DVPPAERGVGMVFQSY--ALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVGEGLRIHKMG-TEAEQEQAIIAALKEVG--LDpetrhRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK11000 91 SVAENMSFGLKLAGAKkEEINQRVNQVAEVLQLAhlLD-----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 457 RTVQRQV-VELLRsLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:PRK11000 166 AALRVQMrIEISR-LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-236 |
3.14e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.67 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLlpYPLARhpsGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEPMt 104
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF--YQPQG---GQVLLDGKPISQYEHKYLH----SKVSLVGQEPV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 slnpLHSIEKQINevlgIHKGLiGKVATKRTLELLEMVG----IPEPEKRLKALPHE----LSGGQRQRVMIAMALANEP 176
Cdd:cd03248 99 ----LFARSLQDN----IAYGL-QSCSFECVKEAAQKAHahsfISELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 177 ELLIADEPTTALDVTVQLKILELLKELQARlgMALLLISHDLNLVKRiAHRVCVMQRGCI 236
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
299-510 |
4.30e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLIG--SKGGIRFEGKQLDSLTQQQVRPLRRE-MQVVFQDPfgSL 375
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLDkpTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRY--HL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SPRMCVSQIVgEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:PRK10535 98 LSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQ 510
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQ 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-245 |
6.36e-18 |
|
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: 87.08 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNLLNLKEK 85
Cdd:TIGR02203 330 DVEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPR-FYEPDSGQILLDGHDLADYTLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRhirgNRIAMIFQEpmtslnpLHSIEKQINEvlGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHE-------- 157
Cdd:TIGR02203 403 SLR----RQVALVSQD-------VVLFNDTIAN--NIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvl 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDvtvqlkiLELLKELQARL-----GMALLLISHDLNLVKRiAHRVCVMQ 232
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALD-------NESERLVQAALerlmqGRTTLVIAHRLSTIEK-ADRIVVMD 541
|
250
....*....|...
gi 1834229548 233 RGCIVEQASCEQL 245
Cdd:TIGR02203 542 DGRIVERGTHNEL 554
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
304-513 |
7.00e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.53 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTqqqVRPLRREMQVVFQDPF---GSlsprm 379
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGeIRVNGREIGAYG---LRELRRQFSMIPQDPVlfdGT----- 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cVSQIVGEGLrihkmgtEAEQEQaIIAALKEVGLdpetRHRYPHE--------------FSGGQRQRIAIARALVLK-PA 444
Cdd:PTZ00243 1400 -VRQNVDPFL-------EASSAE-VWAALELVGL----RERVASEsegidsrvleggsnYSVGQRQLMCMARALLKKgSG 1466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 445 LILLDEPTSALDRTVQRQVVELLRSLQSKYnlTYLFISHDLAVVkALSHQLMVVKQGQVVEQG-------DAQSIF 513
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTV-AQYDKIIVMDHGAVAEMGsprelvmNRQSIF 1539
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
300-513 |
7.40e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGKQLDSLTQ-QQVRPLRREMQVVFQDPfgsls 376
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTI-MQLLNglHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQFP----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcVSQIVGEG-LRIHKMG------TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:PRK13649 95 ----ESQLFEETvLKDVAFGpqnfgvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIF 513
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-237 |
9.56e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVefvVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPSGTIEYSGQNLLNLk 83
Cdd:COG3845 255 EVVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDGEDITGL- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 ekTIRHIRGNRIAMIFQEPM-TSLNPLHSIEKqiNEVLGIH-------KGLI-GKVATKRTLELLEMVGI--PEPEKRLK 152
Cdd:COG3845 326 --SPRERRRLGVAYIPEDRLgRGLVPDMSVAE--NLILGRYrrppfsrGGFLdRKAIRAFAEELIEEFDVrtPGPDTPAR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 ALphelSGGQRQRVMIAMALANEPELLIADEPTTALDV----TVqlkilellkelQARL------GMALLLISHDLNLVK 222
Cdd:COG3845 402 SL----SGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFI-----------HQRLlelrdaGAAVLLISEDLDEIL 466
|
250
....*....|....*
gi 1834229548 223 RIAHRVCVMQRGCIV 237
Cdd:COG3845 467 ALSDRIAVMYEGRIV 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-515 |
1.06e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvtahSILRLLP--YPLarhPSGTIEYSGQNllnlkektiRHIRGNR------IAMIF 99
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKS----TMMKVLTgiYTR---DAGSILYLGKE---------VTFNGPKssqeagIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 100 QEpmtsLN--PLHSIEKQIneVLGIH-KGLIGKVATKRTLE----LLEMVGIPEPEKRLKAlphELSGGQRQRVMIAMAL 172
Cdd:PRK10762 86 QE----LNliPQLTIAENI--FLGREfVNRFGRIDWKKMYAeadkLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 173 ANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRG-----CIVEQASCEQLF- 246
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGqfiaeREVADLTEDSLIe 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 247 ----RAPQHPYTRelLAAEPsgtpatnvvGPPMLTVEDLkvwfpikKGllkktvdyvKAVDGINFSLPQGQTLGIVGESG 322
Cdd:PRK10762 236 mmvgRKLEDQYPR--LDKAP---------GEVRLKVDNL-------SG---------PGVNDVSFTLRKGEILGVSGLMG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 323 SGKSTLGLAIL-RLIGSKGGIRFEGKQLDSLTQQQvrPLRREMQVVFQDPFG-------SLSPRMCVS---QIVGEGLRI 391
Cdd:PRK10762 289 AGRTELMKVLYgALPRTSGYVTLDGHEVVTRSPQD--GLANGIVYISEDRKRdglvlgmSVKENMSLTalrYFSRAGGSL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 392 HKmgteAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQ 471
Cdd:PRK10762 367 KH----ADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1834229548 472 SKyNLTYLFISHDLAVVKALSHQLMVVKQGQV-----VEQGDAQSIFAA 515
Cdd:PRK10762 443 AE-GLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMAA 490
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
292-510 |
1.20e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaILRLIGSKGGIRFEGKQLDSLTQ---------QQVRPLRR 362
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTL---LRHLSGLITGDKSAGSHIELLGRtvqregrlaRDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 363 EMQVVFQDpfGSLSPRMCVSqivgEGLRIHKMGT-----------EAEQEQAIIAALKEVGLdPETRHRYPHEFSGGQRQ 431
Cdd:PRK09984 87 NTGYIFQQ--FNLVNRLSVL----ENVLIGALGStpfwrtcfswfTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 432 RIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQ 510
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-504 |
1.20e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplarhpSGtiEY---SGQNLLNLKEKTIRHIR---GNRIAM 97
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKS----TLLKIL--------SG--NYqpdAGSILIDGQEMRFASTTaalAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 98 IFQEpmtslnpLHSI-EKQINEVLGI----HK-GLI-GKVATKRTLELLEMVGIP-EPEKRLKalphELSGGQRQRVMIA 169
Cdd:PRK11288 84 IYQE-------LHLVpEMTVAENLYLgqlpHKgGIVnRRLLNYEAREQLEHLGVDiDPDTPLK----YLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 170 MALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQ-ASCEQLfra 248
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 249 pqhpyTRELLAAEPSGTPATNV-------VGPPMLTVEDLKvwfpiKKGLlkktvdyvkaVDGINFSLPQGQTLGIVGES 321
Cdd:PRK11288 229 -----DRDQLVQAMVGREIGDIygyrprpLGEVRLRLDGLK-----GPGL----------REPISFSVRAGEIVGLFGLV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 322 GSGKSTLglaiLRLI-----GSKGGIRFEGKQLD-SLTQQQVR------PLRREMQVVFqdPFGSLSPRMCVS---QIVG 386
Cdd:PRK11288 289 GAGRSEL----MKLLygatrRTAGQVYLDGKPIDiRSPRDAIRagimlcPEDRKAEGII--PVHSVADNINISarrHHLR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 387 EGLRIHKmGTEAEQEQAIIAALKEVGLDPETRHRYpheFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVEL 466
Cdd:PRK11288 363 AGCLINN-RWEAENADRFIRSLNIKTPSREQLIMN---LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNV 438
|
490 500 510
....*....|....*....|....*....|....*...
gi 1834229548 467 LRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:PRK11288 439 IYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
307-529 |
1.33e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 307 FSLPQGQTLGIVGESGSGKSTLGLAILrligskGGIRFEGKQLDSLTQQQVRPLRREM-QVVFQDPFGSLSPRMCVSQIV 385
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALM------GFVRLASGKISILGQPTRQALQKNLvAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 386 GEGlRIHKMG----TEAEQEQAIIAALKEVGLdPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQR 461
Cdd:PRK15056 102 MMG-RYGHMGwlrrAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 462 QVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKqGQVVEQGDAQSIFAAPQhpytqqlLEAAF 529
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAEN-------LELAF 238
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-217 |
1.46e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.60 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLArhPSgtieySGQNLLNlkEKT 86
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIAGFLA--PS-----SGEITLD--GVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRiAMIFQEpmTSLNP-LHSIEkqiNEVLGIH-KGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQ 164
Cdd:COG4525 71 VTGPGADR-GVVFQK--DALLPwLNVLD---NVAFGLRlRGVPKAERRARAEELLALVGLADFARRR---IWQLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHD 217
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
302-502 |
1.87e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.89 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIrfegkqldsltqqqVRPLRREMQVVFQDPFgsls 376
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSL----FRALAglwpwGSGRI--------------GMPEGEDLLFLPQRPY---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prMCVsqivgeglrihkmGTEAEQeqaIIaalkevgldpetrhrYP--HEFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:cd03223 75 --LPL-------------GTLREQ---LI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1834229548 455 LDRTVQRQVVELLRSLQSkynlTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:cd03223 122 LDEESEDRLYQLLKELGI----TVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-259 |
2.42e-17 |
|
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: 81.03 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEktirHIRGNR-IA------M 97
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK-----SGSIRLDGEDITKLPP----HERARAgIAyvpqgrE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 98 IFqepmtslnPLHSIEKQINEVLGihkgLIGKVATKRTLELLEMVGIpepekrLKALPH----ELSGGQRQRVMIAMALA 173
Cdd:TIGR03410 86 IF--------PRLTVEENLLTGLA----ALPRRSRKIPDEIYELFPV------LKEMLGrrggDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 174 NEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLfrapQHPY 253
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDK 223
|
....*.
gi 1834229548 254 TRELLA 259
Cdd:TIGR03410 224 VRRYLA 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-242 |
2.56e-17 |
|
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: 80.68 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 30 SFDIKRGETLALVGESGSGKSvTAHSILRLLPYPLarhpSGTIEYSGQNLLNLKEKTirhirgNRIAMIFQEPmtslNPL 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIAGFIEPA----SGSIKVNDQSHTGLAPYQ------RPVSMLFQEN----NLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 110 HSIEKQINEVLGIHKGL-IGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:TIGR01277 83 AHLTVRQNIGLGLHPGLkLNAEQQEKVVDAAQQVGIADYLDRL---PEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASC 242
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-238 |
2.65e-17 |
|
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: 80.26 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEfvVGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpyplARHPS-----GTIEYSGQNLLN 81
Cdd:cd03217 1 LEIKDLHVS--VGGK--EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--------MGHPKyevteGEILFKGEDITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LkEKTIRHIRGnrIAMIFQEPMtslnplhsiekqinEVLGIhkgligkvatkRTLELLEMVGIpepekrlkalphELSGG 161
Cdd:cd03217 69 L-PPEERARLG--IFLAFQYPP--------------EIPGV-----------KNADFLRYVNE------------GFSGG 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDVtVQLKILELLKELQARLGMALLLISHDLNLVKRI-AHRVCVMQRGCIVE 238
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-261 |
3.17e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.90 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYplarhpSGTIEYSGQNLLN 81
Cdd:PRK11174 345 NDPVTIEAEDLEILSPDG---KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY------QGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHirgnRIAMIFQEPMTslnPLHSIEKQInevlgihkgLIGKV-ATKRTLE-LLEMVGIPEPEKRL-KALPHE- 157
Cdd:PRK11174 416 LDPESWRK----HLSWVGQNPQL---PHGTLRDNV---------LLGNPdASDEQLQqALENAWVSEFLPLLpQGLDTPi 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 ------LSGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRIaHRVCVM 231
Cdd:PRK11174 480 gdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVM 556
|
250 260 270
....*....|....*....|....*....|
gi 1834229548 232 QRGCIVEQASCEQLfrAPQHPYTRELLAAE 261
Cdd:PRK11174 557 QDGQIVQQGDYAEL--SQAGGLFATLLAHR 584
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-241 |
3.20e-17 |
|
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: 80.62 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYplarhPSGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEPMT 104
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDISKIGLHDLR----SRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 -------SLNPL--HSiEKQINEVLgihkgligkvatkRTLELLEMVgipepEKRLKALPHE-------LSGGQRQRVMI 168
Cdd:cd03244 90 fsgtirsNLDPFgeYS-DEELWQAL-------------ERVGLKEFV-----ESLPGGLDTVveeggenLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 169 AMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQAS 241
Cdd:cd03244 151 ARALLRKSKILVLDEATASVD--PETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-245 |
3.98e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVTahsILRLLPYPLARHpsGTIEYSGQNLlnlK 83
Cdd:PRK13647 2 DNIIEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHLNGIYLPQR--GRVKVMGREV---N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRgNRIAMIFQEPMtslNPLHSIEKQINEVLG-IHKGLIGKVATKRTLELLEMVGIPEpeKRLKAlPHELSGGQ 162
Cdd:PRK13647 71 AENEKWVR-SKVGLVFQDPD---DQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEALKAVRMWD--FRDKP-PYHLSYGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 163 RQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASC 242
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
...
gi 1834229548 243 EQL 245
Cdd:PRK13647 223 SLL 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-515 |
4.23e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKST-----LGLAIlrliGSKGGIRFEGKQLdsltQQQVRPLRREMQVVFQdpFGSLS 376
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTtlrmlLGLTH----PDAGSISLCGEPV----PSRARHARQRVGVVPQ--FDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 PRMCVSqivgEGLRI--HKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:PRK13537 93 PDFTVR----ENLLVfgRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 455 LDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:PRK13537 169 LDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-247 |
4.98e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHPSGTIEYSGQNllnlKEKTIRHIRgNRIAMIFQEPM 103
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 TSLNPlHSIEKQIN---EVLGIHKGLIGKVATKRtlelLEMVGIPEpeKRLKALPHELSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK13643 95 SQLFE-ETVLKDVAfgpQNFGIPKEKAEKIAAEK----LEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 181 ADEPTTALDVTVQLKILELLKELQaRLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-245 |
6.30e-17 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 84.22 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKektiRHIRGNRIAMIFQ---- 100
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKS----TIAKLVA-GLYQPWSGEILFDGIPREEIP----REVLANSVAMVDQdifl 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 ------EPMTSLNPlhSI-EKQINEVL---GIHkGLIGKVATKRTLELLEMVGipepekrlkalphELSGGQRQRVMIAM 170
Cdd:TIGR03796 565 fegtvrDNLTLWDP--TIpDADLVRACkdaAIH-DVITSRPGGYDAELAEGGA-------------NLSGGQRQRLEIAR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 171 ALANEPELLIADEPTTALDVTVQLKILELLkelqARLGMALLLISHDLNLVkRIAHRVCVMQRGCIVEQASCEQL 245
Cdd:TIGR03796 629 ALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLSTI-RDCDEIIVLERGKVVQRGTHEEL 698
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-512 |
6.71e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSltqqQVRPLRREMQVVFQdpFGSLSPRMC 380
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPA----RARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQ---IVGEGLRIHkmgteAEQEQAIIAALKEVG-LDPETRHRYPhEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK13536 131 VREnllVFGRYFGMS-----TREIEAVIPSLLEFArLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 457 RTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:PRK13536 205 PHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
305-515 |
7.18e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.61 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTlgLAILrLIG----SKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQDPFgSLSPRMC 380
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKST--LASL-LMGyyplTEGEIRLDGRPLSSLSHSV---LRQGVAMVQQDPV-VLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVGEGLRihkmgteaeqEQAIIAALKEVGLD------PETRHRYPHE----FSGGQRQRIAIARALVLKPALILLDE 450
Cdd:PRK10790 433 ANVTLGRDIS----------EEQVWQALETVQLAelarslPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 451 PTSALDRTVQRQVVELLRSLQSKynLTYLFISHDLA-VVKAlsHQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLStIVEA--DTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
293-470 |
1.05e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 79.24 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 293 KKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSK----GGIRFEGKQLDsltqqqvrplRREMQ--V 366
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttsGQILFNGQPRK----------PDQFQkcV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPFGSLSPRMCVSQIV--GEGLRIHKMGTEAE-QEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKP 443
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLtyTAILRLPRKSSDAIrKKRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180
....*....|....*....|....*..
gi 1834229548 444 ALILLDEPTSALDRTVQRQVVELLRSL 470
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
292-516 |
1.49e-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: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTQQQvrplRREMQVVF-- 368
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGKILLDGQDITKLPMHK----RARLGIGYlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDPfgSLSPRMCVSQIVGEGLRIHKMgTEAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALILL 448
Cdd:cd03218 82 QEA--SIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 449 DEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-231 |
1.72e-16 |
|
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: 82.33 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhP-SGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEPm 103
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD------PtEGSIAVNGVPLADADADSWR----DQIAWVPQHP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 tslnplHSIEKQINEVLGIHKGLIGKVATKRTLE---LLEMV-GIPEP-EKRLKALPHELSGGQRQRVMIAMALANEPEL 178
Cdd:TIGR02857 406 ------FLFAGTIAENIRLARPDASDAEIREALEragLDEFVaALPQGlDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 179 LIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVM 231
Cdd:TIGR02857 480 LLLDEPTAHLD--AETEAEVLEALRALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-239 |
2.08e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.15 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLL 80
Cdd:PRK09452 9 SSLSPLVELRGISKSF--DGKE--VISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIA-GFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NL-KEKtiRHIRgnriaMIFQEpmTSLNPLHSIEKQINEVLGIHKGLIGKVATkRTLELLEMVGIPEPEKRLkalPHELS 159
Cdd:PRK09452 80 HVpAEN--RHVN-----TVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQLEEFAQRK---PHQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIvEQ 239
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI-EQ 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
305-516 |
2.21e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSLtqqQVRPLRREMQVVFQdpfgSLSPR- 378
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTL----LKMLGrhqppSEGEILLDAQPLESW---SSKAFARKVAYLPQ----QLPAAe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 -MCVSQIVGEGlRIHKMGT----EAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:PRK10575 99 gMTVRELVAIG-RYPWHGAlgrfGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 454 ALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-190 |
2.27e-16 |
|
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: 78.97 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDlaVEFVVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpypLARHPSGtieySGQNLLNLK 83
Cdd:COG1119 1 DPLLELRN--VTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKS----TLLSLI---TGDLPPT----YGNDVRLFG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EK----TIRHIRgNRIAMIFQEPMTSLNPLHSIEkqinEV--------LGIHKGlIGKVATKRTLELLEMVGIpepEKRL 151
Cdd:COG1119 66 ERrggeDVWELR-KRIGLVSPALQLRFPRDETVL----DVvlsgffdsIGLYRE-PTDEQRERARELLELLGL---AHLA 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1834229548 152 KALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:COG1119 137 DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-218 |
2.27e-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: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvgERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNLKEKT 86
Cdd:TIGR02868 335 LELRDLSAGY---PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-PL----QGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRhirgNRIAMIFQEPmtslnplHSIEKQINEVLGIHKGligKVATKRTLELLEMVGIPEPekrLKALPH---------- 156
Cdd:TIGR02868 407 VR----RRVSVCAQDA-------HLFDTTVRENLRLARP---DATDEELWAALERVGLADW---LRALPDgldtvlgegg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 157 -ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVqlKILELLKELQARLGMALLLISHDL 218
Cdd:TIGR02868 470 aRLSGGERQRLALARALLADAPILLLDEPTEHLDAET--ADELLEDLLAALSGRTVVLITHHL 530
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-247 |
2.38e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.13 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCQ-----------------RVVEGVSFDIKRGETLALVGESGSGKSVTahsiLRLLPYPLarHP- 68
Cdd:COG4586 2 IEVENLSKTYRVYEKEPglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLTGIL--VPt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 69 SGTIEYSGqnlLNLKEKTIRHIRgnRIAMIF---QEPMTSLNPLHSIEkqineVLG-IHKglIGKVATKRTL-ELLEMVG 143
Cdd:COG4586 76 SGEVRVLG---YVPFKRRKEFAR--RIGVVFgqrSQLWWDLPAIDSFR-----LLKaIYR--IPDAEYKKRLdELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 144 IpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKR 223
Cdd:COG4586 144 L---GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEA 220
|
250 260
....*....|....*....|....
gi 1834229548 224 IAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:COG4586 221 LCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-238 |
2.72e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDLAVEfvVGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpyplARHP-----SGTIEYSGQNLLNL 82
Cdd:COG0396 2 EIKNLHVS--VEGK--EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--------MGHPkyevtSGSILLDGEDILEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 kEKTIRHIRGnrIAMIFQEP-----MTSLNPLHSIEKQINEvlgihKGLIGKVATKRTLELLEMVGIPEpekrlKALPHE 157
Cdd:COG0396 70 -SPDERARAG--IFLAFQYPveipgVSVSNFLRTALNARRG-----EELSAREFLKLLKEKMKELGLDE-----DFLDRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 L----SGGQRQRVMIAMALANEPELLIADEPTTALDV--------TVQLKILEllkelqarlGMALLLISHD---LNLVK 222
Cdd:COG0396 137 VnegfSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalrivaeGVNKLRSP---------DRGILIITHYqriLDYIK 207
|
250
....*....|....*.
gi 1834229548 223 riAHRVCVMQRGCIVE 238
Cdd:COG0396 208 --PDFVHVLVDGRIVK 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
23-189 |
6.65e-16 |
|
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: 76.46 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGeTLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEKtirhIRGnRIAMIFQEP 102
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILA-TLTPPSSGTIRIDGQDVLKQPQK----LRR-RIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSlnPLHSIEKQINeVLGIHKGLIGKVATKRTLELLEMVGIPEpekRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03264 82 GVY--PNFTVREFLD-YIAWLKGIPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
....*..
gi 1834229548 183 EPTTALD 189
Cdd:cd03264 156 EPTAGLD 162
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-189 |
6.71e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVG---ERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLP--YPLArhpSGTIEYSGQNLLN 81
Cdd:COG1101 2 LELKNLSKTFNPGtvnEK--RALDGLNLTIEEGDFVTVIGSNGAGKS----TLLNAIAgsLPPD---SGSILIDGKDVTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEktirHIRGNRIAMIFQEPMTSLNPLHSIE------KQINEVLGIHKGLIGKVAT--KRTLELLEMvGIpepEKRLKA 153
Cdd:COG1101 73 LPE----YKRAKYIGRVFQDPMMGTAPSMTIEenlalaYRRGKRRGLRRGLTKKRRElfRELLATLGL-GL---ENRLDT 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 1834229548 154 LPHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG1101 145 KVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
299-505 |
7.27e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGKQL------DSLTqQQVRPLRREMQVVfqd 370
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTL-LKILSgnYQPDAGSILIDGQEMrfasttAALA-AGVAIIYQELHLV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 371 pfgslsPRMCVSQIVGEGLRIHKMG--TEAEQEQAIIAALKEVG--LDPETRHRYpheFSGGQRQRIAIARALVLKPALI 446
Cdd:PRK11288 92 ------PEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGvdIDPDTPLKY---LSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVE 505
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-503 |
7.71e-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: 75.55 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 272 GPPMLTVEDLKVWfpikkgllkktvdyvKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLD 350
Cdd:cd03215 1 GEPVLEVRGLSVK---------------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGeITLDGKPVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 351 SLTQQQVRplRREMQVVFQDPFGslsprmcvsqivgEGLrIHKMGTEaeqEQAIIAALkevgldpetrhrypheFSGGQR 430
Cdd:cd03215 66 RRSPRDAI--RAGIAYVPEDRKR-------------EGL-VLDLSVA---ENIALSSL----------------LSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 431 QRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
276-509 |
7.79e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.03 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVwfpikkgllkkTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL---RLIGSKGGIRFEGKQLDSL 352
Cdd:cd03217 1 LEIKDLHV-----------SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 353 TQQQvRPlRREMQVVFQDPfgslsPRMcvsqivgEGLRIHKMgteaeqeqaiiaaLKEVGLDpetrhrypheFSGGQRQR 432
Cdd:cd03217 70 PPEE-RA-RLGIFLAFQYP-----PEI-------PGVKNADF-------------LRYVNEG----------FSGGEKKR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 433 IAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHD---LAVVKALSHQLMVvkQGQVVEQGDA 509
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIKPDRVHVLY--DGRIVKSGDK 189
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
303-499 |
8.19e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLGLAILRLI-GSKGGIRFEgkqldsltqqqvrplrremqvVFQDPFGSLSPrmcv 381
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkGTPVAGCVD---------------------VPDNQFGREAS---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 382 sqiVGEGLRIHKMGTEAeqeqaiIAALKEVGL-DPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQ 460
Cdd:COG2401 102 ---LIDAIGRKGDFKDA------VELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1834229548 461 RQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVK 499
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
276-508 |
8.34e-16 |
|
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: 76.92 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 276 LTVEDLKVwfpikkgllkkTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAIL---RLIGSKGGIRFEGKQLDSL 352
Cdd:TIGR01978 1 LKIKDLHV-----------SVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpSYEVTSGTILFKGQDLLEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 353 TQQQvRPlRREMQVVFQDPfgSLSPRMCVSQIVGEGLRIHkmgTEAEQEQAIIA---------ALKEVGLDPETRHRYPH 423
Cdd:TIGR01978 70 EPDE-RA-RAGLFLAFQYP--EEIPGVSNLEFLRSALNAR---RSARGEEPLDLldfekllkeKLALLDMDEEFLNRSVN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 424 E-FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALS----HQLMvv 498
Cdd:TIGR01978 143 EgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRLLNYIKpdyvHVLL-- 219
|
250
....*....|
gi 1834229548 499 kQGQVVEQGD 508
Cdd:TIGR01978 220 -DGRIVKSGD 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-236 |
1.03e-15 |
|
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: 74.95 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAveFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQnllnlkekt 86
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-PT----SGRVRLDGA--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 irhirgnriamifqepmtslnPLHSIEkqinevLGIHKGLIGKVAtkRTLELLE---MVGIpepekrlkalpheLSGGQR 163
Cdd:cd03246 65 ---------------------DISQWD------PNELGDHVGYLP--QDDELFSgsiAENI-------------LSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRiAHRVCVMQRGCI 236
Cdd:cd03246 103 QRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
1.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLL 80
Cdd:PRK13648 2 EDKNSIIVFKN--VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-----SGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKEKTIRhirgNRIAMIFQEPMTSLnpLHSIEKqINEVLGI------HKGLIGKVatKRTLELLEMVGIPEPEkrlkal 154
Cdd:PRK13648 75 DDNFEKLR----KHIGIVFQNPDNQF--VGSIVK-YDVAFGLenhavpYDEMHRRV--SEALKQVDMLERADYE------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHrVCVMQRG 234
Cdd:PRK13648 140 PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKG 218
|
250
....*....|..
gi 1834229548 235 CIVEQASCEQLF 246
Cdd:PRK13648 219 TVYKEGTPTEIF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
304-468 |
1.12e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDSltqqqvrPLRREmQVVFQDPFGSLSPR 378
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTL----LRLIAgllppAAGTIKLDGGDIDD-------PDVAE-ACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSQIVGEGLRIHkmGTEaeqEQAIIAALKEVGLDPETrHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:PRK13539 88 LTVAENLEFWAAFL--GGE---ELDIAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170
....*....|
gi 1834229548 459 VQRQVVELLR 468
Cdd:PRK13539 162 AVALFAELIR 171
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-219 |
1.13e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.98 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVtahsilrLLPYpLARHPSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEP 102
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKST-------LLAA-IAGTLSPAFSASGEVLLNGRRLTALPAEQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MtsLNPLHSIEKqiNEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:COG4136 86 L--LFPHLSVGE--NLAFALPPTIGRAQRRARVEQALEEAGLAGFADRD---PATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARLGMALLLISHDLN 219
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-241 |
1.41e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 75.53 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 3 QDNLIEVRDLAVEFvvGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYplarhPSGTIEYSGQNLLNL 82
Cdd:cd03369 3 EHGEIEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 KEKTIRhirgNRIAMIFQEPM-------TSLNPL-HSIEKQINEVLGIHKGligkvatkrtlellemvgipepekrlkal 154
Cdd:cd03369 76 PLEDLR----SSLTIIPQDPTlfsgtirSNLDPFdEYSDEEIYGALRVSEG----------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVKRIAhRVCVMQRG 234
Cdd:cd03369 123 GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYD-KILVMDAG 199
|
....*..
gi 1834229548 235 CIVEQAS 241
Cdd:cd03369 200 EVKEYDH 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-237 |
1.51e-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: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:cd03245 3 IEFRN--VSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS----TLLKLL-AGLYKPTSGSVLLDGTDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHirgnRIAMIFQEPM----------TSLNPLHSIEK--QINEVLGIHKgLIGKvaTKRTLELleMVGipepEKrlkal 154
Cdd:cd03245 76 LRR----NIGYVPQDVTlfygtlrdniTLGAPLADDERilRAAELAGVTD-FVNK--HPNGLDL--QIG----ER----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVKrIAHRVCVMQRG 234
Cdd:cd03245 138 GRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE--ERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSG 214
|
...
gi 1834229548 235 CIV 237
Cdd:cd03245 215 RIV 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-238 |
1.79e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLArhpsGTIEYSGQNLlnlkEKTIRHIRGnRIAMIFQepMT 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS-PDA----GKITVLGVPV----PARARLARA-RIGVVPQ--FD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLNPLHSIEKQInEVLGIHKGLigkvaTKRTLE-----LLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELL 179
Cdd:PRK13536 124 NLDLEFTVRENL-LVFGRYFGM-----STREIEavipsLLEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 180 IADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGC-IVE 238
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRkIAE 253
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-239 |
1.84e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 74.27 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLARHpSGTIEYSGQNLLNLkEKT 86
Cdd:cd03247 1 LSINN--VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQ-QGEITLDGVPVSDL-EKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIrgnrIAMIFQEPmtslnplHSIEKQINEVLGIhkgligkvatkrtlellemvgipepekrlkalphELSGGQRQRV 166
Cdd:cd03247 73 LSSL----ISVLNQRP-------YLFDTTLRNNLGR----------------------------------RFSGGERQRL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQ 239
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLDPITE--RQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-236 |
1.98e-15 |
|
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: 75.66 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 31 FDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPSGTIEYSGQNllnlKEKTIRHIR--GNRIAMIFQEPMtslnp 108
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP-----PAKGTVKVAGAS----PGKGWRHIGyvPQRHEFAWDFPI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 lhSIEkqiNEVLGIHKGLIG-----KVATKR-TLELLEMVGIPEPEKRLKAlphELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:TIGR03771 67 --SVA---HTVMSGRTGHIGwlrrpCVADFAaVRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLD 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 183 EPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVCVMQRGCI 236
Cdd:TIGR03771 139 EPFTGLDMPTQELLTELFIEL-AGAGTAILMTTHDLAQAMATCDRVVLLNGRVI 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
274-509 |
1.99e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.22 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 274 PMLTVEDLKVwfpikkgllkkTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAI-----LRLIgsKGGIRFEGKQ 348
Cdd:CHL00131 6 PILEIKNLHA-----------SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKIL--EGDILFKGES 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDSLTQQQvrplRREMQV--VFQDPFgslsprmcvsQIVG----EGLRI-----HKMGTEAEQE-----QAIIAALKEVG 412
Cdd:CHL00131 73 ILDLEPEE----RAHLGIflAFQYPI----------EIPGvsnaDFLRLaynskRKFQGLPELDpleflEIINEKLKLVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 413 LDPETRHRYPHE-FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISH-----DLa 486
Cdd:CHL00131 139 MDPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHyqrllDY- 216
|
250 260
....*....|....*....|...
gi 1834229548 487 VVKALSHqlmVVKQGQVVEQGDA 509
Cdd:CHL00131 217 IKPDYVH---VMQNGKIIKTGDA 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-236 |
2.31e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 19 GERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYplARHPSGTIEYSGQNLLNLKEKTIRhirgnriaMI 98
Cdd:PRK11247 23 GER--TVLNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAG--LETPSAGELLAGTAPLAEAREDTR--------LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 99 FQEpmTSLNPLHSIekqINEVlGIhkGLIGKVATkRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPEL 178
Cdd:PRK11247 87 FQD--ARLLPWKKV---IDNV-GL--GLKGQWRD-AALQALAAVGL---ADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 179 LIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCI 236
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-238 |
2.53e-15 |
|
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: 75.26 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLlpypLAR--HP-SGTIEysgqnllnlkektirhIRGnRIAMIFq 100
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKS----TLLRL----LAGiyPPdSGTVT----------------VRG-RVSSLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 EPMTSLNPLHSIEKQINEVLGIHkGLIGKVATKRTLELLEMVGIPEP-EKRLKalphELSGGQRQRVMIAMALANEPELL 179
Cdd:cd03220 90 GLGGGFNPELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELGDFiDLPVK----TYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 180 IADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
312-507 |
2.80e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 312 GQTLGIVGESGSGKSTL--GLAILRLIGSKGG--IRFEGKQLDsltqqqvrplRREMQV----VFQDP--FGSLSPRMCV 381
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLmnALAFRSPKGVKGSgsVLLNGMPID----------AKEMRAisayVQQDDlfIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 382 sqIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDP--ETRHRYPHE---FSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:TIGR00955 121 --MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 457 RTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-221 |
5.83e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarhPSgtieysgqnllnlkE 84
Cdd:PRK09544 3 SLVSLENVSVSF--GQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA------PD--------------E 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KTIRHIRGNRIAMIFQE-PMTSLNPLhSIEKQINEVLGIHKGLIGKvATKRTlellemvgipEPEKRLKALPHELSGGQR 163
Cdd:PRK09544 59 GVIKRNGKLRIGYVPQKlYLDTTLPL-TVNRFLRLRPGTKKEDILP-ALKRV----------QAGHLIDAPMQKLSGGET 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-218 |
6.10e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNlkektirhiRGNRIAMIFQEp 102
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-----HGSITLDGKPVEG---------PGAERGVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mTSLNPLHSIekQINEVLGIHKGLIGKVATK-RTLELLEMVGIPEPEKRLkalPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:PRK11248 79 -EGLLPWRNV--QDNVAFGLQLAGVEKMQRLeIAHQMLKKVGLEGAEKRY---IWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1834229548 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDL 218
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
263-521 |
6.63e-15 |
|
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: 74.56 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 263 SGTPATNVVG-PPMLTVEDLKVWFpikKGLLKKTVDYVKAVdginfsLPQGQTLGIVGESGSGKSTLGLAILRLIGS-KG 340
Cdd:cd03288 6 SGSSNSGLVGlGGEIKIHDLCVRY---ENNLKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 341 GIRFEGKQLDSLTQQQvrpLRREMQVVFQDPF---GS----LSP-RMCVSQIVGEGLRIhkmgteaEQEQAIIAALKEvG 412
Cdd:cd03288 77 KIVIDGIDISKLPLHT---LRSRLSIILQDPIlfsGSirfnLDPeCKCTDDRLWEALEI-------AQLKNMVKSLPG-G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 413 LDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLrsLQSKYNLTYLFISHDLAVVKAlS 492
Cdd:cd03288 146 LDAVVTEG-GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-A 221
|
250 260
....*....|....*....|....*....
gi 1834229548 493 HQLMVVKQGQVVEQGDAQSIFAAPQHPYT 521
Cdd:cd03288 222 DLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-245 |
9.89e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLlpYPLArhpSGTIEYSGqnlLNLKEKT 86
Cdd:PRK11176 342 IEFRN--VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF--YDID---EGEILLDG---HDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRgNRIAMIFQEpmtslnpLHSIEKQI-NEVLGIHKGLIGKVATKRTLELL-EMVGIPEPEKRLKALPHE----LSG 160
Cdd:PRK11176 412 LASLR-NQVALVSQN-------VHLFNDTIaNNIAYARTEQYSREQIEEAARMAyAMDFINKMDNGLDTVIGEngvlLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQA 240
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
....*
gi 1834229548 241 SCEQL 245
Cdd:PRK11176 561 THAEL 565
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-245 |
1.11e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplARH---PSGTIEYSGQNLLNL 82
Cdd:PRK11160 338 SLTLNN--VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLL----TRAwdpQQGEILLNGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 KEKTIRhirgNRIAMIFQEP---MTSL--NPLHSIEKQINEVLgihkgligkvatkrtLELLEMVGIP---EPEKRLKAL 154
Cdd:PRK11160 408 SEAALR----QAISVVSQRVhlfSATLrdNLLLAAPNASDEAL---------------IEVLQQVGLEkllEDDKGLNAW 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 PHE----LSGGQRQRVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQarlGMALLLISHDLNLVKRIaHRVC 229
Cdd:PRK11160 469 LGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaETERQILELLAEHAQ---NKTVLMITHRLTGLEQF-DRIC 544
|
250
....*....|....*.
gi 1834229548 230 VMQRGCIVEQASCEQL 245
Cdd:PRK11160 545 VMDNGQIIEQGTHQEL 560
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-249 |
1.39e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.58 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKT 86
Cdd:COG4604 2 IEIKNVSKRY--GG--KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHirgnRIAMIFQEPmtSLNPLHSIEkqinEVLGI-----HKGLIGK---VATKRTLELLEmvgipepekrLKALPH-- 156
Cdd:COG4604 73 LAK----RLAILRQEN--HINSRLTVR----ELVAFgrfpySKGRLTAedrEIIDEAIAYLD----------LEDLADry 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 --ELSGGQRQRVMIAMALANEPELLIADEPTTALDVtvqlkilellkeLQARLGMALL------------LISHDLNLVK 222
Cdd:COG4604 133 ldELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM------------KHSVQMMKLLrrladelgktvvIVLHDINFAS 200
|
250 260
....*....|....*....|....*..
gi 1834229548 223 RIAHRVCVMQRGCIVEQASCEQLFRAP 249
Cdd:COG4604 201 CYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-250 |
1.47e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSVTAHSILRLLPYplarhpSGTIEYSGQNLLNLKEKTIRHIRG-----NR--IAM-IFQ 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG------SGSIQFAGQPLEAWSAAELARHRAylsqqQTppFAMpVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 EPMTSL---NPLHSIEKQINEVLgihkgligkvatkrtlellEMVGIpepEKRLKALPHELSGGQRQRVMIAMAL----- 172
Cdd:PRK03695 89 YLTLHQpdkTRTEAVASALNEVA-------------------EALGL---DDKLGRSVNQLSGGEWQRVRLAAVVlqvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 173 ANEPE--LLIADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:PRK03695 147 DINPAgqLLLLDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-488 |
1.75e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 31 FDIKRGETLALVGESGSGKS----VTAHSIL---------------RLLPYPlARHPSGTI-EYSGQNLLNLKEKTIRHI 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKStlmkILNGEVLlddgriiyeqdlivaRLQQDP-PRNVEGTVyDFVAEGIEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 91 RGNRIAMifQEPMTS-LNPLhsieKQINEVLGIHKGLIGKVATKRTLELLEMvgipEPEKRLKalphELSGGQRQRVMIA 169
Cdd:PRK11147 103 DISHLVE--TDPSEKnLNEL----AKLQEQLDHHNLWQLENRINEVLAQLGL----DPDAALS----SLSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 170 MALANEPELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF--- 246
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYlle 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 247 -------RAPQHPYTRELLAAEPS----GTPA----------------------TNVVGPPMLTVEDL----KVWFPIKK 289
Cdd:PRK11147 245 keealrvEELQNAEFDRKLAQEEVwirqGIKArrtrnegrvralkalrrerserREVMGTAKMQVEEAsrsgKIVFEMEN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 290 glLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTL-GLAILRLIGSKGGIRFeGKQLDSLTQQQVRplrremqvvf 368
Cdd:PRK11147 325 --VNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLlKLMLGQLQADSGRIHC-GTKLEVAYFDQHR---------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 qdpfGSLSPRMCVSQIVGEGlrihKMGTEAE-QEQAIIAALKEVgLDPETRHRYP-HEFSGGQRQRIAIARaLVLKPA-L 445
Cdd:PRK11147 392 ----AELDPEKTVMDNLAEG----KQEVMVNgRPRHVLGYLQDF-LFHPKRAMTPvKALSGGERNRLLLAR-LFLKPSnL 461
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1834229548 446 ILLDEPTSALDrtvqRQVVELLRSLQSKYNLTYLFISHDLAVV 488
Cdd:PRK11147 462 LILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-221 |
2.27e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEfvVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLlnlkeKT 86
Cdd:TIGR01189 1 LAARNLACS--RGER--MLFEGLSFTLNAGEALQVTGPNGIGKT----TLLRILA-GLLRPDSGEVRWNGTPL-----AE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRIAMIFQEPmtSLNPLHSIEKQINEVLGIHKGligkvATKRTLELLEMVGIPEPEKRLKalpHELSGGQRQRV 166
Cdd:TIGR01189 67 QRDEPHENILYLGHLP--GLKPELSALENLHFWAAIHGG-----AQRTIEDALAAVGLTGFEDLPA---AQLSAGQQRRL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 167 MIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-222 |
2.29e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRDLAVEFVVGERC--QRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplarhpsgtieysgqnllnlkek 85
Cdd:COG2401 26 RVAIVLEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKS----TLLRLL------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 tIRHIRGNRIAMIFQEPMTSLNPLHSIEKQInevlgihkGLIGKVATKrtLELLEMVGIPEPEKrLKALPHELSGGQRQR 165
Cdd:COG2401 77 -AGALKGTPVAGCVDVPDNQFGREASLIDAI--------GRKGDFKDA--VELLNAVGLSDAVL-WLRRFKELSTGQKFR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVK 222
Cdd:COG2401 145 FRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-239 |
3.47e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.11 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEKTirhiRGnrIAMIFQE--- 101
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVA-GLERITSGEIWIGGRVVNELEPAD----RD--IAMVFQNyal 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 -P-MTSLN-----------PLHSIEKQINEVlgihkgligkvatKRTLELLEMvgipepekrLKALPHELSGGQRQRVMI 168
Cdd:PRK11650 88 yPhMSVREnmayglkirgmPKAEIEERVAEA-------------ARILELEPL---------LDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 169 AMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGcIVEQ 239
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG-VAEQ 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-256 |
3.66e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.51 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSvtahSILR-------LLPYPLArhpSGTIEYSGQNLlNLKEKTIRHIRgNRIAMI 98
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKS----TILRcfnrlndLIPGFRV---EGKVTFHGKNL-YAPDVDPVEVR-RRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 99 FQEPmtslNPL-HSIEKQIN---EVLGiHKGLIGKVATKrtlELLEMVGIPEPEKRLKALPHELSGGQRQRVMIAMALAN 174
Cdd:PRK14243 97 FQKP----NPFpKSIYDNIAygaRING-YKGDMDELVER---SLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 175 EPELLIADEPTTALD--VTVQLKILELLKELQarlgMALLLISHDLNLVKRIAHRVCVM---------QRGCIVEQASCE 243
Cdd:PRK14243 169 QPEVILMDEPCSALDpiSTLRIEELMHELKEQ----YTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTE 244
|
250
....*....|...
gi 1834229548 244 QLFRAPQHPYTRE 256
Cdd:PRK14243 245 KIFNSPQQQATRD 257
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
289-509 |
5.74e-14 |
|
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: 75.33 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 289 KGLLKKTVDYVKAV-DGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQQQvrpLRREMQVV 367
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQT---WRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 368 FQDPFgslsprmcvsqIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHE-----------FSGGQRQRIAIA 436
Cdd:TIGR01271 1298 PQKVF-----------IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLK-SVIEQFPDKldfvlvdggyvLSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 437 RALVLKPALILLDEPTSALDrTVQRQVVEllRSL-QSKYNLTYLFISHDLAVVkaLSHQLMVVKQGQVVEQGDA 509
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLD-PVTLQIIR--KTLkQSFSNCTVILSEHRVEAL--LECQQFLVIEGSSVKQYDS 1434
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
292-502 |
6.30e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.01 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIgskggirfegkqldsltqqqvrplrremqvvfqdp 371
Cdd:cd03221 6 LSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTL----LKLI----------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 fgslsprmcvsqivgeglrihkMGTEAEQEQAIIaalkevgLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:cd03221 47 ----------------------AGELEPDEGIVT-------WGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 452 TSALDRTVQRQVVELLRslqsKYNLTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:cd03221 98 TNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
25-247 |
8.80e-14 |
|
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: 74.01 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLlpYPLARhpsGTIEYSGQNLLNLKEKTIRHirgnRIAMIFQEP-- 102
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRL--YTPQH---GQVLVDGVDLAIADPAWLRR----QMGVVLQENvl 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 --------MTSLNPLHSIEKQIN--EVLGIHKGLIGKVATKRTlELLEMVGipepekrlkalphELSGGQRQRVMIAMAL 172
Cdd:TIGR01846 543 fsrsirdnIALCNPGAPFEHVIHaaKLAGAHDFISELPQGYNT-EVGEKGA-------------NLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 173 ANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVkRIAHRVCVMQRGCIVEQASCEQLFR 247
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTV-RACDRIIVLEKGQIAESGRHEELLA 680
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-497 |
8.89e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 33 IKRGETLALVGESGSGKSvTAHSILrllpyplarhpsgtieySGQNLLNL--------KEKTIRHIRGNRIAMIFQEpmt 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKT-TAVKIL-----------------SGELIPNLgdyeeepsWDEVLKRFRGTELQNYFKK--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 slnpLHSiekqiNEVLGIHK----GLIGKVATKRTLELLEMV---GI-PEPEKRLKALP------HELSGGQRQRVMIAM 170
Cdd:PRK13409 155 ----LYN-----GEIKVVHKpqyvDLIPKVFKGKVRELLKKVderGKlDEVVERLGLENildrdiSELSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 171 ALANEPELLIADEPTTALDVtVQlkilellkelqaRLGMA-----------LLLISHDLNLVKRIAHRVCVM--QRGC-- 235
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDI-RQ------------RLNVArlirelaegkyVLVVEHDLAVLDYLADNVHIAygEPGAyg 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 236 IVeqasceqlfrapQHPY-TRE--------LLAAE-----------PSGTPATNVVGPPMLTVEDlkvwfpikkglLKKT 295
Cdd:PRK13409 293 VV------------SKPKgVRVgineylkgYLPEEnmrirpepiefEERPPRDESERETLVEYPD-----------LTKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 296 VDyvkavdgiNFSLP-------QGQTLGIVGESGSGKSTLglaiLRLIGskGGIR-FEGKQLDSLT----QQQVRPlRRE 363
Cdd:PRK13409 350 LG--------DFSLEveggeiyEGEVIGIVGPNGIGKTTF----AKLLA--GVLKpDEGEVDPELKisykPQYIKP-DYD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 364 MQVvfQDPFGSLSPRMCVSQI---VGEGLRIHKMgteaeqeqaiiaalkevgLDpetrhRYPHEFSGGQRQRIAIARALV 440
Cdd:PRK13409 415 GTV--EDLLRSITDDLGSSYYkseIIKPLQLERL------------------LD-----KNVKDLSGGELQRVAIAACLS 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 441 LKPALILLDEPTSALDrtV-QR-QVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMV 497
Cdd:PRK13409 470 RDADLYLLDEPSAHLD--VeQRlAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-248 |
9.85e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 73.70 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKTIRHIrgnrIAMIFQEpmTSL- 106
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKS----TLARLL-FRFYDVTSGRILIDGQDIRDVTQASLRAA----IGIVPQD--TVLf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 107 -----------NPLHSiEKQINEVLG---IH---KGLIGKVATkrtlelleMVGipepEKRLKalpheLSGGQRQRVMIA 169
Cdd:COG5265 445 ndtiayniaygRPDAS-EEEVEAAARaaqIHdfiESLPDGYDT--------RVG----ERGLK-----LSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 170 MALANEPELLIADEPTTALD-VTVQLKILELLKELQARlgmALLLISHDLNLVKRiAHRVCVMQRGCIVEQASCEQLFRA 248
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDsRTERAIQAALREVARGR---TTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
304-495 |
1.10e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.83 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLDsltqQQVRPLRREMQVVFQDPF--GSLS 376
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTL----LRILAglsppLAGRVLLNGGPLD----FQRDSIARGLLYLGHAPGikTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 PRmcvsqivgEGLRI-HKMGTEAEQEQAiiaaLKEVGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:cd03231 90 VL--------ENLRFwHADHSDEQVEEA----LARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQL 495
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-249 |
1.16e-13 |
|
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: 70.65 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKekt 86
Cdd:cd03218 1 LRAENLSKRY--GKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV-----KPDSGKILLDGQDITKLP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 iRHIRGnRIAMIF--QEPmtSLNPLHSIEKQINEVLGIHKgLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQ 164
Cdd:cd03218 69 -MHKRA-RLGIGYlpQEA--SIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALD-VTVQLKILELLKELQarLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCE 243
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDpIAVQDIQKIIKILKD--RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
....*.
gi 1834229548 244 QLFRAP 249
Cdd:cd03218 219 EIAANE 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-234 |
1.37e-13 |
|
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: 70.19 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNlkektirhiRGNRIAMIFQEpmTS 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS----TLLNLIS-GLAQPTSGGVILEGKQITE---------PGPDRMVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LNPLHSIEKQIneVLGIHKGLIGKVATKRTL---ELLEMVGIPEP-EKRlkalPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:TIGR01184 65 LLPWLTVRENI--ALAVDRVLPDLSKSERRAiveEHIALVGLTEAaDKR----PGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 182 DEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
158-484 |
1.69e-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: 73.05 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDV-TVQLKILELlkelqARLGMALLLISHDLNLVKRIAHRVCVMQRG-C 235
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAeSVAWLERHL-----QEYPGTVVAVTHDRYFLDNVAGWILELDRGrG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 236 I----------------VEQASCEQLFRAP----------QHPYTR------------ELLAAEPSGTPATN-VVGPPML 276
Cdd:TIGR03719 237 IpwegnysswleqkqkrLEQEEKEESARQKtlkrelewvrQSPKGRqakskarlaryeELLSQEFQKRNETAeIYIPPGP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 277 TVEDLKVWFpikKGLLKKTVDYVkAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGSK-----GGIRF-EGKQLD 350
Cdd:TIGR03719 317 RLGDKVIEA---ENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTL----FRMITGQeqpdsGTIEIgETVKLA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 351 SLTQQqvrplrREmqvvfqdpfgSLSPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRhryPHEFSGGQR 430
Cdd:TIGR03719 389 YVDQS------RD----------ALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKK---VGQLSGGER 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 431 QRIAIARALVLKPALILLDEPTSALDrtvqrqvVELLRSLQS---KYNLTYLFISHD 484
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALEEallNFAGCAVVISHD 499
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-483 |
2.06e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 30 SFDIKRGETLALVGESGSGKSVtahsilrllpypLARHPSGT-IEYSGQnllnlkektiRHIRGNRIAMIFQEpmtSLNP 108
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA------------LARALAGElPLLSGE----------RQSQFSHITRLSFE---QLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 LHSIEKQIN--EVLGIHKGLIGKVA----------TKRTLELLEMVGI-PEPEKRLKalphELSGGQRQRVMIAMALANE 175
Cdd:PRK10938 78 LVSDEWQRNntDMLSPGEDDTGRTTaeiiqdevkdPARCEQLAQQFGItALLDRRFK----YLSTGETRKTLLCQALMSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 176 PELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVM---------QRGCIVEQASCEQLF 246
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLadctlaetgEREEILQQALVAQLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 247 RAPQHPYTRELLAAEPSGTPATNVVGPPMLtvedlkvwfpikkgLLKKTVDY--VKAVDGINFSLPQGQTLGIVGESGSG 324
Cdd:PRK10938 233 HSEQLEGVQLPEPDEPSARHALPANEPRIV--------------LNNGVVSYndRPILHNLSWQVNPGEHWQIVGPNGAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 325 KSTLgLAI------------LRLIGSKGG-----------IRFEGKQL--DSLTQQQVRplrremQVVFQDPFGSLSprm 379
Cdd:PRK10938 299 KSTL-LSLitgdhpqgysndLTLFGRRRGsgetiwdikkhIGYVSSSLhlDYRVSTSVR------NVILSGFFDSIG--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cVSQIVGEGLRIhkmgtEAEQEQAIIaalkevGLDPETRHRYPHEFSGGQrQRIA-IARALVLKPALILLDEPTSALD-- 456
Cdd:PRK10938 369 -IYQAVSDRQQK-----LAQQWLDIL------GIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDpl 435
|
490 500
....*....|....*....|....*...
gi 1834229548 457 -RTVQRQVVELLRSlQSKYNLtyLFISH 483
Cdd:PRK10938 436 nRQLVRRFVDVLIS-EGETQL--LFVSH 460
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
302-513 |
2.71e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGgirFEGKQLDSlTQQQVRPLRREMQVVFQDPFgsLSPRMCV 381
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTILAN-NRKPTKQILKRTGFVTQDDI--LYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 382 SQ--IVGEGLRIHKMGTEAEQEQAIIAALKEVGLDPETRHRYPHEF----SGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:PLN03211 158 REtlVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG---DAQSIF 513
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGkgsDAMAYF 298
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-228 |
3.64e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.29 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 12 LAVEFVVGERCQRVV-EGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKEKTIR-- 88
Cdd:cd03231 1 LEADELTCERDGRALfSGLSFTLAAGEALQVTGPNGSGKT----TLLRILA-GLSPPLAGRVLLNGGPLDFQRDSIARgl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 89 ----HIRGNRIAMIFQEPMTSLNPLHSiekqinevlgihkgligkvaTKRTLELLEMVGIPEPEKRLKalpHELSGGQRQ 164
Cdd:cd03231 76 lylgHAPGIKTTLSVLENLRFWHADHS--------------------DEQVEEALARVGLNGFEDRPV---AQLSAGQQR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 165 RVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRV 228
Cdd:cd03231 133 RVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-250 |
3.66e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARHpsgTIEYSGQNLLNLKEktiRHIRGnrIAMIFQEP 102
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI---IIDDEDISLLPLHA---RARRG--IGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mtSLNPLHSIEKQINEVLGIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:PRK10895 88 --SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 183 EPTTALDvTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:PRK10895 163 EPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-189 |
5.08e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 67.96 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFV--VGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLARHP-SGTIEYSGQNLlnlK 83
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS----TLLNALAGRRTGLGvSGEVLINGRPL---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRhirgNRIAMIFQEPMtslnpLHSiEKQINEVLGIHKGLIGkvatkrtlellemvgipepekrlkalpheLSGGQR 163
Cdd:cd03213 77 KRSFR----KIIGYVPQDDI-----LHP-TLTVRETLMFAAKLRG-----------------------------LSGGER 117
|
170 180
....*....|....*....|....*.
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALD 189
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-250 |
5.77e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.71 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYplarhpSGTIEYSGQNLLNLKEKTIRHIRgnriAMIFQEPMTSLN 107
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG------QGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 108 -PL-HSIEkqinevLGIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMAL------AN-EPEL 178
Cdd:COG4138 84 mPVfQYLA------LHQPAGASSEAVEQLLAQLAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 179 LIADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:COG4138 155 LLLDEPMNSLDVA-QQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
295-503 |
6.58e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 69.11 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 295 TVDYVKA----VDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQQQvrpLRREMQVVFQD 370
Cdd:cd03289 9 TAKYTEGgnavLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQK---WRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 371 PFgslsprmcvsqIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHE-----------FSGGQRQRIAIARAL 439
Cdd:cd03289 86 VF-----------IFSGTFRKNLDPYGKWSDEEIWKVAEEVGLK-SVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 440 VLKPALILLDEPTSALDRTVQRQVVELLRslQSKYNLTYLFISHDLAVVKAlSHQLMVVKQGQV 503
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
305-489 |
6.70e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG--IRFEGKQLDSLTQQQ-------------------------- 356
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhIVFKNEHTNDMTNEQdyqgdeeqnvgmknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 357 ------------------------VRPLRREMQVVFQDPfgslsprMCVSQIVGEGLrihKMGTEAEQEQAIIAALKEVG 412
Cdd:PTZ00265 1267 gedstvfknsgkilldgvdicdynLKDLRNLFSIVSQEP-------MLFNMSIYENI---KFGKEDATREDVKRACKFAA 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 413 LDpETRHRYPHEF-----------SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFI 481
Cdd:PTZ00265 1337 ID-EFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
....*...
gi 1834229548 482 SHDLAVVK 489
Cdd:PTZ00265 1416 AHRIASIK 1423
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-189 |
6.70e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILR----LLPYplarhpsgtieYSGq 77
Cdd:COG4178 358 SEDGALALEDLTLRTPDG---RPLLEDLSLSLKPGERLLITGPSGSGKS----TLLRaiagLWPY-----------GSG- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 78 nllnlkekTIRHIRGNRIAMIFQEPMTslnPLHSIEKQInevlgIHKGLIGKVATKRTLELLEMVGIPEPEKRL---KAL 154
Cdd:COG4178 419 --------RIARPAGARVLFLPQRPYL---PLGTLREAL-----LYPATAEAFSDAELREALEAVGLGHLAERLdeeADW 482
|
170 180 190
....*....|....*....|....*....|....*
gi 1834229548 155 PHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-189 |
7.80e-13 |
|
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: 68.07 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 22 CQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplarHPSGTIeySGQNLLNLKEKTiRHIRGNRIAMIFQ- 100
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV------EGGGTT--SGQILFNGQPRK-PDQFQKCVAYVRQd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 101 ----------EPMT----SLNPLHSIEKQINEVlgihkgligkVATKRTLEL-LEMVGipepEKRLKALphelSGGQRQR 165
Cdd:cd03234 90 dillpgltvrETLTytaiLRLPRKSSDAIRKKR----------VEDVLLRDLaLTRIG----GNLVKGI----SGGERRR 151
|
170 180
....*....|....*....|....
gi 1834229548 166 VMIAMALANEPELLIADEPTTALD 189
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
305-515 |
9.60e-13 |
|
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: 71.13 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS-KGGIRFEGKQLDSLTqqqVRPLRREMQVVFQDPF---GSLspRMC 380
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVlfsGSL--RMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 V---SQIVGEGLRihkMGTEAEQEQAIIAALKEvGLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:TIGR00957 1380 LdpfSQYSDEEVW---WALELAHLKTFVSALPD-KLDHECAEG-GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 458 TVQRQVVELLRSLQSkyNLTYLFISHDLAVVKALShQLMVVKQGQVVEQGDAQSIFAA 515
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-220 |
1.05e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVefVVGERCqrVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNLLNLKE 84
Cdd:PRK13539 1 MMLEGEDLAC--VRGGRV--LFSGLSFTLAAGEALVLTGPNGSGKT----TLLRLIA-GLLPPAAGTIKLDGGDIDDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KTIRHIRGNRIAMifqepmtslNPLHSIEKQIN---EVLGIHKGLIgkvatkrtLELLEMVGIPepekRLKALP-HELSG 160
Cdd:PRK13539 72 AEACHYLGHRNAM---------KPALTVAENLEfwaAFLGGEELDI--------AAALEAVGLA----PLAHLPfGYLSA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 161 GQRQRVMIA-MALANEPeLLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNL 220
Cdd:PRK13539 131 GQKRRVALArLLVSNRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGL 190
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
304-536 |
1.45e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKqldSLTQQQVRPLRREMQVVFQDPfgslsprMCVS 382
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVElEKGRIMIDDC---DVAKFGLTDLRRVLSIIPQSP-------VLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 QIVGEGLRIHKMGTEAEQEQAI-IAALKEV------GLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDADLWEALeRAHIKDVidrnpfGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 456 D-RT---VQRQVVELLRSlqskynLTYLFISHDLAVVKALShQLMVVKQGQVVEQGDAQSIFAAPQHPYTQQLLEAAflv 531
Cdd:PLN03232 1403 DvRTdslIQRTIREEFKS------CTMLVIAHRLNTIIDCD-KILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG--- 1472
|
....*
gi 1834229548 532 PATAQ 536
Cdd:PLN03232 1473 PANAQ 1477
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-249 |
1.60e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 36 GETLALVGESGSGKSvtahSILRLLpyplARH---PSGTIEYSGQNLLNLKEKTIrhirGNRIAMIFQ-----EPMTsln 107
Cdd:PRK10575 37 GKVTGLIGHNGSGKS----TLLKML----GRHqppSEGEILLDAQPLESWSSKAF----ARKVAYLPQqlpaaEGMT--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 108 plhsiekqINEVLGIHK-------GLIGKVATKRTLELLEMVGipepekrLKALPHEL----SGGQRQRVMIAMALANEP 176
Cdd:PRK10575 102 --------VRELVAIGRypwhgalGRFGAADREKVEEAISLVG-------LKPLAHRLvdslSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 177 ELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAP 249
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-248 |
1.66e-12 |
|
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: 69.89 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDlaVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLLNLKEKT 86
Cdd:TIGR03375 464 IEFRN--VSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKS----TLLKLL-LGLYQPTEGSVLLDGVDIRQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHirgnRIAMIFQEPMTSLNPLHSiekqiNEVLGihKGLIGKVatkRTLELLEMVGIPEPEKRLKA---LP-HE----L 158
Cdd:TIGR03375 537 LRR----NIGYVPQDPRLFYGTLRD-----NIALG--APYADDE---EILRAAELAGVTEFVRRHPDgldMQiGErgrsL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHD---LNLVKRIAhrvcVMQRGC 235
Cdd:TIGR03375 603 SGGQRQAVALARALLRDPPILLLDEPTSAMD--NRSEERFKDRLKRWLAGKTLVLVTHRtslLDLVDRII----VMDNGR 676
|
250
....*....|...
gi 1834229548 236 IVEQASCEQLFRA 248
Cdd:TIGR03375 677 IVADGPKDQVLEA 689
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
304-490 |
2.26e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.84 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLglaiLRLIG-----SKGGIRFEGKQLdsltqQQVRPLRREmQVVFQDPFGSLSPR 378
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTL----LRILAgllrpDSGEVRWNGTPL-----AEQRDEPHE-NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 379 MCVSqivgEGLRIHKMGTEAEQeQAIIAALKEVGLDPETrHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRT 458
Cdd:TIGR01189 88 LSAL----ENLHFWAAIHGGAQ-RTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|..
gi 1834229548 459 VQRQVVELLRSLQSKYNLTYLFISHDLAVVKA 490
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-248 |
2.31e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFVVGERCQR------------------VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplar 66
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKS----TLLKLI------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 67 hpSGTIE-YSGqnllnlkekTIRhIRGnRIAMIFqEPMTSLNPLHSIEKQInevlgIHKGLIGKVATKRTLELLEMV--- 142
Cdd:COG1134 73 --AGILEpTSG---------RVE-VNG-RVSALL-ELGAGFHPELTGRENI-----YLNGRLLGLSRKEIDEKFDEIvef 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 143 -GIPE----PEKRlkalpheLSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL------GMAL 211
Cdd:COG1134 134 aELGDfidqPVKT-------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ-------KKCLARIrelresGRTV 199
|
250 260 270
....*....|....*....|....*....|....*..
gi 1834229548 212 LLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRA 248
Cdd:COG1134 200 IFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-234 |
2.59e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDnLIEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLL 80
Cdd:PRK11300 1 MSQP-LLSVSGLMMRF--GGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY-----KPTGGTILLRGQHIE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKE---------KTIRHIRgnriamIFQEpMTSL-NPLHSIEKQINEvlGIHKGLIG--------KVATKRTLELLEMV 142
Cdd:PRK11300 71 GLPGhqiarmgvvRTFQHVR------LFRE-MTVIeNLLVAQHQQLKT--GLFSGLLKtpafrraeSEALDRAATWLERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 143 GIPEPEKRLKAlphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVK 222
Cdd:PRK11300 142 GLLEHANRQAG---NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVM 218
|
250
....*....|..
gi 1834229548 223 RIAHRVCVMQRG 234
Cdd:PRK11300 219 GISDRIYVVNQG 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-249 |
3.06e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.93 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 26 VEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNL-KEKTIRHIRGnriaMIFQEPMT 104
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL-----RPQKGKVLVSGIDTGDFsKLQGIRKLVG----IVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLnplhsIEKQINEVLGI---HKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIA 181
Cdd:PRK13644 89 QF-----VGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGL---EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 182 DEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVkRIAHRVCVMQRGCIVEQASCEQLFRAP 249
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-234 |
3.15e-12 |
|
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: 64.01 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplarhpSGTIE-YSGqnllnlkek 85
Cdd:cd03221 1 IELENLSKTY--GGKL--LLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI--------AGELEpDEG--------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 TIRHIRGNRIAMIFQepmtslnplhsiekqinevlgihkgligkvatkrtlellemvgipepekrlkalpheLSGGQRQR 165
Cdd:cd03221 56 IVTWGSTVKIGYFEQ---------------------------------------------------------LSGGEKMR 78
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 166 VMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
289-512 |
3.70e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.84 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 289 KGLLKKTVDyVKAVDGINFSLPQGQTLGIVGESGSGKSTlGLAILRLIGSKGGIRfeGKQLDSLTQQQvRPLRREM---Q 365
Cdd:NF000106 17 RGLVKHFGE-VKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRR--PWRF*TWCANR-RALRRTIg*hR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 366 VVFQDPFGSLSPRMCVsQIVGEGLRIHKMGTEAEQEQAiiaaLKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPAL 445
Cdd:NF000106 92 PVR*GRRESFSGRENL-YMIGR*LDLSRKDARARADEL----LERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-238 |
4.39e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYsGQN 78
Cdd:COG0488 313 KKVLELEGLSKSY--GDK--TLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLagelePD------SGTVKL-GET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 LlnlkektirhirgnRIAMIFQEpMTSLNPLHSIekqINEVLGIHKGliGKVATKRTLelLEMVGIPePEKRLKALpHEL 158
Cdd:COG0488 378 V--------------KIGYFDQH-QEELDPDKTV---LDELRDGAPG--GTEQEVRGY--LGRFLFS-GDDAFKPV-GVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDV-TVQLkilellkelqarLGMAL-------LLISHDLNLVKRIAHRVCV 230
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA------------LEEALddfpgtvLLVSHDRYFLDRVATRILE 501
|
....*...
gi 1834229548 231 MQRGCIVE 238
Cdd:COG0488 502 FEDGGVRE 509
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
299-509 |
5.16e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKST-LGLAILRLIGSKGGIRFEGKqlDSLTQQQVRPLRREMQVVfqdPFGSlsp 377
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTlLGTLCGDPRATSGRIVFDGK--DITDWQTAKIMREAVAIV---PEGR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGLRIHKMGTEAEQEQAIIAALKEvgLDP---ETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:PRK11614 90 RVFSRMTVEENLAMGGFFAERDQFQERIKWVYE--LFPrlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 455 LDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVV--EQGDA 509
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDA 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-258 |
6.52e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLLNLKEKTIrhirGNRIAMIFQEPMT 104
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT-PA----HGHVWLDGEHIQHYASKEV----ARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLNPlhSIEKQINEVLGIHKGLIgkvaTKRTLELLEMVGIPEPEKRLKALPHE----LSGGQRQRVMIAMALANEPELLI 180
Cdd:PRK10253 93 PGDI--TVQELVARGRYPHQPLF----TRWRKEDEEAVTKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 181 ADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQAsceqlfrAPQHPYTRELL 258
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELI 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
305-485 |
9.65e-12 |
|
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: 64.66 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGKQLDSLTQQQVRPLRR-----------------EMQV 366
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRNRysvayaaqkpwllnatvEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPFGSlsprmcvsqivgeglRIHKMGTEAEQEQAIIAALKeVGLDPETRHRYPHeFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03290 100 TFGSPFNK---------------QRYKAVTDACSLQPDIDLLP-FGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1834229548 447 LLDEPTSAL-----DRTVQRQVVELLRSLQSkynlTYLFISHDL 485
Cdd:cd03290 163 FLDDPFSALdihlsDHLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-236 |
1.05e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGERcQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLlpYPLArhpsgtieYSGQNLLNLK 83
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPH-IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA--YPGR--------WEGEIFIDGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRH----IRgNRIAMIFQE-PMTSLNPLHSIEKQIN-EVLG--IHKGLIGKVATKRTL--ELLEM-VGIPEPEKRLK 152
Cdd:PRK13549 326 PVKIRNpqqaIA-QGIAMVPEDrKRDGIVPVMGVGKNITlAALDrfTGGSRIDDAAELKTIleSIQRLkVKTASPELAIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 153 alphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:PRK13549 405 ----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
....
gi 1834229548 233 RGCI 236
Cdd:PRK13549 480 EGKL 483
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
305-500 |
1.10e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIgskggirfegkQLDSLTQQQVRPLRREM--QVVFQDPFGSLSprmcvs 382
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLV-----------APDEGVIKRNGKLRIGYvpQKLYLDTTLPLT------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 qiVGEGLRIHKmgteAEQEQAIIAALKEVglDPETRHRYP-HEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQR 461
Cdd:PRK09544 86 --VNRFLRLRP----GTKKEDILPALKRV--QAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1834229548 462 QVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQ 500
Cdd:PRK09544 158 ALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-245 |
1.45e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEFvvgeRCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLA--RHPSGTIEYSGqNLLNLK 83
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKS----TLLRHLSGLITgdKSAGSHIELLG-RTVQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 EKTIRHIRGNR--IAMIFQEpMTSLNPLHSIEKQINEVLGIHK------GLIGKVATKRTLELLEMVGIPE-PEKRLKAL 154
Cdd:PRK09984 75 GRLARDIRKSRanTGYIFQQ-FNLVNRLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALTRVGMVHfAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 155 phelSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:PRK09984 154 ----SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
250
....*....|.
gi 1834229548 235 CIVEQASCEQL 245
Cdd:PRK09984 230 HVFYDGSSQQF 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
273-456 |
1.72e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.28 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFPikkgllKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDS 351
Cdd:COG1137 1 MMTLEAENLVKSYG------KRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGrIFLDGEDITH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 352 LtqqqvrPL----RREMQVVFQDP--FGSLSPR---MCVsqivgegLRIHKMgTEAEQEQAIIAALKEVGLDpETRHRYP 422
Cdd:COG1137 70 L------PMhkraRLGIGYLPQEAsiFRKLTVEdniLAV-------LELRKL-SKKEREERLEELLEEFGIT-HLRKSKA 134
|
170 180 190
....*....|....*....|....*....|....
gi 1834229548 423 HEFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-189 |
1.72e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.28 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLkekT 86
Cdd:COG1137 4 LEAENLVKSY--GKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV-----KPDSGRIFLDGEDITHL---P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IrHIRGNR-IAMIFQEPmtslnplhSI------EKQINEVLGIHKgLIGKVATKRTLELLEMVGIpepEKRLKALPHELS 159
Cdd:COG1137 72 M-HKRARLgIGYLPQEA--------SIfrkltvEDNILAVLELRK-LSKKEREERLEELLEEFGI---THLRKSKAYSLS 138
|
170 180 190
....*....|....*....|....*....|
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
304-502 |
1.87e-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: 63.26 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLGLAIL----RLIGS---------------------KGGIRFeGKQLDSLTQQQVR 358
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLgeleKLSGSvsvpgsiayvsqepwiqngtiRENILF-GKPFDEERYEKVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 359 P---LRREMQVVfqdPFGSLSprmcvsqIVGEglrihkmgteaeqeqaiiaalKEVGLdpetrhryphefSGGQRQRIAI 435
Cdd:cd03250 102 KacaLEPDLEIL---PDGDLT-------EIGE---------------------KGINL------------SGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 436 ARALVLKPALILLDEPTSALDRTVQRQVVE-LLRSLQSKyNLTYLFISHDLAVVKAlSHQLMVVKQGQ 502
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-246 |
1.96e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLlNLKEKTIRHIRgNRIAMIFQEP 102
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLL-----RPQKGAVLWQGKPL-DYSKRGLLALR-QQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 MTSLNpLHSIEKQIN---EVLGIHKGLIgkvaTKRTLELLEMVGipepEKRLKALPHE-LSGGQRQRVMIAMALANEPEL 178
Cdd:PRK13638 87 EQQIF-YTDIDSDIAfslRNLGVPEAEI----TRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 179 LIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF 246
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
300-517 |
2.10e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 300 KAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQQQVRPlRREMQVVFQDPfgSLSPRM 379
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRGIGYLPQEA--SIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 CVSQIVGEGLRIHKMGTEAEQEQAIIAALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTV 459
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 460 Q---RQVVELLRSlqskYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFAAPQ 517
Cdd:PRK10895 173 VidiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
294-512 |
3.86e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 294 KTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI--GSKGGIRFEGKQLDSLTQQQVRPLrrEMQVVFQDp 371
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTL-MKVLSGIhePTKGTITINNINYNKLDHKLAAQL--GIGIIYQE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 fgslsprmcVSQI----VGEGLRIHKMGTE----------AEQEQAIIAALKEVGL--DPETRhryPHEFSGGQRQRIAI 435
Cdd:PRK09700 89 ---------LSVIdeltVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLkvDLDEK---VANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 436 ARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
305-489 |
5.59e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQldSLTQQQVRPLRREMQVVFQDPF----------- 372
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIINDSH--NLKDINLKWWRSKIGVVSQDPLlfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 -------------------------GSLSPRMCVSQIVGEGLRIHKMGT-----EAEQEQAIIAALKEVGLdpeTRHRYP 422
Cdd:PTZ00265 482 yslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAGDLNDMSNTTDsneliEMRKNYQTIKDSEVVDV---SKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 423 HEF-------------------SGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISH 483
Cdd:PTZ00265 559 HDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
....*.
gi 1834229548 484 DLAVVK 489
Cdd:PTZ00265 639 RLSTIR 644
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-236 |
6.59e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 64.68 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 12 LAVEFVVG---ERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKTIr 88
Cdd:TIGR01842 317 LSVENVTIvppGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT-----SGSVRLDGADLKQWDRETF- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 89 hirGNRIAMIFQEpmtslnplhsIEkqinevlgIHKGLIGKvatkrtlELLEMVGIPEPEKRLKALP----HE------- 157
Cdd:TIGR01842 391 ---GKHIGYLPQD----------VE--------LFPGTVAE-------NIARFGENADPEKIIEAAKlagvHElilrlpd 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 ------------LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKrIA 225
Cdd:TIGR01842 443 gydtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLG-CV 520
|
250
....*....|.
gi 1834229548 226 HRVCVMQRGCI 236
Cdd:TIGR01842 521 DKILVLQDGRI 531
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-190 |
8.74e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 6 LIEVRDLAVEfvVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNllnlkek 85
Cdd:PRK13538 1 MLEARNLACE--RDER--ILFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILA-GLARPDAGEVLWQGEP------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 86 tIRHIRGnriamIFQEPMTSLNPLHSIEKQIN--EVLGIHKGLIGKVATKRTLELLEMVGIpepEKRLKALPHELSGGQR 163
Cdd:PRK13538 65 -IRRQRD-----EYHQDLLYLGHQPGIKTELTalENLRFYQRLHGPGDDEALWEALAQVGL---AGFEDVPVRQLSAGQQ 135
|
170 180
....*....|....*....|....*..
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDV 190
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-234 |
1.03e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFVVGERCQRVvEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplARHpSGTIeYSGQNLLNLK 83
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---GKF-EGNV-FINGKPVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 84 --EKTIRHirgnRIAMIfqepmtslnPLHSIEKQINEVLGIHKGLIGKVATK-----RTLELLEMVGIPEPEKRLKA--- 153
Cdd:TIGR02633 329 npAQAIRA----GIAMV---------PEDRKRHGIVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVkta 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 154 ---LP-HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVC 229
Cdd:TIGR02633 396 spfLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVL 474
|
....*
gi 1834229548 230 VMQRG 234
Cdd:TIGR02633 475 VIGEG 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-497 |
1.29e-10 |
|
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: 64.04 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 34 KRGETLALVGESGSGKSvTAHSILrllpyplarhpsgtieySGQ---NLLNL-----KEKTIRHIRGNRIamifQEPMTS 105
Cdd:COG1245 97 KKGKVTGILGPNGIGKS-TALKIL-----------------SGElkpNLGDYdeepsWDEVLKRFRGTEL----QDYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 LnplhsIEKQINEVlgiHK----GLIGKVATKRTLELLEMVG----IPEPEKRLKaLPH-------ELSGGQRQRVMIAM 170
Cdd:COG1245 155 L-----ANGEIKVA---HKpqyvDLIPKVFKGTVRELLEKVDergkLDELAEKLG-LENildrdisELSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 171 ALANEPELLIADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVM--QRGC--IVeqasceqlf 246
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIY-QRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygEPGVygVV--------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 247 rapQHPY-TRE--------LLAAE-----------PSGTPATNVVGPPMLTVEDLKVWFPikkgllkktvdyvkavdgiN 306
Cdd:COG1245 296 ---SKPKsVRVginqyldgYLPEEnvrirdepiefEVHAPRREKEEETLVEYPDLTKSYG-------------------G 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 307 FSLP-------QGQTLGIVGESGSGKSTLglaiLRLIGskGGIRFEGKQLD-----SLTQQQVRPlRREMQV------VF 368
Cdd:COG1245 354 FSLEveggeirEGEVLGIVGPNGIGKTTF----AKILA--GVLKPDEGEVDedlkiSYKPQYISP-DYDGTVeeflrsAN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 QDPFGSlspRMCVSQIVgEGLRIHKMgteaeqeqaiiaalkevgLDpetrhRYPHEFSGGQRQRIAIARALvLKPA-LIL 447
Cdd:COG1245 427 TDDFGS---SYYKTEII-KPLGLEKL------------------LD-----KNVKDLSGGELQRVAIAACL-SRDAdLYL 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 448 LDEPTSALDrtV-QR-QVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMV 497
Cdd:COG1245 479 LDEPSAHLD--VeQRlAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-248 |
1.58e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.58 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSVTAHsiLRLLPYPLArhpSGTIEYSGQNLLNLKEKT 86
Cdd:PRK10790 341 IDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLAS--LLMGYYPLT---EGEIRLDGRPLSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRhirgNRIAMIFQEPMTSLNPLHSiekqiNEVLGIHkglIGKVATKRTLE---LLEMV-GIPEP-EKRLKALPHELSGG 161
Cdd:PRK10790 413 LR----QGVAMVQQDPVVLADTFLA-----NVTLGRD---ISEEQVWQALEtvqLAELArSLPDGlYTPLGEQGNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 162 QRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellkelQArLGMALLLISHDLNLVKrIAHR---------VCVMQ 232
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTE----------QA-IQQALAAVREHTTLVV-IAHRlstiveadtILVLH 548
|
250
....*....|....*.
gi 1834229548 233 RGCIVEQASCEQLFRA 248
Cdd:PRK10790 549 RGQAVEQGTHQQLLAA 564
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
299-507 |
2.37e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGG-IRFEGKQLDSLTQQQVRPLrrEMQVVFQDPFgsLSP 377
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtLEIGGNPCARLTPAKAHQL--GIYLVPQEPL--LFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIVGEGLRIHkmgteAEQEQAIIAALKEVGLdpetrHRYPHEFSG----GQRQRIAIARALVLKPALILLDEPTS 453
Cdd:PRK15439 100 NLSVKENILFGLPKR-----QASMQKMKQLLAALGC-----QLDLDSSAGslevADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 454 ALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-243 |
2.79e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEfvVGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpyplARHPS-----GTIEYS 75
Cdd:CHL00131 2 NKNKPILEIKNLHAS--VNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--------AGHPAykileGDILFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 76 GQNLLNLkEKTIRHIRGnrIAMIFQEPMtslnplhsiekqinEVLGIHKGLIGKVA--TKRT---------LELLEMvgI 144
Cdd:CHL00131 70 GESILDL-EPEERAHLG--IFLAFQYPI--------------EIPGVSNADFLRLAynSKRKfqglpeldpLEFLEI--I 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 145 PEPEKRLKALPHEL--------SGGQRQRVMI-AMALAnEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLIS 215
Cdd:CHL00131 131 NEKLKLVGMDPSFLsrnvnegfSGGEKKRNEIlQMALL-DSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILIT 208
|
250 260
....*....|....*....|....*....
gi 1834229548 216 HDLNLVKRIA-HRVCVMQRGCIVEQASCE 243
Cdd:CHL00131 209 HYQRLLDYIKpDYVHVMQNGKIIKTGDAE 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
298-489 |
3.80e-10 |
|
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: 58.87 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 298 YVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFegkqldsltqqqvRPLRREMQVVFQDpfgslsp 377
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISF-------------LPKFSRNKLIFID------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 rmcvsqivgeglrihkmgteaeQEQAIIaalkEVGLDPETRHRYPHEFSGGQRQRIAIARALV--LKPALILLDEPTSAL 455
Cdd:cd03238 67 ----------------------QLQFLI----DVGLGYLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....
gi 1834229548 456 DRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVK 489
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLS 153
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
302-532 |
3.96e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTL---------GLAILRLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPF 372
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 GslsprMCVSQIVGEGLRIH--KMGTEAEQEQAII-AALKEVGLDPETRhRYPHEFSGGQRQRIAIARAL---------V 440
Cdd:PRK13547 97 A-----FSAREIVLLGRYPHarRAGALTHRDGEIAwQALALAGATALVG-RDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 441 LKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGdaqsifaAPQHPY 520
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG-------APADVL 243
|
250
....*....|..
gi 1834229548 521 TQQLLEAAFLVP 532
Cdd:PRK13547 244 TPAHIARCYGFA 255
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
294-505 |
3.97e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 294 KTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLI---GS-KGGIRFEGKQldsltqQQVRPLR----REMQ 365
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVyphGSyEGEILFDGEV------CRFKDIRdseaLGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 366 VVFQDPfgSLSPRMCVSQIVGEGLRIHKMG----TEAEQEQAiiAALKEVGLD--PETRhryPHEFSGGQRQRIAIARAL 439
Cdd:NF040905 82 IIHQEL--ALIPYLSIAENIFLGNERAKRGvidwNETNRRAR--ELLAKVGLDesPDTL---VTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 440 VLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVE 505
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
305-532 |
4.56e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQ-----------QQVRPLrremqvvfqdpfg 373
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAaelarhraylsQQQTPP------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 slsPRMCVSQIvgegLRIHkmGTEAEQEQAIIAALKEV----GLDPETrHRYPHEFSGGQRQRIAIARAL-----VLKPA 444
Cdd:PRK03695 82 ---FAMPVFQY----LTLH--QPDKTRTEAVASALNEVaealGLDDKL-GRSVNQLSGGEWQRVRLAAVVlqvwpDINPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 445 --LILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFaapqhpyTQ 522
Cdd:PRK03695 152 gqLLLLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL-------TP 223
|
250
....*....|
gi 1834229548 523 QLLEAAFLVP 532
Cdd:PRK03695 224 ENLAQVFGVN 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
303-470 |
5.22e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGS-----KGGIRFEGkqldsltqqqvRPLRREMQVVFQDPF----- 372
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSL----LRILAGlarpdAGEVLWQG-----------EPIRRQRDEYHQDLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 ----GSLSPRmcvsqivgEGLRI-HKMGTEAEQEqAIIAALKEVGLdpETRHRYP-HEFSGGQRQRIAIARALVLKPALI 446
Cdd:PRK13538 83 pgikTELTAL--------ENLRFyQRLHGPGDDE-ALWEALAQVGL--AGFEDVPvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180
....*....|....*....|....
gi 1834229548 447 LLDEPTSALDrtvqRQVVELLRSL 470
Cdd:PRK13538 152 ILDEPFTAID----KQGVARLEAL 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-250 |
5.23e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIeYSGQNLLNLKEKTIRHIrgnriAMIFQEpmTSLNP 108
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKS----TLLRMIA-GLEDITSGDL-FIGEKRMNDVPPAERGV-----GMVFQS--YALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 LHSIEKqiNEVLGIHKGLIGKVATKRTLEllEMVGIPEPEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTAL 188
Cdd:PRK11000 89 HLSVAE--NMSFGLKLAGAKKEEINQRVN--QVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 189 DVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ 250
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
5.53e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAvefvvgERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpYPLARHPSGTIEYSGQNL- 79
Cdd:PRK09700 260 LAHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDIs 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 ----LNLKEKTIRHIRGNRIAMIFQePMTSLNPLHSIEKQINevLGIHKGLIGKVATKRTLEllemvgIPEPEKRLKALP 155
Cdd:PRK09700 329 prspLDAVKKGMAYITESRRDNGFF-PNFSIAQNMAISRSLK--DGGYKGAMGLFHEVDEQR------TAENQRELLALK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 --------HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHR 227
Cdd:PRK09700 400 chsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDR 478
|
250
....*....|.
gi 1834229548 228 VCVMQRGCIVE 238
Cdd:PRK09700 479 IAVFCEGRLTQ 489
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-245 |
5.84e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.90 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFvvGErcQRVVEGVSFDIKRGETLALVGESGSGKSVTAhsilrlLPYPLARHPSGTIEYSGQNLLNLKE 84
Cdd:NF000106 12 NAVEVRGLVKHF--GE--VKAVDGVDLDVREGTVLGVLGP*GAA**RGA------LPAHV*GPDAGRRPWRF*TWCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 85 KTIRHIRGNR-IAMIFQEPMTSLNPLHSIEKQINevlgihkgLIGKVATKRTLELLEMVGIPEPEKRLKAlphELSGGQR 163
Cdd:NF000106 82 ALRRTIG*HRpVR*GRRESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAA---KYSGGMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 164 QRVMIAMALANEPELLIADEPTTALDVTVQlKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCE 243
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTR-NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
..
gi 1834229548 244 QL 245
Cdd:NF000106 230 EL 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
289-512 |
6.49e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 289 KGLLKKTVD--YVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL-IGSKGGIRFEGKQldsltqqqvrplrrEMQ 365
Cdd:PRK13545 25 KDLFFRSKDgeYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKGSA--------------ALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 366 VVFQDPFGSLSPrmcVSQIVGEGLRihkMGTEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPAL 445
Cdd:PRK13545 91 AISSGLNGQLTG---IENIELKGLM---MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSI 512
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
292-517 |
7.46e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.34 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTV-DYVKAVDGINFSlpQGQTLGIVGESGSGKSTLglaiLRLIGskGGIR-FEGKQLDSLTQQQVRPlrREMQVVFQ 369
Cdd:cd03237 6 MKKTLgEFTLEVEGGSIS--ESEVIGILGPNGIGKTTF----IKMLA--GVLKpDEGDIEIELDTVSYKP--QYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 370 dpfgslsprMCVSQIVGEGLRIHkmGTEAEQEQAIIAALK-EVGLDPETRhryphEFSGGQRQRIAIArALVLKPA-LIL 447
Cdd:cd03237 76 ---------GTVRDLLSSITKDF--YTHPYFKTEIAKPLQiEQILDREVP-----ELSGGELQRVAIA-ACLSKDAdIYL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 448 LDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVkQGQVVEQGDAqsifAAPQ 517
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVA----NPPQ 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-248 |
1.00e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEV---RDLA-----VEFVVGERCQRV-------VEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLA 65
Cdd:PRK10762 228 LTEDSLIEMmvgRKLEdqyprLDKAPGEVRLKVdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALP 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 66 RHpSGTIEYSGQNLLNLKEKT-----IRHIRGNR------IAMIFQEPM--TSLNPLHSIEKQINevlgiHKGLIGKVAt 132
Cdd:PRK10762 304 RT-SGYVTLDGHEVVTRSPQDglangIVYISEDRkrdglvLGMSVKENMslTALRYFSRAGGSLK-----HADEQQAVS- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 133 krtlELLEMVGI--PEPEKRLKalphELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMA 210
Cdd:PRK10762 377 ----DFIRLFNIktPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLS 447
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1834229548 211 LLLISHDLNLVKRIAHRVCVMQRGCI-----VEQASCEQLFRA 248
Cdd:PRK10762 448 IILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMAA 490
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
403-483 |
1.09e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 403 AIIAALKevgLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDrtvqRQVVELLRSLQSKYNLTYLFIS 482
Cdd:PLN03073 326 SILAGLS---FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVS 398
|
.
gi 1834229548 483 H 483
Cdd:PLN03073 399 H 399
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
304-505 |
1.24e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GINFSLPQGQTLGIVGESGSGKSTLGLAILRLIG-SKGGIRFEGKQLDSLTqqqVRPLRREMQVVFQDPfgslsprMCVS 382
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVElERGRILIDGCDISKFG---LMDLRKVLGIIPQAP-------VLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 383 QIVGEGLRIHKMGTEAEQEQAIIAA-LKEV------GLDPETRHRyPHEFSGGQRQRIAIARALVLKPALILLDEPTSAL 455
Cdd:PLN03130 1327 GTVRFNLDPFNEHNDADLWESLERAhLKDVirrnslGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 456 D-RT---VQRQVVELLRSlqskynLTYLFISHDLAVVKAlSHQLMVVKQGQVVE 505
Cdd:PLN03130 1406 DvRTdalIQKTIREEFKS------CTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
303-504 |
1.42e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 303 DGINFSLPQGQTLGIVGESGSGKSTLgLAIL--RLIGSKGGIRFEGKQLDSLTQQQvrPLRREMQVVFQDPFGSLsprmc 380
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTL-MKILngEVLLDDGRIIYEQDLIVARLQQD--PPRNVEGTVYDFVAEGI----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 vsQIVGEGLRI-----HKMGTEAE----------QEQ-----------AIIAALKEVGLDPETRHRyphEFSGGQRQRIA 434
Cdd:PRK11147 92 --EEQAEYLKRyhdisHLVETDPSeknlnelaklQEQldhhnlwqlenRINEVLAQLGLDPDAALS---SLSGGWLRKAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 435 IARALVLKPALILLDEPTSALDRTvqrqVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
299-485 |
1.54e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLIGSK--GGIRFEGKQ-----------------------LDSLT 353
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTM-MKVLTGIYTRdaGSILYLGKEvtfngpkssqeagigiihqelnlIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 354 QQQVRPLRREmqvvFQDPFGSLSPRmcvsqivgeglrihKMGTEAEqeqaiiAALKEVGLdPETRHRYPHEFSGGQRQRI 433
Cdd:PRK10762 96 IAENIFLGRE----FVNRFGRIDWK--------------KMYAEAD------KLLARLNL-RFSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 434 AIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDL 485
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRL 201
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
138-253 |
1.61e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 138 LLEMVGIpepEKRLKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHD 217
Cdd:PRK11144 112 IVALLGI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHS 188
|
90 100 110
....*....|....*....|....*....|....*..
gi 1834229548 218 LNLVKRIAHRVCVMQRGCIVEQASCEQLFRAPQ-HPY 253
Cdd:PRK11144 189 LDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-503 |
1.75e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLlnlKEKTIRHIRGNRIAMIFQEpmtsLNP 108
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKS----TLLKCL-FGIYQKDSGSILFQGKEI---DFKSSKEALENGISMVHQE----LNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 LHSIEKQINEVLGIH--KGLI--GKVATKRTLELLEMVGIP-EPEKRLKalphELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:PRK10982 85 VLQRSVMDNMWLGRYptKGMFvdQDKMYRDTKAIFDELDIDiDPRAKVA----TLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 184 PTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGciveqasceqlfrapQHPYTRELlaaepS 263
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG---------------QWIATQPL-----A 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 264 GTPATNVVGppMLTVEDLKVWFPIKKGLLKKTVDYVK--------AVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRL 335
Cdd:PRK10982 220 GLTMDKIIA--MMVGRSLTQRFPDKENKPGEVILEVRnltslrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 336 IGSKGG-IRFEGKQLDSLTQQQ--------VRPLRREMQVV----------------FQDPFGSLSPRMCVS--QIVgeg 388
Cdd:PRK10982 298 REKSAGtITLHGKKINNHNANEainhgfalVTEERRSTGIYayldigfnslisnirnYKNKVGLLDNSRMKSdtQWV--- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 389 lrIHKMGTEAEQEQAIIAALkevgldpetrhryphefSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLR 468
Cdd:PRK10982 375 --IDSMRVKTPGHRTQIGSL-----------------SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIA 435
|
490 500 510
....*....|....*....|....*....|....*
gi 1834229548 469 SLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:PRK10982 436 ELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-248 |
1.86e-09 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 60.15 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyPLarhpSGTIEYSGQNLlnlkektirhirgnriamifqepmT 104
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-PT----AGSVRLDGADL------------------------S 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLNPlhsiekqinEVLGIHkglIGKVAtkRTLELLE--------MVGIPEPEKRLKA------------LP--------- 155
Cdd:COG4618 398 QWDR---------EELGRH---IGYLP--QDVELFDgtiaeniaRFGDADPEKVVAAaklagvhemilrLPdgydtrige 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 --HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVkRIAHRVCVMQR 233
Cdd:COG4618 464 ggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRD 541
|
250
....*....|....*
gi 1834229548 234 GCIVEQASCEQLFRA 248
Cdd:COG4618 542 GRVQAFGPRDEVLAR 556
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
273-470 |
1.88e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 273 PPMLTVEDLKVWFPIKKG---LLKKTVDYVKAvdginfslpqGQTLGIVGESGSGKSTL--GLAILRLIGS-KGGIRFEG 346
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGkrqLLNNISGYVKP----------GTLTALMGESGAGKTTLldVLAGRKTAGViTGEILING 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 347 KQLDSltqqqvrPLRREMQVVFQDPFgsLSPrmcvSQIVGEGLRIHkmgteaeqeqaiiAALKevGLDPEtrhryphefs 426
Cdd:cd03232 71 RPLDK-------NFQRSTGYVEQQDV--HSP----NLTVREALRFS-------------ALLR--GLSVE---------- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1834229548 427 ggQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSL 470
Cdd:cd03232 113 --QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-189 |
1.98e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvTAHSILrllpypLARHPSGTiEYSGQNLLNLKEKTIRHIRgNRIAMIFQEPM---- 103
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKT-TLMNAL------AFRSPKGV-KGSGSVLLNGMPIDAKEMR-AISAYVQQDDLfipt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 -TSLNPLhsiekQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHE---LSGGQRQRVMIAMALANEPELL 179
Cdd:TIGR00955 114 lTVREHL-----MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLL 188
|
170
....*....|
gi 1834229548 180 IADEPTTALD 189
Cdd:TIGR00955 189 FCDEPTSGLD 198
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
311-484 |
2.63e-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: 55.84 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 311 QGQTLGIVGESGSGKSTLGLAILRLIGSKGGirfegkqldsltqqqvrplrremQVVFQDPfgslsprmcvsqivgeglr 390
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-----------------------GVIYIDG------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 391 ihkmgteaeqeqAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRS- 469
Cdd:smart00382 39 ------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELr 106
|
170
....*....|....*....
gi 1834229548 470 ----LQSKYNLTYLFISHD 484
Cdd:smart00382 107 llllLKSEKNLTVILTTND 125
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
305-528 |
9.12e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIG--SKGGIRFEGK-----QLDSLTQQQVRPlrremQVVFQDPFGSlsp 377
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprSDASVVIRGTvayvpQVSWIFNATVRD-----NILFGSPFDP--- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 rmcvsqivgeglrihkmgteAEQEQAI-IAALK-EVGLDPETRHRYPHE----FSGGQRQRIAIARALVLKPALILLDEP 451
Cdd:PLN03130 708 --------------------ERYERAIdVTALQhDLDLLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 452 TSALDRTVQRQVVE--LLRSLQSKynlTYLFISHDLAVvkaLSH--QLMVVKQGQVVEQGDAQSIFAapQHPYTQQLLEA 527
Cdd:PLN03130 768 LSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHF---LSQvdRIILVHEGMIKEEGTYEELSN--NGPLFQKLMEN 839
|
.
gi 1834229548 528 A 528
Cdd:PLN03130 840 A 840
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
305-507 |
1.06e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.08 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL------RLIGSKG----GIRFEG-KQLDSLTqqqvrplrremqVVFQDPFG 373
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarRLHLKKEqpgnHDRIEGlEHIDKVI------------VIDQSPIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 374 SlSPRMC---------------------------VSQIVGEGLRIH---KMGTEAEQE--------QAIIAALKEVGLDP 415
Cdd:cd03271 82 R-TPRSNpatytgvfdeirelfcevckgkrynreTLEVRYKGKSIAdvlDMTVEEALEffenipkiARKLQTLCDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 416 ETRHRYPHEFSGGQRQRIAIARALvLKPA----LILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKAL 491
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKCA 238
|
250 260
....*....|....*....|.
gi 1834229548 492 SHQLMV-----VKQGQVVEQG 507
Cdd:cd03271 239 DWIIDLgpeggDGGGQVVASG 259
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
312-484 |
1.28e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 312 GQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGKQLDSLTQQQVRPLRR---EMQVVFQDPFGSLSPRMCVSQIVG 386
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTL-LALLKneISADGGSYTFPGNWQLAWVNQETPALPQpalEYVIDGDREYRQLEAQLHDANERN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 387 EGlriHKMGTEAEQEQAIIA---------ALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDR 457
Cdd:PRK10636 106 DG---HAIATIHGKLDAIDAwtirsraasLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180
....*....|....*....|....*..
gi 1834229548 458 TVqrqVVELLRSLQSkYNLTYLFISHD 484
Cdd:PRK10636 183 DA---VIWLEKWLKS-YQGTLILISHD 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
292-484 |
1.49e-08 |
|
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: 57.25 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAV-DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGskgGI--RFEGKqldsltqqqVRPlRREMQVVF 368
Cdd:TIGR03719 10 VSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMA---GVdkDFNGE---------ARP-QPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 369 --QDPfgSLSPRMCVSQIVGEGLR----------------------IHKMGTEAEQEQAIIAALK--------EVGLDPe 416
Cdd:TIGR03719 73 lpQEP--QLDPTKTVRENVEEGVAeikdaldrfneisakyaepdadFDKLAAEQAELQEIIDAADawdldsqlEIAMDA- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 417 trHRYP------HEFSGGQRQRIAIARALVLKPALILLDEPTSALDrtvQRQVVELLRSLQsKYNLTYLFISHD 484
Cdd:TIGR03719 150 --LRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQ-EYPGTVVAVTHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
305-465 |
1.56e-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: 57.61 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQ 383
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMgELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 384 IVGEglriHKMGTEAEQEQAIiaaLKEVGLdpetrhryphEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQV 463
Cdd:TIGR01271 525 CQLE----EDIALFPEKDKTV---LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
..
gi 1834229548 464 VE 465
Cdd:TIGR01271 588 FE 589
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-234 |
1.67e-08 |
|
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: 54.78 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPSGTIEYSG------QN--LLNlkektiRHIRGNria 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-----KLSGSVSVPGsiayvsQEpwIQN------GTIREN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 97 MIFQEPMtslnplhsIEKQINEVLgihkgligKV-ATKRTLELLE-----MVGipepEKRLKalpheLSGGQRQRVMIAM 170
Cdd:cd03250 86 ILFGKPF--------DEERYEKVI--------KAcALEPDLEILPdgdltEIG----EKGIN-----LSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 171 ALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRG 234
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
302-483 |
1.83e-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: 57.07 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGS----KGGIRFegkqldsltqqqvRPLRREMQVVFQDPFGSLsp 377
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSL----FRILGElwpvYGGRLT-------------KPAKGKLFYVPQRPYMTL-- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 378 RMCVSQIvgeglrIHKMGTEAEQ-----EQAIIAALKEVGLDP--------ETRHRYPHEFSGGQRQRIAIARALVLKPA 444
Cdd:TIGR00954 529 GTLRDQI------IYPDSSEDMKrrglsDKDLEQILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 1834229548 445 LILLDEPTSALDRTVQRQVVELLRslqsKYNLTYLFISH 483
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
301-507 |
1.96e-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: 57.33 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTLgLAILR--LIGSKGGIRFEGKQLDSltqqQVRPLRREMQVVFQDP--FGSLS 376
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTT-LSILTglLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQHNilFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcvsqiVGEGLRIHKMGTEAEQEQAII---AALKEVGLDpETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTS 453
Cdd:TIGR01257 1020 --------VAEHILFYAQLKGRSWEEAQLemeAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 454 ALDRTVQRQVVELLrsLQSKYNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQG 507
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
302-484 |
1.96e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGSK-----GGIRF-EGKQLDSLTQQqvrplrREmqvvfqdpfgSL 375
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTL----FKMITGQeqpdsGTIKIgETVKLAYVDQS------RD----------AL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SPRMCVSQIVGEGLRIHKMGTEAEQEQAIIAAL--------KEVGldpetrhryphEFSGGQRQRIAIARALVLKPALIL 447
Cdd:PRK11819 400 DPNKTVWEEISGGLDIIKVGNREIPSRAYVGRFnfkggdqqKKVG-----------VLSGGERNRLHLAKTLKQGGNVLL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1834229548 448 LDEPTSALDrtvqrqvVELLRSLQS---KYNLTYLFISHD 484
Cdd:PRK11819 469 LDEPTNDLD-------VETLRALEEallEFPGCAVVISHD 501
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
305-465 |
3.18e-08 |
|
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: 55.25 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLSPRMCVSQ 383
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 384 IVGEglriHKMGTEAEQEQAIIAalkEVGLDpetrhrypheFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQV 463
Cdd:cd03291 136 CQLE----EDITKFPEKDNTVLG---EGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
..
gi 1834229548 464 VE 465
Cdd:cd03291 199 FE 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
299-504 |
4.02e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLgLAILRLIGSK--GGIRFEGKQLDSLTQQQ-----VRPLRREMQVVFQDp 371
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTL-LKCLFGIYQKdsGSILFQGKEIDFKSSKEalengISMVHQELNLVLQR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 372 fgSLSPRMCVSQIVGEGLRI--HKMGTEAEqeqaiiAALKEVGLDPETRHRYPhEFSGGQRQRIAIARALVLKPALILLD 449
Cdd:PRK10982 89 --SVMDNMWLGRYPTKGMFVdqDKMYRDTK------AIFDELDIDIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 450 EPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVV 504
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-231 |
4.45e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYpLARHPSGTIEYSGQNllNLKEKTIRHIRgNRIAMIFQEPMT 104
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIER-LYDPTEGDIIINDSH--NLKDINLKWWR-SKIGVVSQDPLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 --------------SLNPLHSIEKQINE------------------VLGIHKGLI------GKVATKRTLELLEMVGIPE 146
Cdd:PTZ00265 472 fsnsiknnikyslySLKDLEALSNYYNEdgndsqenknkrnscrakCAGDLNDMSnttdsnELIEMRKNYQTIKDSEVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 147 PEKRL------KALP-----------HELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARLGM 209
Cdd:PTZ00265 552 VSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|..
gi 1834229548 210 ALLLISHDLNLVkRIAHRVCVM 231
Cdd:PTZ00265 632 ITIIIAHRLSTI-RYANTIFVL 652
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
307-498 |
4.55e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 307 FSLP---QGQTLGIVGESGSGKSTLgLAIL--RLI---------GSKGGI--RFEGKQL----DSLTQQQVRPLRReMQV 366
Cdd:PRK13409 91 YGLPipkEGKVTGILGPNGIGKTTA-VKILsgELIpnlgdyeeePSWDEVlkRFRGTELqnyfKKLYNGEIKVVHK-PQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgslsprMCVSQIVGEGLRihkmgtEAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALvLKPALI 446
Cdd:PRK13409 169 VDLIP-------KVFKGKVRELLK------KVDERGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAAL-LRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834229548 447 -LLDEPTSALDrTVQR-QVVELLRSLQSKYNLtyLFISHDLAVVKALSHQLMVV 498
Cdd:PRK13409 234 yFFDEPTSYLD-IRQRlNVARLIRELAEGKYV--LVVEHDLAVLDYLADNVHIA 284
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
291-507 |
5.02e-08 |
|
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: 53.42 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 291 LLKKTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSK----GGIRFEGKQLDSLTQQQVRplrremQV 366
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsveGDIHYNGIPYKEFAEKYPG------EI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFqdpfgslsprmcVSQivgEGLRIHKMGTEaeqeQAIIAALKEVGldpetrHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03233 86 IY------------VSE---EDVHFPTLTVR----ETLDFALRCKG------NEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNLTyLFISHDLAVVKALS--HQLMVVKQGQVVEQG 507
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTT-TFVSLYQASDEIYDlfDKVLVLYEGRQIYYG 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-189 |
5.03e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDlaVEFVVGERcqRVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPYPlarhPSGTIEYSGQNLL 80
Cdd:PRK10247 2 QENSPLLQLQN--VGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASLISP----TSGTLLFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 NLKEKTIRHirgnRIAMIFQEPM----TSLNPL---HSIEKQinevlgihkgligKVATKRTLELLEMVGIPEP--EKRL 151
Cdd:PRK10247 73 TLKPEIYRQ----QVSYCAQTPTlfgdTVYDNLifpWQIRNQ-------------QPDPAIFLDDLERFALPDTilTKNI 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 1834229548 152 kalpHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:PRK10247 136 ----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
302-514 |
5.08e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 302 VDGINFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKGGIRFEGKQLDSLTQQQVRPLRREMQVVFQDPfgsLSPRMC 380
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKA---LNEKYY 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 381 VSQIVG----EGLRIHKMGTEAEqeqaiiaaLKEVGLDpetrhrypheFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:TIGR00957 731 QQVLEAcallPDLEILPSGDRTE--------IGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 457 RTVQRQVVE-LLRSLQSKYNLTYLFISHDLAVVKALSHqLMVVKQGQVVEQGDAQSIFA 514
Cdd:TIGR00957 793 AHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELLQ 850
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
307-492 |
6.47e-08 |
|
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: 53.91 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 307 FSLP---QGQTLGIVGESGSGKSTlGLAIL--RLIGSKGGIR-----------FEGKQL----DSLTQQQVRPLRREmQV 366
Cdd:cd03236 18 HRLPvprEGQVLGLVGPNGIGKST-ALKILagKLKPNLGKFDdppdwdeildeFRGSELqnyfTKLLEGDVKVIVKP-QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 367 VFQDPfgslsprmcvSQIVGEGLRIHKMGTEAEQEQAIIAALkevGLDPeTRHRYPHEFSGGQRQRIAIARALVLKPALI 446
Cdd:cd03236 96 VDLIP----------KAVKGKVGELLKKKDERGKLDELVDQL---ELRH-VLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834229548 447 LLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALS 492
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLS 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
158-456 |
6.80e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALD-----------VTVQlkilellkelQARLGMALLLISHDLNLVKRIAH 226
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplsrrqfweliDRIR----------AERPGMSVLVATAYMEEAERFDW 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 227 RVcVMQRGCIVEQASCEQLFRAPQHP-----YTReLLAAEPSGTPATNVVGPPMLTVEDLKVwfpIK-KGLLKKTVDYVk 300
Cdd:NF033858 207 LV-AMDAGRVLATGTPAELLARTGADtleaaFIA-LLPEEKRRGHQPVVIPPRPADDDDEPA---IEaRGLTMRFGDFT- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTL-----GLailrLIGSKGGIRFEGKQLDSltqqqvrplrremqvvfqdpfGSL 375
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTmkmltGL----LPASEGEAWLFGQPVDA---------------------GDI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 376 SPRMCV---SQ--------IVGEGLRIH----KMGtEAEQEQAIIAALKEVGLDPETRHRyPHEFSGGQRQRIAIARALV 440
Cdd:NF033858 336 ATRRRVgymSQafslygelTVRQNLELHarlfHLP-AAEIAARVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVI 413
|
330
....*....|....*.
gi 1834229548 441 LKPALILLDEPTSALD 456
Cdd:NF033858 414 HKPELLILDEPTSGVD 429
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
426-502 |
9.50e-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: 52.61 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 426 SGGQRQ------RIAIARALVLKPALILLDEPTSALDR-TVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
....
gi 1834229548 499 KQGQ 502
Cdd:cd03240 197 KDGR 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-503 |
1.06e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 147 PEKRLKAlPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVtvqlKILELLKELQARLGMALLLISHDLNLVKRIAH 226
Cdd:PLN03073 335 PEMQVKA-TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL----HAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 227 RVCVMQRGCIV---------EQASCEQLF----------RAPQHPYT----------------RELLAAEPSG------- 264
Cdd:PLN03073 410 DILHLHGQKLVtykgdydtfERTREEQLKnqqkafesneRSRSHMQAfidkfrynakraslvqSRIKALDRLGhvdavvn 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 265 ---------TPaTNVVGPPMLTVEDLKVWFPIKKGLLKKtvdyvkavdgINFSLPQGQTLGIVGESGSGKSTlglaILRL 335
Cdd:PLN03073 490 dpdykfefpTP-DDRPGPPIISFSDASFGYPGGPLLFKN----------LNFGIDLDSRIAMVGPNGIGKST----ILKL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 336 IGSkggirfegkqldsltqqqvrplrrEMQVVFQDPFGSLSPRMCV-SQIVGEGLRIHKMGT-------EAEQEQAIIAA 407
Cdd:PLN03073 555 ISG------------------------ELQPSSGTVFRSAKVRMAVfSQHHVDGLDLSSNPLlymmrcfPGVPEQKLRAH 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 408 LKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKynltYLFISHDLAV 487
Cdd:PLN03073 611 LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG----VLMVSHDEHL 686
|
410
....*....|....*.
gi 1834229548 488 VKALSHQLMVVKQGQV 503
Cdd:PLN03073 687 ISGSVDELWVVSEGKV 702
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-248 |
1.22e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 1 MNQDNLIEVRDLAVEFVVGERCQRvveGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQnll 80
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-----RLASGKISILGQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 81 nlkeKTIRHIRGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIgKVATKRTLEL----LEMVGIPEPEKRLKAlph 156
Cdd:PRK15056 70 ----PTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWL-RRAKKRDRQIvtaaLARVDMVEFRHRQIG--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVcVMQRGCI 236
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTV 219
|
250
....*....|..
gi 1834229548 237 VEQASCEQLFRA 248
Cdd:PRK15056 220 LASGPTETTFTA 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
304-498 |
1.86e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 304 GIN----FSLP---QGQTLGIVGESGSGKSTLgLAIL--RLI---------GSKGGI--RFEGKQL----DSLTQQQVRP 359
Cdd:COG1245 84 GENgfrlYGLPvpkKGKVTGILGPNGIGKSTA-LKILsgELKpnlgdydeePSWDEVlkRFRGTELqdyfKKLANGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 360 LRREMQVvfqdpfgSLSPRMcVSQIVGEGLRihkmgtEAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARAL 439
Cdd:COG1245 163 AHKPQYV-------DLIPKV-FKGTVRELLE------KVDERGKLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 440 VLKPALILLDEPTSALDrTVQR-QVVELLRSLqSKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:COG1245 228 LRDADFYFFDEPSSYLD-IYQRlNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
105-495 |
1.86e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.06 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 SLNPLHSIEKQINE-VLGIHKGLIGkvaTKRTLELLEMVGIP--EPEKRLKALphelSGGQRQRVMIAMALANEPE--LL 179
Cdd:PRK00635 428 SLQELFIFLSQLPSkSLSIEEVLQG---LKSRLSILIDLGLPylTPERALATL----SGGEQERTALAKHLGAELIgiTY 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 180 IADEPTTALDV--TVQLKILELLKELQarlGMALLLISHDLNLVKrIAHRVCVMQRGCIVEQAscEQLFrapqhpytrel 257
Cdd:PRK00635 501 ILDEPSIGLHPqdTHKLINVIKKLRDQ---GNTVLLVEHDEQMIS-LADRIIDIGPGAGIFGG--EVLF----------- 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 258 laaepSGTPATNVVGPPMLTVE----DLKVWFPIKKGLLKKTVDYVKA----VDGINFSLPQGQTLGIVGESGSGKS--- 326
Cdd:PRK00635 564 -----NGSPREFLAKSDSLTAKylrqELTIPIPEKRTNSLGTLTLSKAtkhnLKDLTISLPLGRLTVVTGVSGSGKSsli 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 327 --TLGLAILRLI--GSKGGIRFEG--------------------------KQLDSLTQ---QQVRPLRREM---QVVFQD 370
Cdd:PRK00635 639 ndTLVPAVEEFIeqGFCSNLSIQWgaisrlvhitrdlpgrsqrsipltyiKAFDDLRElfaEQPRSKRLGLtksHFSFNT 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 371 PFGSLS---------------PRMCVS----QIVGEGLRIHKMGT-----------EAEQ----EQAI---IAALKEVGL 413
Cdd:PRK00635 719 PLGACAecqglgsitttdnrtSIPCPSclgkRFLPQVLEVRYKGKniadilemtayEAEKffldEPSIhekIHALCSLGL 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 414 DPETRHRYPHEFSGGQRQRIAIARAL---VLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKA 490
Cdd:PRK00635 799 DYLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVVKV 877
|
....*
gi 1834229548 491 LSHQL 495
Cdd:PRK00635 878 ADYVL 882
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-249 |
2.02e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpyplARH---PSGTIEYSGQNLLNLKektIRHIRGnRIAMIFQE 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKS----TLLSLI----QRHfdvSEGDIRFHDIPLTKLQ---LDSWRS-RLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 PMtslnpLHSIEKQINEVLGIHKgligkvATKRTLEllEMVGIPEPEKRLKALPH-----------ELSGGQRQRVMIAM 170
Cdd:PRK10789 398 PF-----LFSDTVANNIALGRPD------ATQQEIE--HVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIAR 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 171 ALANEPELLIADEPTTALDvtVQLKILELLKELQARLGMALLLISHDLNLVKRiAHRVCVMQRGCIVEQASCEQLFRAP 249
Cdd:PRK10789 465 ALLLNAEILILDDALSAVD--GRTEHQILHNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
424-498 |
2.08e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 2.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 424 EFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVVKALSHQLMVV 498
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-216 |
2.27e-07 |
|
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: 50.62 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVefvVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL----PYplarhpsgtieYSGqnllnl 82
Cdd:cd03223 1 IELENLSL---ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKS----SLFRALaglwPW-----------GSG------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 kekTIRHIRGNRIAMIFQEPMTslnPLHSIEKQInevlgihkgligkvatkrtlellemvgipepekrlkALP--HELSG 160
Cdd:cd03223 57 ---RIGMPEGEDLLFLPQRPYL---PLGTLREQL------------------------------------IYPwdDVLSG 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 161 GQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKelqaRLGMALLLISH 216
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
159-503 |
2.57e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlgmALLLISHDLNLVKRIAHRVCVMQRGCIVE 238
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 239 --------------------------QASCEQL------FRA----PQHPYTR-------ELLAAEPSGTP------ATN 269
Cdd:PRK10636 227 ytgnyssfevqratrlaqqqamyesqQERVAHLqsyidrFRAkatkAKQAQSRikmlermELIAPAHVDNPfhfsfrAPE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 270 VVGPPMLTVEDlkvwfpIKKGLLKKTVdyvkaVDGINFSLPQGQTLGIVGESGSGKSTLglaILRLIGS----KGGIRF- 344
Cdd:PRK10636 307 SLPNPLLKMEK------VSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTL---IKLLAGElapvSGEIGLa 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 345 EGKQLDSLTQQQVRPLRREmqvvfQDPFGSLSprmcvsqivgeglRIhkmgTEAEQEQAIIAALKEVGLDPETRHRYPHE 424
Cdd:PRK10636 373 KGIKLGYFAQHQLEFLRAD-----ESPLQHLA-------------RL----APQELEQKLRDYLGGFGFQGDKVTEETRR 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 425 FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSkynlTYLFISHDLAVVKALSHQLMVVKQGQV 503
Cdd:PRK10636 431 FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
286-470 |
2.76e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 286 PIKKG---LLKKTVDYVKAvdginfslpqGQTLGIVGESGSGKSTLgLAIL--RLIGS--KGGIRF-EGKQLDS------ 351
Cdd:TIGR00956 770 KIKKEkrvILNNVDGWVKP----------GTLTALMGASGAGKTTL-LNVLaeRVTTGviTGGDRLvNGRPLDSsfqrsi 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 352 -LTQQQ--------VRP-------LRREMQVvfqdpfgSLSPRMcvsQIVGEGLRIHKMGTEAEqeqAIIAALKEvGLDP 415
Cdd:TIGR00956 839 gYVQQQdlhlptstVREslrfsayLRQPKSV-------SKSEKM---EYVEEVIKLLEMESYAD---AVVGVPGE-GLNV 904
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 416 EtrhryphefsggQRQRIAIARALVLKPALIL-LDEPTSALDRTVQRQVVELLRSL 470
Cdd:TIGR00956 905 E------------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-190 |
3.84e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 32 DIKRGETLALVGESGSGKSvTAHSIL--RLLPYPLARHPSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEPMtslnpl 109
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKT-TFAKILagVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRSANTDDFGSSY------ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 110 hsIEKQINEVLGIHKgligkvatkrtleLLEmvgipepeKRLKalphELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:COG1245 435 --YKTEIIKPLGLEK-------------LLD--------KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
.
gi 1834229548 190 V 190
Cdd:COG1245 488 V 488
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-231 |
5.32e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 34 KRGETLALVGESGSGKSvTAHSILrllpyplarhpsgtieySGQNLLNLKEKT--------IRHIRGNRIAMIFqepmts 105
Cdd:cd03236 24 REGQVLGLVGPNGIGKS-TALKIL-----------------AGKLKPNLGKFDdppdwdeiLDEFRGSELQNYF------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 lnplhsiEKQIN-EVLGIHK----GLIGKVATKRTLELL----------EMVGIPEPEKRLKALPHELSGGQRQRVMIAM 170
Cdd:cd03236 80 -------TKLLEgDVKVIVKpqyvDLIPKAVKGKVGELLkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 171 ALANEPELLIADEPTTALDVTvQLKILELLKELQARLGMALLLISHDLNLVKRIAHRVCVM 231
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIK-QRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-245 |
6.02e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 8 EVRdLAVEFVVGercQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLpYPLARHPSGTIEYSGQNLlnlkekti 87
Cdd:PRK11288 255 EVR-LRLDGLKG---PGLREPISFSVRAGEIVGLFGLVGAGRS----ELMKLL-YGATRRTAGQVYLDGKPI-------- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 88 rHIRGNRIA-----MIFQEPMTSLN--PLHSIEKQIN---EVLGIHKGLI--GKVATKRTLELLEMVGIPEPEKRLKALp 155
Cdd:PRK11288 318 -DIRSPRDAiragiMLCPEDRKAEGiiPVHSVADNINisaRRHHLRAGCLinNRWEAENADRFIRSLNIKTPSREQLIM- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 156 hELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGC 235
Cdd:PRK11288 396 -NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
250
....*....|....*
gi 1834229548 236 IV-----EQASCEQL 245
Cdd:PRK11288 474 IAgelarEQATERQA 488
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
305-536 |
1.28e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIgskggirfegkqldsltqqqvrPLRREMQVVFQdpfGSLSPRMCVSQI 384
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGEL----------------------SHAETSSVVIR---GSVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 385 VGEGLRIHKM-GTEAEQE---QAIIAALKEVGLDPETRHRYPH------EFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:PLN03232 691 FNATVRENILfGSDFESErywRAIDVTALQHDLDLLPGRDLTEigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 455 LDRTVQRQVVE--LLRSLQSKynlTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAAPQhpYTQQLLEAAFLVP 532
Cdd:PLN03232 771 LDAHVAHQVFDscMKDELKGK---TRVLVTNQLHFL-PLMDRIILVSEGMIKEEGTFAELSKSGS--LFKKLMENAGKMD 844
|
....
gi 1834229548 533 ATAQ 536
Cdd:PLN03232 845 ATQE 848
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-191 |
1.65e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpyplarhpSGTIE---YSGQNLLNLKEKTIRHIRgnRIAMIFQE 101
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL------------AGRIQgnnFTGTILANNRKPTKQILK--RTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 102 PMtsLNPLHSIEKQI--NEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRL--KALPHELSGGQRQRVMIAMALANEPE 177
Cdd:PLN03211 149 DI--LYPHLTVRETLvfCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170
....*....|....
gi 1834229548 178 LLIADEPTTALDVT 191
Cdd:PLN03211 227 LLILDEPTSGLDAT 240
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
305-507 |
1.68e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLailRLIGSKGGIRFegkqLDSLTQQqVRPLRREMQVVFQDPFGSLSPRMCVSQ- 383
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLAF---DTIYAEGQRRY----VESLSAY-ARQFLGQMDKPDVDSIEGLSPAIAIDQk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 384 --------IVGEGLRIH--------KMGTEAEqeqaiIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARAL--VLKPAL 445
Cdd:cd03270 86 ttsrnprsTVGTVTEIYdylrllfaRVGIRER-----LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 446 ILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALSHQLMV-----VKQGQVVEQG 507
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
301-484 |
1.93e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 301 AVDGINFSLPQGQTLGIVGESGSGKSTlgLAILrLIG----SKGGIRFEGKQLDSLTQQQVRPLrreMQVVFQD------ 370
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKST--LAML-LTGlyqpQSGEILLDGKPVTAEQPEDYRKL---FSAVFTDfhlfdq 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 371 ---PFGSLSPrmcvSQIVGEGLRIHKMGTEAEQEQAIIAALKevgldpetrhrypheFSGGQRQRIAIARALVLKPALIL 447
Cdd:PRK10522 412 llgPEGKPAN----PALVEKWLERLKMAHKLELEDGRISNLK---------------LSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1834229548 448 LDEptSALDRTVQ-RQVV--ELLRSLQSKyNLTYLFISHD 484
Cdd:PRK10522 473 LDE--WAADQDPHfRREFyqVLLPLLQEM-GKTIFAISHD 509
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-254 |
2.17e-06 |
|
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: 49.14 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKT 86
Cdd:cd03288 20 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRhirgNRIAMIFQEPMtslnpLHSIEKQINevLGIHKgligKVATKRTLELLEmvgIPEPEKRLKALPHEL-------- 158
Cdd:cd03288 93 LR----SRLSIILQDPI-----LFSGSIRFN--LDPEC----KCTDDRLWEALE---IAQLKNMVKSLPGGLdavvtegg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 159 ---SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQArlGMALLLISHDLNLVKRiAHRVCVMQRGC 235
Cdd:cd03288 155 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA--DRTVVTIAHRVSTILD-ADLVLVLSRGI 231
|
250
....*....|....*....
gi 1834229548 236 IVEQASCEQLFRAPQHPYT 254
Cdd:cd03288 232 LVECDTPENLLAQEDGVFA 250
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-223 |
2.21e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPLARH------------------------------------- 67
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHivfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 68 ------PSGTIEYSGQNLL---NLKEKTIRHIRgNRIAMIFQEPMTslnplhsIEKQINEVLGIHKGLIGKVATKRTLEL 138
Cdd:PTZ00265 1263 eggsgeDSTVFKNSGKILLdgvDICDYNLKDLR-NLFSIVSQEPML-------FNMSIYENIKFGKEDATREDVKRACKF 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 139 LEMvgipepEKRLKALPHE-----------LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARL 207
Cdd:PTZ00265 1335 AAI------DEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1408
|
250
....*....|....*.
gi 1834229548 208 GMALLLISHDLNLVKR 223
Cdd:PTZ00265 1409 DKTIITIAHRIASIKR 1424
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-248 |
2.45e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEF-VVGERcqRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIL-RllPYplARHPSGTIeysgqnLLN 81
Cdd:NF040905 255 EVVFEVKNWTVYHpLHPER--KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgR--SY--GRNISGTV------FKD 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 82 LKEKTIRHIR---GNRIA----------MIFQEPM---TSLNPLHSIEKQ--INEVLGIhkgligKVATK-------RTL 136
Cdd:NF040905 323 GKEVDVSTVSdaiDAGLAyvtedrkgygLNLIDDIkrnITLANLGKVSRRgvIDENEEI------KVAEEyrkkmniKTP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 137 ELLEMVGipepekrlkalphELSGGQRQRVMIAMALANEPELLIADEPTTALDV-------TVqlkilellKELQARLGM 209
Cdd:NF040905 397 SVFQKVG-------------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyeiyTI--------INELAAEGK 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1834229548 210 ALLLISHDLNLVKRIAHRVCVMQRGCIV-----EQASCEQLFRA 248
Cdd:NF040905 456 GVIVISSELPELLGMCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-190 |
2.96e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 48.56 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 32 DIKRGETLALVGESGSGKSvtahSILRLLpyplarhpSGTIEYSGQNLLnlkektirhIRGNRIAMIFQE-----PMTSL 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKT----TFIKML--------AGVLKPDEGDIE---------IELDTVSYKPQYikadyEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 107 NPLHSIEKQinevLGIHKGLIGKVATKrtlelLEMVGIPEPEKRlkalphELSGGQRQRVMIAMALANEPELLIADEPTT 186
Cdd:cd03237 80 DLLSSITKD----FYTHPYFKTEIAKP-----LQIEQILDREVP------ELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
....
gi 1834229548 187 ALDV 190
Cdd:cd03237 145 YLDV 148
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
158-251 |
3.46e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALAN---------EPELLIADEPTTALDVTVQLKILELLKELQARLGMALLLISHDLNLVKRIAHRV 228
Cdd:PRK13547 146 LSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI 225
|
90 100
....*....|....*....|...
gi 1834229548 229 CVMQRGCIVEQASCEQLFRaPQH 251
Cdd:PRK13547 226 AMLADGAIVAHGAPADVLT-PAH 247
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-248 |
4.26e-06 |
|
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: 49.94 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFvvGERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKEKT 86
Cdd:TIGR00957 1285 VEFRNYCLRY--REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN-----ESAEGEIIIDGLNIAKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRhirgNRIAMIFQEPM-------TSLNPLHSIEKQinevlgihkgligKVATKRTLELLEMVGIPEPEKrlkaLPHE-- 157
Cdd:TIGR00957 1358 LR----FKITIIPQDPVlfsgslrMNLDPFSQYSDE-------------EVWWALELAHLKTFVSALPDK----LDHEca 1416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 -----LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQlkilellKELQARL-----GMALLLISHDLNLVKRIAhR 227
Cdd:TIGR00957 1417 eggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-------NLIQSTIrtqfeDCTVLTIAHRLNTIMDYT-R 1488
|
250 260
....*....|....*....|.
gi 1834229548 228 VCVMQRGCIVEQASCEQLFRA 248
Cdd:TIGR00957 1489 VIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
275-508 |
7.51e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 275 MLTVEDLKVwfpikkgllkkTVDYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAilrLIGSK------GGIRFEGKQ 348
Cdd:PRK09580 1 MLSIKDLHV-----------SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREdyevtgGTVEFKGKD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 349 LDSLTqqqvrPLRREMQVVF---QDP--FGSLSPRMCVSQIVGEgLRIHKMGTEAEQ---EQAIIAALKEVGLDPETRHR 420
Cdd:PRK09580 67 LLELS-----PEDRAGEGIFmafQYPveIPGVSNQFFLQTALNA-VRSYRGQEPLDRfdfQDLMEEKIALLKMPEDLLTR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 421 YPHE-FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLM-VV 498
Cdd:PRK09580 141 SVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKPDYVhVL 219
|
250
....*....|
gi 1834229548 499 KQGQVVEQGD 508
Cdd:PRK09580 220 YQGRIVKSGD 229
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
504-527 |
7.69e-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: 7.69e-06
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
306-514 |
7.77e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 306 NFSLPQGQTLGIVGESGSGKSTLGLAIL-RLIGSKG--------GIRFEGKQLDSLTQQQVRPLRREMQVVFQDPFGSLs 376
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAgELPLLSGerqsqfshITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDTGRT- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 prmcVSQIVGEGlriHKMGTEAEQ--EQAIIAALkevgLDpeTRHRYpheFSGGQRQRIAIARALVLKPALILLDEPTSA 454
Cdd:PRK10938 102 ----TAEIIQDE---VKDPARCEQlaQQFGITAL----LD--RRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 455 LDRTVQRQVVELLRSLQSKyNLTYLFISHDLAVVKALSHQLMVVKQGQVVEQGDAQSIFA 514
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
426-500 |
1.05e-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: 45.81 E-value: 1.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 426 SGGQRQRIAIARALVL---KPA-LILLDEPTSALDRTVQRQVVELLRSlQSKYNLTYLFISHDLAVVKALSHQLMVVKQ 500
Cdd:cd03227 79 SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-225 |
1.54e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.62 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 4 DNLIEVRDLAVEFvvGERCqrVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLL-----PYplarhpSGTIEYSgqn 78
Cdd:TIGR03719 320 DKVIEAENLTKAF--GDKL--LIDDLSFKLPPGGIVGVIGPNGAGKS----TLFRMItgqeqPD------SGTIEIG--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 79 llnlkeKTIRhirgnrIAMIFQEpMTSLNPLHSIEKQINEVLGIHKglIGK--VATKRTLELLEMVGiPEPEKRLKalph 156
Cdd:TIGR03719 383 ------ETVK------LAYVDQS-RDALDPNKTVWEEISGGLDIIK--LGKreIPSRAYVGRFNFKG-SDQQKKVG---- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDV-TVQlkilellKELQARLGMA--LLLISHDLNLVKRIA 225
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVeTLR-------ALEEALLNFAgcAVVISHDRWFLDRIA 507
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-222 |
1.54e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPyPLARHPSGTIEYSGQNllnlkektirhIRGNRIA----MI 98
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKT----TLLKLIA-GLLNPEKGEILFERQS-----------IKKDLCTyqkqLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 99 FQEPMTSLNPLHSIEKqiNEVLGIHkgligkvATKRTLELLEMVGIPEPEKRLKALPHELSGGQRQRVMIAMALANEPEL 178
Cdd:PRK13540 78 FVGHRSGINPYLTLRE--NCLYDIH-------FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 179 LIADEPTTALDVTVQLKILELLKELQARlGMALLLISH-DLNLVK 222
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAK-GGAVLLTSHqDLPLNK 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
305-516 |
1.87e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLGLAILRLIGSKGGIRFEGKQLDSLTQQ------QVRPlrremQVVFQDP--FGSLS 376
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQawimnaTVRG-----NILFFDEedAARLA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 377 PRMCVSQIVGEgLRIHKMGTEAEqeqaiiaaLKEVGLDpetrhrypheFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PTZ00243 754 DAVRVSQLEAD-LAQLGGGLETE--------IGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 457 RTVQRQVVE--LLRSLQSKynlTYLFISHDLAVVkALSHQLMVVKQGQVVEQGDAQSIFAAP 516
Cdd:PTZ00243 815 AHVGERVVEecFLGALAGK---TRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
292-456 |
1.90e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 292 LKKTVDYVKAV-DGINFSLPQGQTLGIVGESGSGKSTLglaiLRLIGskgGI--RFEGKqldsltqqqVRP--------L 360
Cdd:PRK11819 12 VSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMA---GVdkEFEGE---------ARPapgikvgyL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 361 RREMQvvfqdpfgsLSPRMCVSQIVGEGLR-----------IH-KMGTE--------AEQE--QAIIAALKevGLDPETR 418
Cdd:PRK11819 76 PQEPQ---------LDPEKTVRENVEEGVAevkaaldrfneIYaAYAEPdadfdalaAEQGelQEIIDAAD--AWDLDSQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 419 -------HRYPH------EFSGGQRQRIAIARALVLKPALILLDEPTSALD 456
Cdd:PRK11819 145 leiamdaLRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-244 |
1.94e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 23 QRVVEGVSFDIKRGETLALVGESGSGKSVTAHSIlrllpYPLARHPSGTIEYSGQNLLNLK-EKTIRH-----IRGNRIA 96
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETL-----FGIREKSAGTITLHGKKINNHNaNEAINHgfalvTEERRST 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 97 MIFQEPMTSLNPLHSIEKQinevlgiHKGLIGKVATKR----TLELLEMVGIPEPEKrlKALPHELSGGQRQRVMIAMAL 172
Cdd:PRK10982 336 GIYAYLDIGFNSLISNIRN-------YKNKVGLLDNSRmksdTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834229548 173 ANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVCVMQRG---CIVEQASCEQ 244
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGlvaGIVDTKTTTQ 480
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-246 |
2.46e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 45.64 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 24 RVVEGVSFDIKRGETLALVGESGSGKSvTAHSILRLLPyplaRHPSGTIEYSGQNLLNLKekTIRHIR--------GNRI 95
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKT-TLLGTLCGDP----RATSGRIVFDGKDITDWQ--TAKIMReavaivpeGRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 96 --AMIFQEPMtSLNPLHSIEKQINEVLgihkgligkvatKRTLELLemvgiPEPEKRLKALPHELSGGQRQRVMIAMALA 173
Cdd:PRK11614 92 fsRMTVEENL-AMGGFFAERDQFQERI------------KWVYELF-----PRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 174 NEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIAHRVCVMQRGCIVEQASCEQLF 246
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
237-266 |
3.26e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 42.00 E-value: 3.26e-05
10 20 30
....*....|....*....|....*....|
gi 1834229548 237 VEQASCEQLFRAPQHPYTRELLAAEPSGTP 266
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDP 30
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-193 |
4.31e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLArhPS-GTIEYSGqnllnlkektirhirgnRIAMifqEPM 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKS----SLLMMIMGELE--PSeGKIKHSG-----------------RISF---SPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 104 TSLNPLHSIEKQIneVLGIHKGLIGKVATKRTLELLEMVGIpEPEKRLKALPH---ELSGGQRQRVMIAMALANEPELLI 180
Cdd:TIGR01271 495 TSWIMPGTIKDNI--IFGLSYDEYRYTSVIKACQLEEDIAL-FPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYL 571
|
170
....*....|...
gi 1834229548 181 ADEPTTALDVTVQ 193
Cdd:TIGR01271 572 LDSPFTHLDVVTE 584
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
426-507 |
4.87e-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: 46.16 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 426 SGGQRQRIAIARALVLK---PALILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKALSHQLMV----- 497
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|
gi 1834229548 498 VKQGQVVEQG 507
Cdd:TIGR00630 910 DGGGTVVASG 919
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-222 |
5.49e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 2 NQDNLIEVRDLAVefvVGERCQRVVEGVSFDIKRGETLALVGESGSGKSvtahSILRLLP--YPLarhpsgtieYSGqnL 79
Cdd:TIGR00954 447 YQDNGIKFENIPL---VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKS----SLFRILGelWPV---------YGG--R 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 80 LNLKEKtirhirgNRIAMIFQEPMTSLNPLH-------SIEKQINevlgihKGLIGKVaTKRTLELLEMVGIPEPEKRLK 152
Cdd:TIGR00954 509 LTKPAK-------GKLFYVPQRPYMTLGTLRdqiiypdSSEDMKR------RGLSDKD-LEQILDNVQLTHILEREGGWS 574
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 153 ALPH---ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKelqaRLGMALLLISHDLNLVK 222
Cdd:TIGR00954 575 AVQDwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHRKSLWK 643
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-263 |
7.41e-05 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 41.58 E-value: 7.41e-05
10 20
....*....|....*....|....*...
gi 1834229548 236 IVEQASCEQLFRAPQHPYTRELLAAEPS 263
Cdd:TIGR01727 2 IVETGPAEEIFKNPLHPYTKALLSAIPT 29
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
305-370 |
8.21e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 45.17 E-value: 8.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834229548 305 INFSLPQGQTLGIVGESGSGKSTLglaiLRLI-G----SKGGIRFEGKQLDSLTQQQVRPLrreMQVVFQD 370
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTL----AKLLtGlyrpESGEILLDGQPVTADNREAYRQL---FSAVFSD 414
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
426-504 |
9.33e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 426 SGGQRQRIAIARALVLKPALILLDEPTSALDrtvqrqvVELLRSLQS---KYNLTYLFISHDLAVVKALSHQLMVVKQGQ 502
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMaleKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
..
gi 1834229548 503 VV 504
Cdd:PRK15064 513 VV 514
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-225 |
1.07e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 35 RGETLALVGESGSGKSVTAHSILRLLPYPLArhpsGTIEYSGQNLLNLKEKTIRHIRGNRIamifqepmtslnplhsiek 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG----GVIYIDGEDILEEVLDQLLLIIVGGK------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 115 qinevlgihkgligkvatkrtlellemvgipepekrlkalPHELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQ- 193
Cdd:smart00382 58 ----------------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEa 97
|
170 180 190
....*....|....*....|....*....|....*.
gi 1834229548 194 ----LKILELLKELQARLGMALLLISHDLNLVKRIA 225
Cdd:smart00382 98 llllLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
502-527 |
1.16e-04 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 40.81 E-value: 1.16e-04
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-338 |
1.33e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 150 RLKALP-----HELSGGQRQRVMIAMALAN---EPELLIADEPTTALDvTVQLKILELLKELQARLGMALLLISHDLNLV 221
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLH-THDIKALIYVLQSLTHQGHTVVIIEHNMHVV 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 222 KrIAHRVCVM------QRGCIVEQASCEQLFrapqHPYTRELLAAEP--SGTPATnvvgpPMLTVEDLKVwfPIKKGLLK 293
Cdd:PRK00635 876 K-VADYVLELgpeggnLGGYLLASCSPEELI----HLHTPTAKALRPylSSPQEL-----PYLPDPSPKP--PVPADITI 943
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1834229548 294 KTVdYVKAVDGINFSLPQGQTLGIVGESGSGKSTLGLAILRLIGS 338
Cdd:PRK00635 944 KNA-YQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGN 987
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-189 |
1.40e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 10 RDLAVEFVVGERCQRVVEGVSFDIKRGETLALVGESGSGKS--------------VTAHSIL---RLLPYPLARhpsgTI 72
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTtllnvlaervttgvITGGDRLvngRPLDSSFQR----SI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 73 EYSGQNLLNLKEKTIRHirgnriAMIFQEPMTSLNPLHSIEKQ--INEVLgihkgligkvatkrtlELLEMVGIPEPekr 150
Cdd:TIGR00956 839 GYVQQQDLHLPTSTVRE------SLRFSAYLRQPKSVSKSEKMeyVEEVI----------------KLLEMESYADA--- 893
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1834229548 151 LKALPHE-LSGGQRQRVMIAMALANEPELLI-ADEPTTALD 189
Cdd:TIGR00956 894 VVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-193 |
1.43e-04 |
|
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: 43.69 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVvgERCQRVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplarHPSGTIEYSGQNLLNLKEKT 86
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRG--NRIAMIFQEPM-TSLNPL--HSIEK--QINEVLGIhKGLIGKVATKRTLELLEMVGIpepekrlkalpheLS 159
Cdd:cd03289 75 WRKAFGviPQKVFIFSGTFrKNLDPYgkWSDEEiwKVAEEVGL-KSVIEQFPGQLDFVLVDGGCV-------------LS 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALD-VTVQ 193
Cdd:cd03289 141 HGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
425-501 |
1.50e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 1.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 425 FSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRSLQSKYNLTYLfISHDLAVVKALSHQLMVVKQG 501
Cdd:TIGR01257 2071 YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKG 2146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-234 |
1.55e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 20 ERCQR-VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPyplarHPSGTIEYSGQNLlnlkEKTIRHIRGNriami 98
Cdd:TIGR01257 939 EPSGRpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP-----PTSGTVLVGGKDI----ETNLDAVRQS----- 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 99 fqepmTSLNPLHSI---EKQINEVLGIHKGLIGKVATKRTLELLEMVGIPEPEKRLKALPHELSGGQRQRVMIAMALANE 175
Cdd:TIGR01257 1005 -----LGMCPQHNIlfhHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834229548 176 PELLIADEPTTALDVTVQlkILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSR--RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
153-189 |
1.56e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.56e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1834229548 153 ALPHELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:NF033858 393 ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
125-232 |
1.78e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 125 GLIGKVATKRTLELLEMVGIPEPEKRLKALPH----------ELSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQL 194
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGitpvykpqyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRL 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 1834229548 195 KILELLKELQARLGMALLLISHDLNLVKRIAHRVCVMQ 232
Cdd:cd03222 109 NAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-263 |
2.06e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKTIRHIrgnrIAMIFQEPMT 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 -------SLNPLhSIEKQINEVLGIHKGLIGKVATKRTLELlemvgipepEKRLKALPHELSGGQRQRVMIAMALANEPE 177
Cdd:PLN03232 1322 fsgtvrfNIDPF-SEHNDADLWEALERAHIKDVIDRNPFGL---------DAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 178 LLIADEPTTALDVTVQLKILELLKELQARLGMalLLISHDLNLVKRiAHRVCVMQRGCIVEQASCEQLFRAPQHPYTREL 257
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
....*.
gi 1834229548 258 LAAEPS 263
Cdd:PLN03232 1469 HSTGPA 1474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-193 |
2.23e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.13 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 7 IEVRDLAVEFVVGERCqrVVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplarHPSGTIEYSGQNLLNLKEKT 86
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA--VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL------STEGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 87 IRHIRGNRIAMIFQEPMT---SLNPLHSIEKQ----INEVLGIhKGLIGKVATKRTLELLEMVGIpepekrlkalpheLS 159
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTfrkNLDPYEQWSDEeiwkVAEEVGL-KSVIEQFPDKLDFVLVDGGYV-------------LS 1355
|
170 180 190
....*....|....*....|....*....|....*
gi 1834229548 160 GGQRQRVMIAMALANEPELLIADEPTTALD-VTVQ 193
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-189 |
2.51e-04 |
|
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: 42.25 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLARH--PSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEPMTs 105
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCS----TLLKALANRTEGNvsVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 106 lnplhsiekqinevlgihkgligkvaTKRTLELlemvgipepekRLKALPHE----LSGGQRQRVMIAMALANEPELLIA 181
Cdd:cd03233 100 --------------------------VRETLDF-----------ALRCKGNEfvrgISGGERKRVSIAEALVSRASVLCW 142
|
....*...
gi 1834229548 182 DEPTTALD 189
Cdd:cd03233 143 DNSTRGLD 150
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-189 |
3.03e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 5 NLIEVRDLAVEFvvGERcqRVVEGVSFDIKRGETLALVGESGSGKSVtahsilrLLPYPLARHPSGtieYSgqNLLNL-- 82
Cdd:PRK10938 259 PRIVLNNGVVSY--NDR--PILHNLSWQVNPGEHWQIVGPNGAGKST-------LLSLITGDHPQG---YS--NDLTLfg 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 83 ----KEKTI----RHIrGNRIAMIFQEPMTSLNPLHSIEKQINEVLGIHKGLIGKvATKRTLELLEMVGIPepeKRLKAL 154
Cdd:PRK10938 323 rrrgSGETIwdikKHI-GYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDR-QQKLAQQWLDILGID---KRTADA 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 1834229548 155 P-HELSGGQRQRVMIAMALANEPELLIADEPTTALD 189
Cdd:PRK10938 398 PfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-230 |
3.44e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 21 RCQRVVEGVSFDikRGETLaLVGESGSGKSvtahSILRLLPYPLARH--PSGTIEYSGQNLLNLKEK------TIRHIRG 92
Cdd:cd03240 10 RSFHERSEIEFF--SPLTL-IVGQNGAGKT----TIIEALKYALTGElpPNSKGGAHDPKLIREGEVraqvklAFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 93 NRIAMIfqepmTSLNplhsiekQINEVLGIHKGLIGKVatkrtleLLEMVGipepekrlkalphELSGGQRQ------RV 166
Cdd:cd03240 83 KKYTIT-----RSLA-------ILENVIFCHQGESNWP-------LLDMRG-------------RCSGGEKVlasliiRL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 167 MIAMALANEPELLIADEPTTALD---VTVQLKILELLKELQArlGMALLLISHDLNLVKRIAHRVCV 230
Cdd:cd03240 131 ALAETFGSNCGILALDEPTTNLDeenIEESLAEIIEERKSQK--NFQLIVITHDEELVDAADHIYRV 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
158-248 |
3.49e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELQARlGMALLLISHDLNLVKRIaHRVCVMQRGCIV 237
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
90
....*....|.
gi 1834229548 238 EQASCEQLFRA 248
Cdd:PLN03232 819 EEGTFAELSKS 829
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
299-340 |
4.20e-04 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 41.96 E-value: 4.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1834229548 299 VKAVDGInFSLPQGQTLGIVGESGSGKSTLGLAILR----------LIGSKG 340
Cdd:pfam00006 2 IRAIDGL-LPIGRGQRIGIFGGSGVGKTVLAGMIARqasadvvvyaLIGERG 52
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
159-234 |
4.73e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.08 E-value: 4.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 159 SGGQRQRVMIAMALANEPELLIADEPTTALDVTVQLKILELLKELqARLGMALLLISHDLNLVKRIAHRVCVMQRG 234
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
426-463 |
5.95e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 5.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1834229548 426 SGGQRQRIAIARALVLKPALILLDEPTSALD--------RTVQRQV 463
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDaraaaivmRTVRNTV 1066
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-190 |
9.31e-04 |
|
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: 40.78 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSVTAHSILRLLpyplaRHPSGTIEYSGQNLLNLKEKTIRHIRGNRIAMIFQEPMTsLNP 108
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL-LNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 109 lhSIEKQIneVLGI------HKGLIGKVATKRTLELLEMVGIPEPEKRlkalPHELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:cd03290 94 --TVEENI--TFGSpfnkqrYKAVTDACSLQPDIDLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLD 165
|
....*...
gi 1834229548 183 EPTTALDV 190
Cdd:cd03290 166 DPFSALDI 173
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
299-472 |
9.60e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 299 VKAVDGINFSLPQGQTLGIVGESGSGKSTLglaiLRLI-GSK----GGIR-FEGKQLDSLTQQQVRPlrremQVVFQdPF 372
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIaGARkiqqGRVEvLGGDMADARHRRAVCP-----RIAYM-PQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 373 G-------SLSprmcvsqiVGEGLRIHkmGT-----EAEQEQAIIAALKEVGLDPeTRHRYPHEFSGGQRQRIAIARALV 440
Cdd:NF033858 84 GlgknlypTLS--------VFENLDFF--GRlfgqdAAERRRRIDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190
....*....|....*....|....*....|..
gi 1834229548 441 LKPALILLDEPTSALDRTVQRQVVELLRSLQS 472
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRA 184
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
128-190 |
1.36e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834229548 128 GKVATKRTLELLEMVGIPEPEKrlKALPHELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:PRK15064 128 GYTAEARAGELLLGVGIPEEQH--YGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
422-499 |
1.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 422 PHEFSGGQRQ------RIAIARALVLK-------PALILlDEPTSALDRTVQRQVVELLRSLQSKYNLTYLFISHDLAVV 488
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELV 857
|
90
....*....|.
gi 1834229548 489 KALSHQLMVVK 499
Cdd:PRK02224 858 GAADDLVRVEK 868
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
317-485 |
1.60e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 317 IVGESGSGKSTLGLAILRLIGSKGGIRfegkqlDSLTQQQVRPLRREMQVVF-----------------QDPFGSLSPRM 379
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYALYGKARSR------SKLRSDLINVGSEEASVELefehggkryrierrqgeFAEFLEAKPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 380 cVSQIVGEGLRIHKMG-------------TEAEQEQAIIAALKEVGLDPETRHRYPHEFSGGQRQRIAIARALVLkpali 446
Cdd:COG0419 102 -RKEALKRLLGLEIYEelkerlkeleealESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLLSL----- 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1834229548 447 LLDepTSALDRTVQRQVVELLRSLQskynltylFISHDL 485
Cdd:COG0419 176 ILD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
399-484 |
1.68e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 399 EQEQAIIA-ALKE----------VGLDPETRHRYPHEFSGGQRQRIAIARAL--VLKPALILLDEPTSALDRTVQRQVVE 465
Cdd:TIGR00630 452 PEEKKIAEeVLKEirerlgflidVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLIN 531
|
90
....*....|....*....
gi 1834229548 466 LLRSLQSKYNlTYLFISHD 484
Cdd:TIGR00630 532 TLKRLRDLGN-TLIVVEHD 549
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-294 |
1.94e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.08 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 28 GVSFDIKRGETLALVGESGSGKSvtahSILRLLPYPLAR-----HPSGTIEYSGQNLLnLKEKTIRHirgnriAMIFQEP 102
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKS----SLLSALLAEMDKveghvHMKGSVAYVPQQAW-IQNDSLRE------NILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 103 mtsLNPLHsiekqinevlgiHKGLIGKVATKRTLELLEmvGIPEPEKRLKALphELSGGQRQRVMIAMALANEPELLIAD 182
Cdd:TIGR00957 725 ---LNEKY------------YQQVLEACALLPDLEILP--SGDRTEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 183 EPTTALDVTVQLKILELLKELQARL-GMALLLISHDLNLVKRIaHRVCVMQRGCIVEQASCEQLFRAP--------QHPY 253
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDgafaeflrTYAP 864
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1834229548 254 TRELLAAEPSGTPATNVVGPPMLTVED-LKVWFPIKKGLLKK 294
Cdd:TIGR00957 865 DEQQGHLEDSWTALVSGEGKEAKLIENgMLVTDVVGKQLQRQ 906
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
426-526 |
2.23e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 426 SGGQRQRIAIARALVL---KPALILLDEPTSALDRTVQRQVVELLRSLQSKYNlTYLFISHDLAVVKalsHQLMVVKQGQ 502
Cdd:PRK00635 1701 SLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGH-SVIYIDHDPALLK---QADYLIEMGP 1776
|
90 100
....*....|....*....|....*
gi 1834229548 503 VVEQGDAQSIFAA-PQHPYTQQLLE 526
Cdd:PRK00635 1777 GSGKTGGKILFSGpPKDISASKDSL 1801
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
408-484 |
2.68e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 2.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834229548 408 LKEVGLdPETRHRYP-HEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLrslqSKYNLTYLFISHD 484
Cdd:PRK15064 139 LLGVGI-PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
157-190 |
2.76e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.76e-03
10 20 30
....*....|....*....|....*....|....
gi 1834229548 157 ELSGGQRQRVMIAMALANEPELLIADEPTTALDV 190
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-183 |
6.13e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.18 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 29 VSFDIKRGETLALVGESGSGKSVTAhsilRLLPyPLARHPSGTIEYSGQNLlnlKEKTIRHIRgNRIAMIFQEpmtslnp 108
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLA----MLLT-GLYQPQSGEILLDGKPV---TAEQPEDYR-KLFSAVFTD------- 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834229548 109 LHSIEKqineVLGIHKGLIGKVATKRTLELLEMVG-IPEPEKRLKALphELSGGQRQRVMIAMALANEPELLIADE 183
Cdd:PRK10522 406 FHLFDQ----LLGPEGKPANPALVEKWLERLKMAHkLELEDGRISNL--KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-245 |
6.67e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 25 VVEGVSFDIKRGETLALVGESGSGKSVTAHSILRLLPYPlarhpSGTIEYSGQNLLNLKEKTIRhirgNRIAMIFQEPMT 104
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDISKFGLMDLR----KVLGIIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834229548 105 -------SLNPLhsiekqiNEvlgiHKgligkvaTKRTLELLEMVGIPEPEKR----LKALPHE----LSGGQRQRVMIA 169
Cdd:PLN03130 1325 fsgtvrfNLDPF-------NE----HN-------DADLWESLERAHLKDVIRRnslgLDAEVSEagenFSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834229548 170 MALANEPELLIADEPTTALDVTVQLKILELLKELQARLGMalLLISHDLNLVkrI-AHRVCVMQRGCIVEQASCEQL 245
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENL 1459
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
158-192 |
6.84e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 6.84e-03
10 20 30
....*....|....*....|....*....|....*
gi 1834229548 158 LSGGQRQRVMIAMALANEPELLIADEPTTALDVTV 192
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
310-344 |
9.24e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 9.24e-03
10 20 30
....*....|....*....|....*....|....*
gi 1834229548 310 PQGQTLgIVGESGSGKSTLGLAILRLIGSKGGIRF 344
Cdd:pfam13555 21 PRGNTL-LTGPSGSGKSTLLDAIQTLLVPAKRARF 54
|
|
|